3x44

Publication Abstract from PubMed

We have recently been successful in cloning a gene cluster necessary for the biosynthesis of D-cycloserine (D-CS) from D-CS-producing Streptomyces lavendulae ATCC11924. Although dcsD, one of the open reading frames located on the gene cluster, encodes a protein homologous to O-acetylserine sulfhydrylase that synthesizes L-cysteine using O-acetyl-L-serine together with sulfide, it functions to form O-ureido-L-serine as a D-CS biosynthetic intermediate, using O-acetyl-L-serine together with hydroxyurea (HU). Using crystallographic and mutational studies, three amino acid residues in DcsD that are important for the substrate preference toward HU were determined in the present study. We showed that two of the three residues are important for the binding of HU into the substrate-binding pocket. The other residue contributes to the formation of a loose hydrogen-bond network during the catalytic reaction. Information regarding the amino acid residues will be very useful in designing a new catalyst to synthesize the beta-substituted-L-alanine derivatives. This article is protected by copyright. All rights reserved.

The structural and mutational analyses of O-ureido-L-serine synthase necessary for D-cycloserine biosynthesis.,Uda N, Matoba Y, Oda K, Kumagai T, Sugiyama M FEBS J. 2015 Jul 24. doi: 10.1111/febs.13386. PMID:26207937^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.