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. 1972 Jun;128(2):229–235. doi: 10.1042/bj1280229

Radiochemical determination of a unique sequence around the reactive serine residue of a di-isopropyl phosphorofluoridate-sensitive plant carboxypeptidase and a yeast peptidase

D C Shaw 1, J R E Wells 1
PMCID: PMC1173758  PMID: 4563640

Abstract

Phaseolain, a carboxypeptidase from French-bean leaves, and a partially purified peptidase from baker's yeast are inhibited by reaction with di-isopropyl phosphorofluoridate. Radioactive di-isopropyl [32P]phosphorofluoridate was used to show that the site of reaction is a unique serine residue and that the sequence of amino acids adjacent to the reactive serine is Glu-Ser-Tyr. This sequence is different from those of other `serine' enzymes previously reported and, for phaseolain, represents an unequivocal example of a `serine' carboxypeptidase.

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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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