Specific in vivo cleavage of D-serine deaminase and properties of tetrameric polypeptide aggregates of the fragments.
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.
D000596:Amino Acids / Q000032:analysis; D002474:Cell-Free System; D004926:Escherichia coli / Q000201:enzymology*; D012695:L-Serine Dehydratase / Q000032:analysis / Q000378:metabolism*; D008970:Molecular Weight; D009154:Mutation; D010447:Peptide Hydrolases / Q000378:metabolism; D010455:Peptides / Q000032:analysis / Q000378:metabolism*; D011732:Pyridoxal Phosphate / Q000032:analysis; D013237:Stereoisomerism; D014105:Tosyl Compounds / Q000494:pharmacology
D000596:Amino Acids; D010455:Peptides; D014105:Tosyl Compounds; D011732:Pyridoxal Phosphate; D010447:Peptide Hydrolases; D012695:L-Serine Dehydratase