Ontology highlight
ABSTRACT:
SUBMITTER: Ayres CA
PROVIDER: S-EPMC4188075 | biostudies-literature | 2014 Oct
REPOSITORIES: biostudies-literature
Ayres Chapelle A CA Schormann Norbert N Senkovich Olga O Fry Alexandra A Banerjee Surajit S Ulett Glen C GC Chattopadhyay Debasish D
Acta crystallographica. Section F, Structural biology communications 20140925 Pt 10
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a conserved cytosolic enzyme, which plays a key role in glycolysis. GAPDH catalyzes the oxidative phosphorylation of D-glyceraldehyde 3-phosphate using NAD or NADP as a cofactor. In addition, GAPDH localized on the surface of some bacteria is thought to be involved in macromolecular interactions and bacterial pathogenesis. GAPDH on the surface of group B streptococcus (GBS) enhances bacterial virulence and is a potential vaccine candidate. Here ...[more]