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. 1976 Apr;126(1):132–139. doi: 10.1128/jb.126.1.132-139.1976

Specific in vivo cleavage of D-serine deaminase and properties of tetrameric polypeptide aggregates of the fragments.

M C Heincz, E McFall
PMCID: PMC233267  PMID: 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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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