Ontology highlight
ABSTRACT:
SUBMITTER: Koutmos M
PROVIDER: S-EPMC3000283 | biostudies-literature | 2010 Dec
REPOSITORIES: biostudies-literature
Koutmos Markos M Kabil Omer O Smith Janet L JL Banerjee Ruma R
Proceedings of the National Academy of Sciences of the United States of America 20101116 49
The catalytic potential for H(2)S biogenesis and homocysteine clearance converge at the active site of cystathionine β-synthase (CBS), a pyridoxal phosphate-dependent enzyme. CBS catalyzes β-replacement reactions of either serine or cysteine by homocysteine to give cystathionine and water or H(2)S, respectively. In this study, high-resolution structures of the full-length enzyme from Drosophila in which a carbanion (1.70 Å) and an aminoacrylate intermediate (1.55 Å) have been captured are report ...[more]