Ontology highlight
ABSTRACT:
SUBMITTER: Avalos D
PROVIDER: S-EPMC6381839 | biostudies-literature | 2019 Feb
REPOSITORIES: biostudies-literature
Avalos Dante D Sabuncu Sinan S Mamounis Kyle J KJ Davidson Victor L VL Moënne-Loccoz Pierre P Yukl Erik T ET
Biochemistry 20190115 6
The LodA-like proteins make up a recently identified family of enzymes that rely on a cysteine tryptophylquinone cofactor for catalysis. They differ from other tryptophylquinone enzymes in that they are oxidases rather than dehydrogenases. GoxA is a member of this family that catalyzes the oxidative deamination of glycine. Our previous work with GoxA from Pseudoalteromonas luteoviolacea demonstrated that this protein forms a stable intermediate upon anaerobic incubation with glycine. The spectro ...[more]