Radiochemical determination of a unique sequence around the reactive serine residue of a di-isopropyl phosphorofluoridate-sensitive plant carboxypeptidase and a yeast peptidase
Keyword(s):
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.
2005 ◽
Vol 53
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pp. 2406-2411
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1975 ◽
pp. 57-61
1977 ◽
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pp. 561-570
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2008 ◽
Vol 71
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pp. 1491-1495
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1989 ◽
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pp. 595-602
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2001 ◽
Vol 49
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pp. 5265-5269
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1974 ◽
Vol 57
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pp. 529-533
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1988 ◽
Vol 173
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pp. 27-34
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1976 ◽
Vol 82
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pp. 283-285
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