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

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 [(32)P]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.

SUBMITTER: Shaw DC

PROVIDER: S-EPMC1173758 | biostudies-other | 1972 Jun

REPOSITORIES: biostudies-other

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The reactive serine residue of epidermolytic toxin A.

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