Activities | Families | Sequences | Fold types | References | Help
B6db references: 21931214

type Journal Article
authors Krishnamoorthy K, Begley TP.
title Protein thiocarboxylate-dependent methionine biosynthesis in Wolinella succinogenes.
journal J Am Chem Soc.
Activity mety
Family mety
sel selected
ui 21931214
year (2011)
volume 133
number 2
pages 379-86
abstract 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 substitution by bisulfide produced by Sir to give the HcyS thiocarboxylate. This adds to O-acetylhomoserine to give HcyS-homocysteine in a PLP-dependent reaction catalyzed by MetY. HcyD-mediated hydrolysis liberates homocysteine. A final methylation completes the biosynthesis. The biosynthetic gene cluster also encodes the enzymes involved in the conversion of sulfate to sulfide suggesting that sulfate is the sulfur source for protein thiocarboxylate formation in this system.
last changed 2018/03/27 10:14

B6db references