| Literature DB >> 770418 |
Abstract
The primary D-serine deaminase (D-serine dehydratase, EC 4.2.1.14) of Escherichia coli K-12 is unstable within the cell. The protein, a single polypeptide chain, is cleaved at a lysine residue by a cellular proteolytic activity. Fragments containing the active site then aggregate into tetramers, which retain substrate affinity and show very low catalytic activity. Such degradations may represent an evolutionary mechanism for the generation of new enzymes.Entities:
Mesh:
Substances:
Year: 1976 PMID: 770418 PMCID: PMC233267 DOI: 10.1128/jb.126.1.132-139.1976
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490