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Truncated hemoglobin HbN protects Mycobacterium bovis from nitric oxide
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Characterization of a glutathione metabolic mutant of Mycobacterium tuberculosis and its resistance to glutathione and nitrosoglutathione
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Multiple thioredoxin-mediated routes to detoxify hydroperoxides in Mycobacterium tuberculosis
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Drug targets in mycobacterial sulfur metabolism
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FUNCTION: In its thiocarboxylated form (CysO-COSH), is the sulfur donor in the CysM-dependent cysteine biosynthetic pathway. May be of particular importance for cysteine biosynthesis in the persistent phase of M.tuberculosis.
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Iron storage proteins are essential for the survival and pathogenesis of Mycobacterium tuberculosis in THP-1 macrophages and the guinea pig model of infection
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FUNCTION: Catalyzes the formation of a covalent CysO-cysteine adduct via a sulfur transfer, using the thiocarboxylated sulfur carrier protein CysO-COSH as sulfur donor and O-phospho-L-serine (OPS) as sulfur acceptor. Can also use sodium sulfide as sulfur donor in vitro, albeit with less efficiency, but not thiosulfate or thio-nitro-benzoate. O-acetylserine (OAS) is a very poor substrate in comparison with OPS. May be of particular importance for cysteine biosynthesis in the persistent phase of M.tuberculosis.
Rv2131c from Mycobacterium tuberculosis is a CysQ 3'-phosphoadenosine-5'-phosphatase
carboxymycobactin (loaded) [ChEBI:47333]
FUNCTION: Catalyzes the conversion of O-acetylserine (OAS) to cysteine through the elimination of acetate and addition of hydrogen sulfide.
Reconstitution of a new cysteine biosynthetic pathway in Mycobacterium tuberculosis
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Cysteine synthase (CysM) of Mycobacterium tuberculosis is an O-phosphoserine sulfhydrylase: evidence for an alternative cysteine biosynthesis pathway in mycobacteria
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Identification of the INO1 gene of Mycobacterium tuberculosis H37Rv reveals a novel class of inositol-1-phosphate synthase enzyme
Genetic analysis of superoxide dismutase, the 23 kilodalton antigen of Mycobacterium tuberculosis
FUNCTION: Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation (By similarity).
FUNCTION: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA (By similarity).
FUNCTION: The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently (By similarity).
FUNCTION: Involved in protein export. Participates in an early event of protein translocation (By similarity).
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FUNCTION: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of precursor proteins, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane (By similarity).
Three pathways for trehalose biosynthesis in mycobacteria
FUNCTION: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane (By similarity).
ChEBI:59629 N-ethylsuccinimide-mycothiol conjugate
Antimicrobial reactive oxygen and nitrogen species: concepts and controversies
Biosynthesis of mycothiol starts from glucose-6-phosphate and proceeds directly to myo-inositol-1-phosphate, contrary to phosphatidylinositol synthesis. One of the following steps, the removal of the phosphate group, is catalyzed by a still unknown phosphatase. The pathway is essential in M. tuberculosis (Newton et al, 2006; Sareen et al., 2003)
Unique features of the sodC-encoded superoxide dismutase from Mycobacterium tuberculosis, a fully functional copper-containing enzyme lacking zinc in the active site
Cloning and overexpression in soluble form of functional shikimate kinase and 5-enolpyruvylshikimate 3-phosphate synthase enzymes from Mycobacterium tuberculosis
Characterization of Mycobacterium tuberculosis mycothiol S-conjugate amidase
FUNCTION: Catalyzes the NAD(P)H-dependent reduction of mycothione (the oxidized disulfide form of mycothiol) to mycothiol.
CATALYTIC ACTIVITY: Thioredoxin + NADP(+) = thioredoxin disulfide + NADPH.
The Mycobacterium tuberculosis ino1 gene is essential for growth and virulence
FUNCTION: Lipoamide dehydrogenase is an essential component of the alpha-ketoacid dehydrogenase complexes, namely the pyruvate dehydrogenase (PDH) complex, the branched-chain alpha-ketoacid dehydrogenase (BCKADH) complex, and likely also the 2-oxoglutarate dehydrogenase (ODH) complex. Catalyzes the reoxidation of dihydrolipoyl groups which are covalently attached to the lipoate acyltransferase components (E2) of the complexes. Is also able to catalyze the transhydrogenation of NADH and thio-NAD(+) in the absence of D,L-lipoamide, and the NADH-dependent reduction of quinones in vitro.
ChEBI:59632 (2R)-2-acetamido-3-phenacylsulfanylpropanoic acid
(2R)-2-acetamido-3-phenacylsulfanylpropanoic acid
ChEBI:59634 3-(1-ethyl-2,5-dioxopyrrolidin-3-yl)sulfanylpropanoic acid
3-(1-ethyl-2,5-dioxopyrrolidin-3-yl)sulfanylpropanoic acid
ChEBI:59630 acetophenone-mycothiol conjugate
DAHP synthase from Mycobacterium tuberculosis H37Rv: cloning, expression, and purification of functional enzyme
The challenge of new drug discovery for tuberculosis
Functional shikimate dehydrogenase from Mycobacterium tuberculosis H37Rv: purification and characterization
UDP-N-acetyl-D-glucosamine [ChEBI:16264]
The ferritins: molecular properties, iron storage function and cellular regulation
Functional analysis of L-serine O-acetyltransferase from Corynebacterium glutamicum
Metabolic enzymes of mycobacteria linked to antioxidant defense by a thioredoxin-like protein
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Thiol and sulfenic acid oxidation of AhpE, the one-cysteine peroxiredoxin from Mycobacterium tuberculosis: kinetics, acidity constants, and conformational dynamics
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Innate protection of Mycobacterium smegmatis against the antimicrobial activity of nitric oxide is provided by mycothiol
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Mycobacterium tuberculosis expresses methionine sulphoxide reductases A and B that protect from killing by nitrite and hypochlorite
O-phospho-L-serine and the thiocarboxylated sulfur carrier protein CysO-COSH are substrates for CysM, a cysteine synthase from Mycobacterium tuberculosis
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Siderophore-based iron acquisition and pathogen control
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Functional and structural characterization of a thiol peroxidase from Mycobacterium tuberculosis
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The OtsAB pathway is essential for trehalose biosynthesis in Mycobacterium tuberculosis
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CATALYTIC ACTIVITY Preferential at -Arg-Ser-Arg-Arg-|- and -Arg-Arg-Ser-Arg-|-, and of Z-Phe-Arg-|-aminomethylcoumarin.PTM Poly-N-acetyllactosaminic carbohydrate moiety seems to be needed for TLR4 activation.POLYMORPHISM The sequence shown corresponds to the reference genome sequence and is likely to represent the minor allele, whereas most publications refer to the longer sequence containing variant Arg-22 ins. Insertion of the additional arginine in variant Arg-22 ins creates an N-terminal basic cluster of four arginines, all of which appear to be important for the full functionality of the protein, including bactericidal and antifungal activities as well as binding to glycosaminoglycans, pspA, LPS, lysozyme and DNA.SIMILARITY Belongs to the transferrin family.SIMILARITY Contains 2 transferrin-like domains.
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FUNCTION: ATP sulfurylase may be the GTPase, regulating ATP sulfurylase activity (By similarity).
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ChEBI:57701 5-enolpyruvyl shikimate-3-phosphate
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Structural enzymology of sulphur metabolism in Mycobacterium tuberculosis
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5'-adenosinephosphosulfate lies at a metabolic branch point in mycobacteria
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Uptake of sulfur in Mycobacterium tuberculosis happens exclusively through sulfate assimiliation, an abundant molecule in the bacterium's environment. All enzymes participating in this process are non-redundant ie they are essential enzymes. Sulfate is first taken up via an ABC transporter and appended to AMP giving APS and PAPS, which can be considered the activated forms of sulfate and are used in cysteine and sulfolipid biosynthesis (Bhave et al, 2007).
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FUNCTION: Protease that hydrolyzes the covalent CysO-cysteine adduct synthesized by CysM to release L-cysteine and regenerate CysO.
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Mycothiol and its adducts that result from detoxification can be readily cleaved into smaller molecules. The mycothiol pool therefore serves as storage for unstable cysteine and sugars. (Rawat and Av-Gay, 2007; Newton et al, 2008)
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Purification and characterization of recombinant catalase-peroxidase, which confers isoniazid sensitivity in Mycobacterium tuberculosis
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In stress situations, Mycobacteria express enzymes for a second pathway that enables cysteine synthesis from serine pathway products, here from phosphoserine. The details of the sulfur donor are not established (Agren et al, 2008).
Characterization of the Mycobacterium tuberculosis H37Rv alkyl hydroperoxidase AhpC points to the importance of ionic interactions in oligomerization and activity
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Structure and mechanism of the alkyl hydroperoxidase AhpC, a key element of the Mycobacterium tuberculosis defense system against oxidative stress
glucosaminyl-inositol and cysteine are ligated to desacetylmycothiol
Ligation of glucosamine-inositol with the amino acid cysteine is zinc-dependent. The catalyzing enzyme MshC is a homologue of Cys-tRNA synthetase (Sareen et al, 2002)
desacetylmycothiol is acetylated to mycothiol using acetyl-CoA
The final step to yield mycothiol is an acetylation using acetyl-CoA. Compounds with other acyl groups can be produced spontaneously without the MshD enzyme and can have mycothiol activity. This explains low levels of mycothiol-like activity and traces of formyl- and succinyl-Cys-GlcN-Ins in MshD null mutants (Koledin et al, 2002)
acetylglucosamine-inositol is deacetylated by Mca
A small part of deacetylase activity required in the step producing glucosaminylinositol comes from the mycothiol S-conjugate amidase Mca. The hydrolaswe also needs zinc for its activity (Steffek et al, 2003).
mycothiol is cleaved to acetylcysteine and glucosaminylinositol
The degradation of mycothiol proceeds through its cleavage into acetylcysteine and glucosaminylinositol which both are completely degradable further. (Steffek et al, 2003)
glucose-6-phosphate is converted to inositol-1-phosphate
M. tuberculosis utilizes myo-inositol-1-phosphate for mycothiol biosynthesis. This substrate comes nearly exclusively from the conversion of glucose-6-phosphate by Ino1. However, mutants devoid of Ino1 still have minimal amounts of mycothiol, so another reaction appears to provide Ins-P in small amounts, most likely the phosphorylation of uptaken inositol (Bachhawat and Mande, 1999; Mohavedzadeh et al, 2004; Newton et al, 2006; Newton et al, 2008).
acetylglucosamine is transferred from UDP-GlcNAc onto inositol-1-phosphate
MshA catalyzes the transfer of acetylglucosamine from UDP-GlcNAc onto inositol-1-phosphate. From biochemical and crystal studies, there is an absolute requirement for the phosphate as substrate (Newton et al, 2006; Vetting, 2008).
acetylglucosamine-inositol-phosphate is dephosphorylated
The enzyme to catalyze dephosphorylation of Glc-NAc-Ins-P is still unknown. Several candidate phosphatases have been characterized. The most likely is Rv3137 which was shown to be essential in M. tuberculosis (Newton et al, 2006; Movahedzadeh, 2010)
mycothiol conjugates with electrophilic xenobiotic
Although mycothiol is able to conjugate by itself with electrophilic substances, analogously to glutathione in eukaryotes, it is possible there are specific MSH transferases for the catalysis of this reaction in cases where the substrate is more inert (Rawat and Av-Gay, 2007).
mycothiol S-conjugate is cleaved into mercapturic acid and GlcN-Ins
The hydrolysis of the mycothiol S-conjugate, catalyzed by the Mca amidase, results in a so called mercapturic acid (acetylcysteine adduct) of the toxin, and glucosaminyl-inositol which is recycled to mycothiol (Steffek et al, 2003).
Mycobacterium tuberculosis and the intimate discourse of a chronic infection
alpha,alpha'-Trehalose 6-phosphate [ChEBI:10201]
Mycothiol-dependent proteins in actinomycetes
N-Acetyl-1-D-myo-inosityl-2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase (MshB) is a key enzyme in mycothiol biosynthesis
ChEBI:52442 1-O-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol
The many niches and strategies used by pathogenic mycobacteria for survival within host macrophages
ChEBI:52443 GlcNAc-(alpha1,1)-1D-Ins-3-P
Biosynthesis and functions of mycothiol, the unique protective thiol of Actinobacteria
Inducible overproduction of the Aspergillus nidulans pentafunctional AROM protein and the type-I and -II 3-dehydroquinases from Salmonella typhi and Mycobacterium tuberculosis
Unique small sulfur compounds, as well as unique pathways to sulfur amino acids are known in Mycobacteria. Sulfoglycolipids and mycothiols are an important part of the hardy pathogen nature of these organisms. Their pathways make interesting targets for drug designers (Bhave et al, 2007).
Identification of the mycothiol synthase gene (mshD) encoding the acetyltransferase producing mycothiol in actinomycetes
Cloning and expression of the trehalose-phosphate phosphatase of Mycobacterium tuberculosis: comparison to the enzyme from Mycobacterium smegmatis
A conserved mechanism for sulfonucleotide reduction
CATALYTIC ACTIVITY: ATP + sulfate = diphosphate + adenylyl sulfate.
FUNCTION: Reduction of activated sulfate into sulfite (By similarity).
FUNCTION: Part of a binding-protein-dependent transport system. Probably responsible for the translocation of the substrate across the membrane (By similarity).
Functional characterization by genetic complementation of aroB-encoded dehydroquinate synthase from Mycobacterium tuberculosis H37Rv and its heterologous expression and purification
Tolerance by Mtb to nitric oxide produced by macrophages
Reactive nitrogen species (RNS), like reactive oxygen species, have numerous target molecules in the bacterial cell, and Mtb has developed remedies to the most important ones of them. This is a key reason for its ability to stay alive in the hostile environment of the late phagosome within human macrophages. Mtb repairs single-base DNA damage caused by DNA alkylation; it scavenges nitric oxide with large amounts of mycothiol and methionine-rich proteins (the nitroso compounds later being reduced). Nitric oxide and peroxynitrite are also directly reduced by a battery of hemoglobins and peroxiredoxins, supported by a network of thioredoxins and respective NADPH-dependent reductases (Fang. 2004).
FUNCTION: Binds oxygen cooperatively with very high affinity (P(50) = 0.013 mmHg at 20 degrees Celsius) because of a fast combination (25 microM(-1).s(-1)) and a slow dissociation (0.2 s(- 1)) rate.
FUNCTION: Catalyzes the transfer of glucose from a nucleoside diphosphate-glucose to glucose-6-phosphate to form trehalose-6- phosphate and nucleoside diphosphate. TPS is specific for the glucosyl acceptor but not for the glucosyl donor. Most active with the purine sugar nucleotides than the pyrimidine sugar nucleotides.
The cysteine biosynthetic pathway using the intermediate O-acetylserine is well preserved among bacteria, and it is also the main pathway in M. tuberculosis in normal medium. It depends on a six electron reduction of sulfite to sulfide (Bhave et al, 2007; Pinto et al, 2007).
CATALYTIC ACTIVITY: Hydrogen sulfide + 6 oxidized ferredoxin + 3 H(2)O = sulfite + 6 reduced ferredoxin + 6 H(+).
FUNCTION: Catalyzes the conversion of the sulfur carrier protein CysO to CysO-thiocarboxylate. The reaction is thought to proceed in two steps: first, ATP-dependent activation of CysO as acyl- adenylate (CysO-COOAMP), followed by sulfur transfer to give CysO- thiocarboxylate (CysO-COSH) (Probable). The sulfur source is unknown.
Mycothiol (MSH), a conjugate of glucosamine, cysteine and inositol, is the Actinobacteria equivalent of glutathione. It serves as a pool for both the unstable cysteine and reduction equivalents. Mycothiol takes part in enzymatic reactions including detoxification of electrophilic compounds, inactivation of reactive oxygen and nitrogen species, reductions, and isomerizations. M. smegmatis mutants devoid of MSH are sensitive to oxidative and nitrosative stress, and antibiotics. In M. tuberculosis, however, mycothiol synthesis is essential, no null mutants are known. Results from MshD mutants, which have about 1 per cent of MSH, show the importance of mycothiol in environments where antimicrobial factors, including reactive oxygen and reactive nitrogen intermediates, are formed, such as within macrophages (Newton et al, 2008; Rawat and Av-Gay, 2007)
FUNCTION: Catalyzes the coenzyme F420-dependent oxidation of glucose 6-phosphate to 6-phosphogluconolactone. Is essential for the bioreductive activation of the prodrug PA-824 (nitroimidazo- oxazine) developed for anti-tuberculosis therapy against both replicating and persistent bacteria. It does not interact directly with PA-824 but, rather, provides reduced F420 to an accessory protein (Rv3547), which in turn activates PA-824. Also probably has a role in resistance to oxidative stress, via its consumption of G6P that serves as a source of reducing power to combat oxidative stress in mycobacteria.
FUNCTION: Iron-storage protein that displays ferroxidase activity, catalyzing the oxidation of Fe(2+) ions into Fe(3+) ions, that can then be deposited as a ferric-oxide mineral core within the central cavity of the protein complex.
FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions (By similarity).
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CATALYTIC ACTIVITY L-histidinol phosphate + H(2)O = L-histidinol + phosphate.PATHWAY Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.SIMILARITY Belongs to the inositol monophosphatase family.
Functional demonstration of reverse transsulfuration in the Mycobacterium tuberculosis complex reveals that methionine is the preferred sulfur source for pathogenic Mycobacteria
FUNCTION: Catalyzes the transfer of a N-acetyl-glucosamine moiety to 1D-myo-inositol 3-phosphate to produce 1D-myo-inositol 2- acetamido-2-deoxy-glucopyranoside 3-phosphate in the mycothiol biosynthesis pathway.
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No cysteine auxotrophs of Mycobacterium tuberculosis are known. This suggests redundant pathways for sulfur uptake and cysteine biosynthesis. Indeed, there is full interconversion between taken up sulfate/sulfide, cysteine, and methionine via cystathionine. (Schnell and Schneider, 2010)
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Biochemistry of the initial steps of mycothiol biosynthesis
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Effect of trehalose on protein structure
CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
FUNCTION: Bifunctional enzyme with both catalase and broad- spectrum peroxidase activity. Displays also NADH oxidase, isoniazid (INH) lyase and isonicotinoyl-NAD synthase activity. May play a role in the intracellular survival of mycobacteria. May be involved in DNA repair. Partly complements recA-deficient E.coli cells exposed to UV radiation, mitomycin C or hydrogen peroxide. Increases resistance to mitomycin C in E.coli cells deficient for either uvrA, uvrB or uvrC.
Trehalose-phosphate synthase of Mycobacterium tuberculosis. Cloning, expression and properties of the recombinant enzyme
MISCELLANEOUS Was identified as a high-confidence drug target.SIMILARITY Belongs to the cysteine synthase/cystathionine beta-synthase family.
The metabolism of nitrosothiols in the Mycobacteria: identification and characterization of S-nitrosomycothiol reductase
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alpha-D-Glucose 6-phosphate [ChEBI:17665]
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Inositol monophosphate phosphatase genes of Mycobacterium tuberculosis
Mechanistic insights into a novel exporter-importer system of Mycobacterium tuberculosis unravel its role in trafficking of iron
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The shikimate pathway leads to the biosynthesis of chorismate, which, in mycobacteria, is a precursor of aromatic amino acids, naphthoquinones, menaquinones and siderophores. The enzymes of this pathway are attractive pharmaceutical targets, as the pathway is absent from mammals, and there are no redundancies in it (Herrmann and Weaver, 1999).
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The crucial role of trehalose and structurally related oligosaccharides in the biosynthesis and transfer of mycolic acids in Corynebacterineae
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Peptide methionine sulfoxide reductase from Escherichia coli and Mycobacterium tuberculosis protects bacteria against oxidative damage from reactive nitrogen intermediates
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The thiol-based redox networks of pathogens: unexploited targets in the search for new drugs
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FUNCTION: Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
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Ferritin structure from Mycobacterium tuberculosis: comparative study with homologues identifies extended C-terminus involved in ferroxidase activity
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The non-reducing disaccharide trehalose is found in insects, plants, and microorganisms. In bacteria, it is a storage energy source and is essential for the survival of many stress conditions. In mycobacteria, trehalose is also part of the cell wall and of the 'cord factor' which is important for entry into the host (Elbein et al, 2003; Tropis et al, 2005; Jain & Roy, 2009) M. tuberculosis has three ways to synthesize trehalose: from UDP-glucose and glucose phosphate (the OtsAB pathway), from maltose (the TreS pathway), and from glycogen (TreYZ pathway). The OtsAB pathway was shown to be essential for the organism. It is not known, however, whether or not the essentiality of trehalose for the mycobacterial growth is directly connected to the biosynthesis of cell wall mycolates (De Smet et al, 2000; Murphy et al, 2005)
The most important response of Mtb to oxidative stress is provided by catalase and peroxiredoxins, both of which get their reducing equivalents through a network of disulfide proteins and, finally, from NAD(P)H. Multiple redundancies make choosing a good drug target difficult (Koul et al. 2011). Optimum efficacy can only be expected from inhibitors of the most upstream components of the redox cascades, i.e. the NAD(P)H-dependent reductases TrxB and Lpd (Jaeger & Flohe 2006).
Re-annotation of the genome sequence of Mycobacterium tuberculosis H37Rv
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SecA2 functions in the secretion of superoxide dismutase A and in the virulence of Mycobacterium tuberculosis
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Tolerance of reactive oxygen produced by macrophages
The expression of AhpC in Mycobacteria does not correlate with virulence; instead, the most important parts of the antioxidant system in Mtb appear to be the lipid cell wall, the enzymes SodB/SodC (superoxide dismutases), and the catalase/peroxidase KatG. Together with the enzyme system that acts on nitrosative stress and the sequestration of iron, these appear to be critical in defending against the macrophage's production of ROS/RNS, and enable the bacterium to exist in the phagosome for extended periods (Zahrt & Deretic 2002).
Mtb encounters a vastly changed environment, soon after it gets internalized by macrophages. The compartment it resides in, the phagosome, is acidified and devoid of important metal ions. It is flooded with reactive oxygen and nitrogen species. And steps will be soon taken by the macrophage to "mature" the phagosome with all kinds of lysosomal digestive enzymes. However, unlike most other bacteria species Mtb. has evolved solutions to each of these threats and, after making sure these are installed, it soon will enter a dormant state (de Chastellier, 2009; Flannagan et al, 2009). A combination of the host defense and the response of the infecting bacillus (active and passive) ensure suppression of bacterial metabolic activity and replication, resulting in a non-replicating state (Russell 2011, Russell et al. 2010).
Functional genomics reveals the sole sulphate transporter of the Mycobacterium tuberculosis complex and its relevance to the acquisition of sulphur in vivo
ATP-dependent L-cysteine:1D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase, mycothiol biosynthesis enzyme MshC, is related to class I cysteinyl-tRNA synthetases
In analogy to glutathione, mycothiol is part of the detoxification machinery of the M. tuberculosis cell. The biotransformation of electrophilic toxins consists of creating an adduct with mycothiol, its cleavage into a "mercapturic acid" and glucosaminyl-inositol (with which mycothiol is recycled), and transport of the mercapturic acid through the membrane. The protein(s) catalyzing the transport are still unidentified. Further molecules that are changed to less dangerous entities with the help of mycothiol are formaldehyde and the nitrosyl radical (Rawat and Av-Gay, 2007; Newton et al, 2008).
Reactive oxygen and nitrogen intermediates in the relationship between mammalian hosts and microbial pathogens
Annu Rev Plant Physiol Plant Mol Biol 50:473-503
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Expression, purification, and characterization of Mycobacterium tuberculosis mycothione reductase
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New drugs and regimens for treatment of TB
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3,4,5-Trihydroxy-1-cyclohexenecarboxylic acid
Structural insights into catalysis and inhibition of O-acetylserine sulfhydrylase from Mycobacterium tuberculosis. Crystal structures of the enzyme alpha-aminoacrylate intermediate and an enzyme-inhibitor complex
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adenosine 5'-monophosphate [ChEBI:16027]
D-Glucono-1,5-lactone 6-phosphate [ChEBI:16938]
ChEBI:58394 (4R,5S,6R)-4,5,6-trihydroxy-2-oxo-7-(phosphonatooxy)heptanoate(3-)
FUNCTION: Antioxidant protein with alkyl hydroperoxidase activity. Required for the reduction of the AhpC active site cysteine residues and for the regeneration of the AhpC enzyme activity.
FUNCTION: Together with AhpD, DlaT and Lpd, constitutes an NADH- dependent peroxidase active against hydrogen and alkyl peroxides as well as serving as a peroxynitrite reductase, thus protecting the bacterium against reactive nitrogen intermediates and oxidative stress generated by the host immune system. Does not however seem to play a role in detoxification of isoniazid.
Structural and enzymatic analysis of MshA from Corynebacterium glutamicum: substrate-assisted catalysis
The Mycobacterium tuberculosis cysD and cysNC genes form a stress-induced operon that encodes a tri-functional sulfate-activating complex
Siroheme- and [Fe4-S4]-dependent NirA from Mycobacterium tuberculosis is a sulfite reductase with a covalent Cys-Tyr bond in the active site
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Crystal structure of inositol 1-phosphate synthase from Mycobacterium tuberculosis, a key enzyme in phosphatidylinositol synthesis
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Antimicrobial mechanisms of phagocytes and bacterial evasion strategies
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FUNCTION: Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.
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FUNCTION: Catalyzes the ATP-dependent condensation of GlcN-Ins and L-cysteine to form L-Cys-GlcN-Ins.
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ChEBI:61088 S-nitroso-L-cysteinylglycine
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FUNCTION: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine (By similarity).
FUNCTION: Part of the ABC transporter complex IrtAB involved in iron import. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation. Required for replication in human macrophages and in mouse lungs.
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CATALYTIC ACTIVITY Acetyl-CoA + L-serine = CoA + O-acetyl-L-serine.PATHWAY Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 1/2.MISCELLANEOUS Was identified as a high-confidence drug target.SIMILARITY Belongs to the transferase hexapeptide repeat family.
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FUNCTION: Part of the ABC transporter complex CysAWTP involved in sulfate/thiosulfate import. Responsible for energy coupling to the transport system.
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The crystal structure of 1-D-myo-inosityl 2-acetamido-2-deoxy-alpha-D-glucopyranoside deacetylase (MshB) from Mycobacterium tuberculosis reveals a zinc hydrolase with a lactate dehydrogenase fold
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Identification and subcellular localization of a novel Cu,Zn superoxide dismutase of Mycobacterium tuberculosis
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One- and two-electron oxidations of methionine by peroxynitrite
The trifunctional sulfate-activating complex (SAC) of Mycobacterium tuberculosis
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FUNCTION: Removes the phosphate from trehalose 6-phosphate to produce free trehalose.
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Mycobacterium tuberculosis biological processes
Mycobacterium tuberculosis H37Rv is the laboratory strain most widely used of the pathogen M. tuberculosis, an actinobacterium that carries many properties of its family to the extreme. It is not only interesting as one of the top three bacterial killers, with one third of the world having a dormant infection, but also as a model for other mycobacteria regarding the processes of slow growing, dormancy, host interaction, very long chain fatty acid biosynthesis, outer cell wall assembly, as well as sulfolipid, siderophore, and mycothiol biosynthesis. M. tuberculosis produces mycolic and phthioceranic acids, the fatty acids with the longest carbon atom chains known. With up to 20 hours, it has the longest reproduction time in mycobacteria. In human macrophages in dormant state, it spends decades without reproduction. Consequently, to fully investigate these properties new methods will have to be invented. While the treatment of an M. tuberculosis infection appears standard in Western countries, it still involves six months of a regime of three antibiotics that have been known for a long time. Not unexpectedly, acceptance and adherence to such a prolonged therapy are less than desired, and this contributes to spontaneous resistance from an already higher than average mutation rate of M. tuberculosis due to replication errors. Fueled by the HIV advance, strains of this bacterium are on the rise with resistance to all used antibiotics. For this reason, M. tuberculosis is the testbed of new antibiotics development, and it offers the opportunity of many unique and essential biochemical pathways. (Camus et al. 2002; Leibert and Rom, 2010)
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Virulence of Mycobacterium tuberculosis depends on lipoamide dehydrogenase, a member of three multienzyme complexes
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FUNCTION: Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex (By similarity).
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FUNCTION: Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions (By similarity).
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Functional genomics reveals extended roles of the Mycobacterium tuberculosis stress response factor sigmaH
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Lipidomic discovery of deoxysiderophores reveals a revised mycobactin biosynthesis pathway in Mycobacterium tuberculosis
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FUNCTION: Catalyzes the reversible interconversion of maltose and trehalose by transglucosylation. Also displays amylase activity, catalyzing the endohydrolysis of (1->4)-alpha-D-glucosidic linkages in glycogen and maltooligosaccharides such as maltoheptaose, to produce maltose which then can be converted to trehalose. TreS probably plays a key role in the utilization of trehalose for the production of glycogen, and might also function as a sensor and/or regulator of trehalose levels within the cell. Thus, when trehalose levels in the cell become dangerously low, TreS could expedite the conversion of glycogen to maltose via its amylase activity and then convert the maltose to trehalose; but this enzyme also could expedite or promote the conversion of trehalose to glycogen when cytoplasmic trehalose levels become too high.
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FUNCTION: Catalyzes the conversion of maltooligosaccharide into the non-reducing saccharide, maltooligosyl trehalose (alpha- maltooligosyl alpha-D-glucoside) by intramolecular transglycosylation (By similarity).
FUNCTION: Is involved in the biosynthesis of trehalose but not in that of capsular glucan and glycogen.
FUNCTION: Has antioxidant activity. Could remove peroxides or H(2)O(2) (By similarity).
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beta-Nicotinamide adenine dinucleotide phosphate
Nicotinamide adenine dinucleotide phosphate
CATALYTIC ACTIVITY Phosphoenolpyruvate + D-erythrose 4-phosphate + H(2)O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate.PATHWAY Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7.SIMILARITY Belongs to the class-II DAHP synthase family.
FUNCTION: Catalyzes a trans-dehydration via an enolate intermediate (By similarity).
CATALYTIC ACTIVITY: 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate = 3-dehydroquinate + phosphate.
FUNCTION: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
CATALYTIC ACTIVITY: 5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate.
3'-Phosphoadenylyl sulfate [ChEBI:17980]
CATALYTIC ACTIVITY: Phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate.
Electrophilic substrate-mycothiol conjugate
Electrophilic substance-mercapturic acid
mycothiol binds formaldehyde and is dehydrogenated
In the detoxification of formaldehyde, mycothiol first binds to the molecule forming a hydroxymethyl adduct intermediate (M-S-CH2OH, not shown), which is dehydrogenated by the bifunctional MscR enzyme to formylmycothiol (Vogt et al, 2003).
1,4-alpha-glucan is converted to glucanotrehalose
Linear alpha-1,4-glucans are modified at one end to a glucanotrehalose by the enzyme TreY (De Smet et al, 2000).
Glucanotrehalose is hydrolyzed to 1,4-alpha-glucan and trehalose
From the glucanotrehalose, the enzyme TreZ cleaves one molecule of trehalose, leaving a linear glucan that is two sugars shorter than before. This is the rate-limiting step in the TreYZ pathway of trehalose biosynthesis (De Smet et al, 2000).
Trehalose-6-phosphate is hydrolyzed to trehalose
Hydrolysis of trehalose phosphate, catalyzed by OtsB2, gives trehalose. The enzyme needs magnesium for its activity. A second homologue, OtsB1 is non-functional (De Smet et al, 2000; Edavana et al, 2004).
Maltose is converted to trehalose. The enzymatic activity of TreS for this reaction is 2-5 fold stronger than for the reverse reaction (De Smet et al, 2000).
Mycothiol is recycled using a reduction equivalent (NADPH/H+) and the help of the mycothione reductase enzyme. Although a mtr null mutant was obtained by McAdam and coworkers in M. tuberculosis, another study by Sassetti suggests the enzyme is essential in the H37Rv strain. It appears possible that thioredoxin reductases can provide some enzymatic rest activity. (Patel and Blanchard, 1999; Rawat and Av-Gay, 2007)
Glucose is transferred from UDP-glucose onto glucose-6-phosphate
Trehalose phosphate synthase, which is a tetramer in solution, catalyzes the transfer of glucose from UDP onto glucose-6-phosphate. The enzyme is stimulated by manganese ions and can also accept ADP-, CDP-, GDP- and TDP-glucose as well as UDP-glucose (De Smet et al, 2000; Pan et al, 2008).
formylmycothiol hydrolyzes into mycothiol and formate
Formylmycothiol, like any S-formyl ester, is unstable and quickly hydrolyzes into mycothiol and formate (Vogt et al, 2003).
The oxidation of mycothiol provides electrons for the maintenance of cell redox homeostasis. In which reactions exactly those electrons are used is unknown. A possibility is the existence of MSH-dependent peroxidases. (Rawat and Av-Gay, 2007)
sulfate binds to SubI outside the membrane
The sulfate binding protein is localized in the plasma membrane using a lipid anchor. It is associated with the ATP sulfate influx pump and binds sulfate and probably also thiosulfate anions from the extracellular space (Wooff et al, 2002).
Sufate is first activated by adding it to ATP, giving APS. Although both sulfate adenylyltransferase and APS kinase activities reside in the same enzyme complex, the intermediate APS is not channeled within the complex. Its accessibility ensures the functionality of the cysteine biosynthetic pathway (Pinto et al, 2004; Sun et al, 2005).
The sulfate transporter of M. tuberculosis, a typical ABC transporter family ATPase, is the sole membrane transport protein in sulfate assimilation. It consists of the CysT/CysW/CysA proteins in 1:1:2 stoichiometry. cysA null mutants in M. bovis were unable to take up sulfate but could be rescued by M. tuberculosis cysA (Wooff et al, 2002).
Although there is no direct evidence for CysE catalyzing the acetylation of serine, it has 58% identity with the serine acetyltransferase of Corynebacterium glutamicum and is upregulated in stress conditions (Haitani et al, 2006; Schnell et al, 2007; Mehra and Kaushal, 2009).
deacetylation of O-acetylserine and sulfhydrylation using CysK1
Sulfhydrylation of O-acetylserine (OAS) is a four step process, as was shown with CysK1, consisting of 1) addition of OAS to pyridoxal phosphate, 2) deacetylation, 3) sulfhydrylation and 4) cleavage of cysteine. It remains to be shown that the enzyme binds to CysE, resulting in a bifunctional complex. Activity of CysK1 is not essential for M. tuberculosis (Schnell et al, 2007).
deacetylation of O-acetylserine and sulfhydrylation using CysK2
Expression of the other enzyme catalyzing the sulfhydrylation of O-acetylserine, CysK2, is increased by oxidative stress (Mehra and Kaushal, 2009; Schnell et al, 2007).
MoeZ appears to catalyze the transfer of sulfur (here sulfide) onto the sulfur carrier protein CysO where the C-terminus carboxyl group becomes a thiocarboxyl group. The small molecule substrate, as well as the exact enzymatic activity of MoeZ, is unknown (Burns et al, 2005).
Energy for the phosphorylation of APS comes from the hydrolysis of a GTP molecule. The resulting PAPS is used in M. tuberculosis by several sulfotransferases for the production of sulfolipids (Pinto et al, 2004; Sun et al, 2005).
PAPS dephosphorylation, as the reverse reaction to APS phosphorylation, may have a regulatory role in the sulfate metabolism of M. tuberculosis (Hatzios et al, 2008).
Reduction and cleavage of the sulfate moiety of APS happens in two distinct steps. First, the C-terminal cysteine of CysH binds sulfite to form an enzyme-thiosulfonate intermediate, which is then reduced by a thioredoxin (donating two electrons, thereby freeing two protons) (Williams et al, 2002; Carroll et al, 2005).
Three molecules of reduced ferredoxin are needed to reduce sulfite to sulfide. Electrons are transferred to sulfite with the help of Sir, an enzyme with siroheme and an iron-sulfur cluster as cofactors (Schnell et al, 2005; Pinto et al, 2007).
The Mycobacterium tuberculosis high-affinity iron importer, IrtA, contains an FAD-binding domain
FUNCTION: Phosphatase with a broad specificity. Its primary physiological function is to dephosphorylate 3'-phosphoadenosine 5'-phosphate (PAP) and 3'-phosphoadenosine 5'-phosphosulfate (PAPS). Thus, plays a role in mycobacterial sulfur metabolism, since it can serve as a key regulator of the sulfate assimilation pathway by controlling the pools of PAP and PAPS in the cell. To a lesser extent, is also able to hydrolyze inositol 1-phosphate (I- 1-P), fructose 1,6-bisphosphate (FBP) (to fructose 6-phosphate (F- 6-P)) and AMP in vitro, but this might has no significance in vivo. Glucose-1-phosphate (G-1-P), p-nitrophenyl phosphate (pNPP), and beta-glycerol phosphate (beta-GP) are also good substrates, compared to I-1-P. With much lower efficiency, can also hydrolyze inositol 2-phosphate (I-2-P) and glucose-6-phosphate (G-6-P) in vitro, but not fructose-6-phosphate (F-6-P) and trehalose-6- phosphate (T-6-P).
Tuberculosis chemotherapy: the influence of bacillary stress and damage response pathways on drug efficacy
The Mycobacterium tuberculosis Rv2540c DNA sequence encodes a bifunctional chorismate synthase
FUNCTION: Catalyzes the conversion of glucose 6-phosphate to 1D- myo-inositol 3-phosphate (By similarity).
FUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems. May play a role in favoring mycobacterial survival in phagocytes (By similarity).
FUNCTION: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Reactive nitrogen and oxygen intermediates and bacterial defenses: unusual adaptations in Mycobacterium tuberculosis
Mycothiol is essential for growth of Mycobacterium tuberculosis Erdman
Tuberculosis: what we don't know can, and does, hurt us
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Nitric oxide scavenging and detoxification by the Mycobacterium tuberculosis haemoglobin, HbN in Escherichia coli
Cloning and expression of functional shikimate dehydrogenase (EC 1.1.1.25) from Mycobacterium tuberculosis H37Rv
The structure of 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase from Mycobacterium tuberculosis reveals a common catalytic scaffold and ancestry for type I and type II enzymes
Crystal structures of F420-dependent glucose-6-phosphate dehydrogenase FGD1 involved in the activation of the anti-tuberculosis drug candidate PA-824 reveal the basis of coenzyme and substrate binding
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The ABC-type transporter IrtA, probably complexed with IrtB and ViuB (Rv2895c), specifically transports iron-loaded mycobactin into the cytosol (Ryndak et al. 2009).
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Mtb bacterioferritin BfrA oxidises Fe2+ to Fe3+, migrates them to its centre, and collects thousands of them as FeO(OH) in the central mineral core from which they can be later remobilised (Reddy et al. 2012).
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Iron is reduced and separates from mycobactin
The IrtA transporter has a flavin reductase domain very much like Fre from E.coli that can probably act as ferrisiderophore reductase to relieve incoming loaded mycobactin from its Fe3+ by reducing it to Fe2+. Furthermore Rv2895c, which co-precipitates with IrtB and therefore is probably part of the transporter complex, has such a domain as well (Farhana et al. 2008).
Mtb bacterioferritin BfrB oxidises Fe2+ to Fe3+, migrates them to its centre, and collects thousands of them as FeO(OH) in the central mineral core from which they can be later remobilised (Harrison & Arrosio 1996, Khare et al. 2011).
Uptake of iron in Mtb, especially when the bacterium is in the host, strongly depends on siderophores. Humans, through secretion of lactoferrin, maintain an iron concentration of 10^(-18) M within macrophages, and the bacterium has evolved the siderophores mycobactin T and exomycobactin T (formerly exochelin) to cope with this shortage. While nonpolar mycobactin T stays in the cell wall and only moves around in liquid droplets, polar exochelin is abundantly secreted. As it can bind iron with higher affinity than lactoferrin, it frequently scavenges iron ions from this molecule (Miethke & Marahiel 2007).
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FUNCTION: Catalyzes the formation of L-cystathionine from O- succinyl-L-homoserine (OSHS) and L-cysteine, via a gamma- replacement reaction (By similarity). In the absence of thiol, catalyzes gamma-elimination to form 2-oxobutanoate, succinate and ammonia.
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Peroxiredoxin AhpC gets its reducing equivalents through a cascade of proteins via AhpD, a disulfide reductase, DlaT, a lipoylated disulfide reductase, and, finally, from Lpd, the NADH-dependent dihydrolipoyl reductase. The latter two are also part of the pyruvate dehydrogenase complex (Venugopal et al. 2011).
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Cloning and characterization of the aroA gene from Mycobacterium tuberculosis
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Another important antioxidant activity is the KatG catalase/peroxidase which also activates the anti-tuberculosis drug isoniazid (Nagy et al. 1997).
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The versatile AhpC reduces hydrogen peroxide to water (Bryk et al. 2002).
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Reduction of peroxidated lipids depends on reduced AhpC, the only alkyl hydoperoxidase in Mtb (Chauhan & Mande 2001).
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H2O2 gets scavenged by unsaturated lipid
Due to their abundance in Mycobacteria, lipids fulfill a buffering role in the tolerance of antioxidants. Lipid production is triggered by oxidative stress. The peroxidated lipid can be reduced by AhpC (Chauhan & Mande 2001).
Nitrosoglutathione gets cleaved to Cys(NO)-Gly
Most gamma-glutamyl transpeptidases (GGT) cleave both glutathione and glutathione conjugates. Mtb GGT cleaves nitrosoglutathione )GSNO) to Cys(NO)-Gly, thus making it soluble for transport into the cytosol (Dayaram et al. 2006).
Superoxide dismutase SodB is secreted via the Sec transport complex (Braunstein et al. 2003).
Iron-containing superoxide dismutase is localized both within and without the bacterium where it catalyzes the reduction of superoxide (Zhang et al. 1991).
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Copper-containing superoxide dismutase is localized in the plasma membrane of the bacterium where it catalyzes the reduction of superoxide (Wu et al. 1998).
MsrA/B reduces peptide-methionine S/R-sulfoxides
MsrA and MsrB are enzymes that can both reduce the S- and R-stereoisomers of (peptidyl-) methionine sulfoxide. The exact nature of the accompanying thioredoxin is not settled, but it is predicted to be TrxA. The whole methionine-MsrA/B-thioredoxin-and-reductase system is an important part of NO detoxification in Mtb (St John et al. 2001, Lee et al. 2009).
New insights on trehalose: a multifunctional molecule
gene ontology term for cellular function
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Carboxymycobactin and mycobactin exchange their iron load
Carboxymycobactin and mycobactin exchange their iron loads. This interplay between polar and nonpolar siderophore is unique to Mtb. However, mycobactin can gather iron from nonpolar regions of the host cell by itself too (Madigan et al. 2012).
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Carboxymycobactin binds iron from lactoferrin
Since bacterial siderophores bind iron with much greater affinity, they can scavenge iron ions from loaded lactoferrin (Madigan et al. 2012).
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Mycobactin is the lipophilic siderophore of Mtb. After export into the periplasmic space, it localizes to the bacterium's cell wall. The responsible transporter activity is still unknown (Madigan et al. 2012).
Carboxymycobactin is the more polar siderophore of Mtb and it is localized, after its secretion, in the phagosomal lumen. The transporters for export and secretion of this molecule are still unknown (Madigan et al. 2012).
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The Tpx peroxiredoxin is reactivated by either TrxA or TrxB1 (Jaeger et al. 2006).
The enzyme in Mtb known to reduce F420 is the glucose-6-phosphate dehydrogenase Fgd1 (Bashiri et al. 2008).
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The peroxiredoxin AhpC can be alternatively reactivated by TrxA (Jaeger et al. 2004).
TrxB is an NADPH-dependent thioredoxin reductase that reactivates TrxA (Jaeger et al. 2006).
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Cyclization and dephosphorylation of DAHP, catalyzed by AroB, establishes the C6 ring in the pathway which is then only modified in the remaining five reactions (Mendonca et al, 2007).
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The first committed step in the biosynthesis of chorismate is the fusion of D-erythrose-4-phosphate with phosphoenolpyruvate, catalyzed by AroG (Rizzi et al, 2005; Webby et al, 2005).
The dimeric form of AroE catalyzes the hydration of dehydroshikimate. The reaction is reversible with high efficiency (Magalhaes et al, 2002; Fonseca et al, 2006).
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AroQ, which catalyzes the dehydratation of 3-dehydroquinate (DHQ) to 3-dehydroshikimate (DHS), is a type II DHQ dehydratase. Unlike fungi DHQ dehydratases, AroQ doesn't take part in catabolism reactions (Moore et al, 1992).
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Condensation with cleavage of one phosphate group of shikimate 3-phosphate and phosphoenolpyruvate to EPSP is catalyzed by AroA (Garbe et al, 1990).
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Shikimate kinase (AroK) phosphorylates shikimate to shikimate 3-phosphate, using ATP (Oliveira et al, 2001).
Dephosphorylation of EPSP yields chorismate
AroF in complex with reduced FMN catalyzes the dehydration and phosphate cleavage of EPSP, yielding chorismate. The cofactor FMN is reduced by NADPH which makes the enzyme stable in aerobic conditions and is known from similar fungal enzymes (Ely et al, 2008).
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Similar to thiamine or pterine biosynthesis, the sulfide carrier protein CysO serves as substrate to the pyridoxal phosphate-dependent, dimeric CysM which transfers O-phosphoserine onto the sulfur (OLeary et al, 2008; Agren et al, 2008).
cleavage of L-cysteine from carrier protein
After serine was transferred onto its sulfhydryl group, a metallopeptidase cleaves the cysteine molecule from the sulfur carrier protein (Burns et al, 2005).
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Cysteine from cystathionine and vice versa
The pyridoxalphosphate-dependent enzyme MetB not only catalyzes destruction of cystathonine to cysteine but also the transfer of homoserine onto cysteine to yield cystathione from O-succinyl-L-homoserine. This ensures that cysteine and methionine can be interconverted when the need arises. (Wheeler et al, 2005)
Peroxynitrite is reduced to nitrite by Tpx
Tpx, like AhpC, is a peroxiredoxin with alkylhydroperoxidase, peroxidase, and peroxynitritase activities. Peroxynitrite is detoxified to nitrite (Jaeger et al. 2006, Rho et al. 2006).
The peroxiredoxin AhpE participates in reducing peroxynitrite to nitrite, but how it is recycled back to the reduced form is still unknown (Hugo et al. 2009).
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Peroxynitrite is reduced to nitrite by AhpC
AhpC is an unusual peroxiredoxin - it has three cysteine residues that participate in the reduction of toxic peroxynitrite to nitrite. In a second step, another thioredoxin or the reductase chain AhpD/DlaT/Lpd is needed for reactivation (Guimaraes et al. 2005).
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Heme proteins, especially the truncated globin GlbN in Mtb possess oxygen-dependent nitric oxide dioxygenase activity, where the heme that is oxidized to ferriheme in the process will need to be reduced in a second step to activate the protein again. The responsible heme protein reductase is unknown (Ouellet et al. 2002, Pathania et al. 2002).
MscR reduces nitrosomycothiol to ammonia
MscR is an alcohol dehydrogenase that can probably reduce nitrosomycothiol with the help of NADH/H+ reducing equivalents to the sulfinamide which then presumably decomposes to the thione and ammonia (Vogt et al. 2003).
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Nitrosyl is scavenged by mycothiol (MSH), which is functionally analogous to glutathione, which mycobacteria do not possess (Miller et al. 2007).
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Bacterioferritin, like ferritin, is a spherical shell-like protein that takes up 48 ferrous iron ions, and subsequently oxidizes and hydrolyzes them for better storage. (Yang et al, 2000)
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Nitrogen dioxide is reduced to NO by F420
The archaeal cofactor F420 reduces toxic nitrogen dioxide that can be produced when NO and oxygen combine. F420 itself is reduced by the enzyme Fgd (Purwantini & Mukhopadyay 2008).
Peroxynitrite oxidizes methionine residues
Peroxynitrite oxidizes methionine residues (Pryor et al. 1994).
Superoxide can enter the bacterium when acidic conditions apply. Together with a proton it forms the hydroperoxyl radical (Nathan & Shiloh 2000, Zahrt & Deretic 2002, Warner & Mizrahi 2006, Spagnolo et al, 2004).
Conversion of NO2 to NO by reduced coenzyme F420 protects mycobacteria from nitrosative damage