The primary D-serine deaminase (D-serine dehydratase, EC 220.127.116.11) 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
To submit an update or takedown request for this paper, please submit an Update/Correction/Removal Request.