Complete genome sequence of Thermomonospora curvata type strain (B9).
A Key Glycine in Bacterial Steroid-Degrading Acyl-CoA Dehydrogenases Allows Flavin-Ring Repositioning and Modulates Substrate Side Chain Specificity.
Copper is a cofactor of the formylglycine-generating enzyme.
In vitro reconstitution of formylglycine-generating enzymes requires copper(I).
Structural basis for copper-oxygen mediated C-H bond activation by the formylglycine-generating enzyme.
The steroid side-chain-cleaving aldolase Ltp2-ChsH2DUF35 is a thiolase superfamily member with a radically repurposed active site.
The ArsI C-As lyase: Elucidating the catalytic mechanism of degradation of organoarsenicals.
Identification of Surface-Exposed Protein Radicals and A Substrate Oxidation Site in A-Class Dye-Decolorizing Peroxidase from Thermomonospora curvata.
Substrates control multimerization and activation of the multi-domain ATPase motor of type VII secretion.
Structure of formylglycine-generating enzyme in complex with copper and a substrate reveals an acidic pocket for binding and activation of molecular oxygen.