170740
units: 411824
value: 7.08333333333333E-14
type: LocalParameter

412018
local parameters: 170740
local parameters: 170739
notes: kf*NM_minus_Arginine*Im_minus_nNOS-kb*Im_minus_nNOS_minus_NM_minus_Arginine
type: KineticLaw

020813
constant: false
boundary condition: false
has only substance units: false
initial concentration: 1.0
initial amount: NaN
in compartment: 020793
type: Species

020773
constant: true
size: 1.0E-18
spatial dimensions: 3.0
type: Compartment

020793
constant: true
size: 1.6667E-18
spatial dimensions: 3.0
type: Compartment

170738
units: 411860
value: 3.33333333333333E-19
type: LocalParameter

411981
stoichiometry: 1.0
species: 020853
type: SpeciesReference

MODEL9088169066
species: 020833
species: 020813
compartment: 020793
notes: This model is taken from the Peer-reviewed publication>Husam M. Abu-Soud et al. Biochemistry 1999, 38, 12446-12451. This model shows kinetic binding of NMArginine to neuronal nitric oxide synthase. Model shows the substrate (NM-Arginine) binding to nNOS in a two-step reversible fashion. First there is rapid binding equilibrium between Im-nNOS and NM-Arginine to form an intermediate that contains bound imidazole and NM-arginine. This is followed by a slower conformational change in the Im-enzyme-substrate complex that is associated with release of bound imidazole and generation of a modified enzyme-substrate complex which is detected due to spectral change. Rates approximated based on data in Table 2. The rates for first reaction are not exact since only Kd known and appropriate graphs do not exist for matching the profile. This model originates from BioModels Database: A Database of Annotated Published Models (http://www.ebi.ac.uk/biomodels/). It is copyright (c) 2005-2011 The BioModels.net Team. To the extent possible under law, all copyright and related or neighbouring rights to this encoded model have been dedicated to the public domain worldwide. Please refer to CC0 Public Domain Dedication for more information. In summary, you are entitled to use this encoded model in absolutely any manner you deem suitable, verbatim, or with modification, alone or embedded it in a larger context, redistribute it, commercially or not, in a restricted way or not.. To cite BioModels Database, please use: Li C, Donizelli M, Rodriguez N, Dharuri H, Endler L, Chelliah V, Li L, He E, Henry A, Stefan MI, Snoep JL, Hucka M, Le Novère N, Laibe C (2010) BioModels Database: An enhanced, curated and annotated resource for published quantitative kinetic models. BMC Syst Biol., 4:92.
substance units: 411908
is described by: http://identifiers.org/pubmed/10493814
units def: 411824
type: SBMLModel
species: 020873
volume units: 679943
time units: 131570
length unit: length
compartment: 020773
name: Abu-Soud1999_NMArginine
units def: 411908
units def: 411860
reaction: 020933
reaction: 020913
species: 020893
species: 020853
curated: false
area units: area

412005
stoichiometry: 1.0
species: 020893
type: SpeciesReference

411957
stoichiometry: 1.0
species: 020833
type: SpeciesReference

411993
stoichiometry: 1.0
species: 020813
type: SpeciesReference

020913
kinetic law: 411969
product: 411957
product: 411944
reactant: 411932
notes: Release of Imidazole from complex of NM-Arginine and Imidazole bound rat brain neuronal Nitric Oxide Synthase. Abu-Soud HM et al. Biochemistry. 1999 21;38(38):12446-51
fast: false
reversible: true
type: Reaction

411969
local parameters: 170738
local parameters: 170737
notes: kf*Im_minus_nNOS_minus_NM_minus_Arginine-kb*nNOS_minus_NM_minus_Arginine*Imidazole
type: KineticLaw

411848
exponent: -1.0
scale: 0
multipler: 1.0
kind: SECOND
type: SBMLUnit

170737
units: 411824
value: 4.5E-17
type: LocalParameter

411884
exponent: -1.0
scale: -6
multipler: 1.0
kind: MOLE
type: SBMLUnit

020933
kinetic law: 412018
product: 412005
reactant: 411993
reactant: 411981
notes: Binding of NM-Arginine to Imidazole bound rat brain neuronal Nitric Oxide Synthase. Only Kd is known, Kf and Kb need to be approximated accordingly to match kinetic profiles. Due to lack of appropriate graphs the choice of Kf and Kb here is arbitrary and matches only the Kd. Kd = 1.7mM = 1700uM Abu-Soud HM et al. Biochemistry. 1999 21;38(38):12446-51
fast: false
reversible: true
type: Reaction

020833
constant: false
boundary condition: false
has only substance units: false
initial concentration: 0.0
initial amount: NaN
in compartment: 020793
type: Species

411836
exponent: 1.0
scale: 0
multipler: 1.0
kind: LITRE
type: SBMLUnit

170739
units: 411860
value: 4.16666666666667E-17
type: LocalParameter

411944
stoichiometry: 1.0
species: 020873
type: SpeciesReference

020893
constant: false
boundary condition: false
has only substance units: false
initial concentration: 0.0
initial amount: NaN
in compartment: 020793
type: Species

411872
exponent: 2.0
scale: 0
multipler: 1.0
kind: LITRE
type: SBMLUnit

411920
exponent: 1.0
scale: -6
multipler: 1.0
kind: MOLE
type: SBMLUnit

020853
constant: false
boundary condition: false
has only substance units: false
initial concentration: 6000.0
initial amount: NaN
in compartment: 020793
type: Species

411896
exponent: -1.0
scale: 0
multipler: 1.0
kind: SECOND
type: SBMLUnit

020873
constant: false
boundary condition: false
has only substance units: false
initial concentration: 0.0
initial amount: NaN
in compartment: 020793
type: Species

411932
stoichiometry: 1.0
species: 020893
type: SpeciesReference