Protein thiocarboxylate-dependent methionine biosynthesis in Wolinella succinogenes. Academic Article

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.

authors

• Begley, Tadhg

published proceedings

• J Am Chem Soc

altmetric score

• 3

author list (cited authors)

• Krishnamoorthy, K., & Begley, T. P.

citation count

• 18

complete list of authors

• Krishnamoorthy, Kalyanaraman||Begley, Tadhg P

publication date

• January 2011

publisher

• American Chemical Society (ACS)  Publisher

published in

• Journal of the American Chemical Society  Journal

keywords

• Alanine
• Biocatalysis
• Dipeptides
• Metalloproteases
• Methionine
• Molecular Structure
• Sulfhydryl Compounds
• Wolinella

PubMed Central ID

• 21162571

Digital Object Identifier (DOI)

• 10.1021/ja107424t

start page

• 379

end page

• 386

volume

• 133

issue

• 2

URL

• http%3A%2F%2Fdx.doi.org%2F10.1021%2Fja107424t