Ontology highlight
ABSTRACT:
SUBMITTER: Krishnamoorthy K
PROVIDER: S-EPMC3089676 | biostudies-literature | 2011 Jan
REPOSITORIES: biostudies-literature
Krishnamoorthy Kalyanaraman K Begley Tadhg P TP
Journal of the American Chemical Society 20101216 2
Thiocarboxylated proteins are important intermediates in a variety of biochemical sulfide transfer reactions. Here we identify a protein thiocarboxylate-dependent methionine biosynthetic pathway in Wolinella succinogenes. In this pathway, the carboxy terminal alanine of a novel sulfur transfer protein, HcyS-Ala, is removed in a reaction catalyzed by a metalloprotease, HcyD. HcyF, an ATP-utilizing enzyme, catalyzes the adenylation of HcyS. HcyS acyl-adenylate then undergoes nucleophilic substitut ...[more]