7vdy
From Proteopedia
Crystal structure of O-ureidoserine racemase
Structural highlights
FunctionDCSC_STRLA Involved in the biosynthesis of the antibiotic D-cycloserine (DCS), a cyclic structural analog of D-alanine, used as an antitubercular agent. Catalyzes the stereoinversion of O-ureido-L-serine to O-ureido-D-serine.[1] [2] [3] Publication Abstract from PubMedThe O-ureidoserine racemase (DcsC) is an enzyme found from the biosynthetic gene cluster of antitubercular agent d-cycloserine. Although DcsC is homologous to diaminopimelate epimerase (DapF) that catalyzes the interconversion between ll- and dl-diaminopimelic acid, it specifically catalyzes the interconversion between O-ureido-l-serine and its enantiomer. Here we determined the crystal structure of DcsC at a resolution of 2.12 A, implicating that the catalytic mechanism of DcsC shares similarity with that of DapF. Comparing the structure of the active center of DcsC to that of DapF, Thr72, Thr198, and Tyr219 of DcsC are likely to be involved in the substrate specificity. Crystal structure of O-ureidoserine racemase found in the d-cycloserine biosynthetic pathway.,Oda K, Sakaguchi T, Matoba Y Proteins. 2022 Apr;90(4):912-918. doi: 10.1002/prot.26290. Epub 2021 Dec 17. PMID:34877716[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||||
