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INHIBITION AND ACTIVATION OF BARLEY PEPTIDE HYDROLASES II. PEPTIDE HYDROLASES B AND C, AND L‐LEUCYL‐β‐NAPHTHYLAMIDASE
Author(s) -
Burger W. C.,
Prentice Neville,
Moeller Mary
Publication year - 1971
Publication title -
journal of the institute of brewing
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.523
H-Index - 51
eISSN - 2050-0416
pISSN - 0046-9750
DOI - 10.1002/j.2050-0416.1971.tb06948.x
Subject(s) - dithiothreitol , chemistry , peptide , enzyme , esterase , hydrolase , serine , biochemistry , chelation , stereochemistry , serine hydrolase , organic chemistry
Peptide hydrolase B is inhibited by DIPF and appears to be a “serine esterase” enzyme. Para‐chloromercuribenzoate is also inhibitory, but it acts irreversibly and not as a mercaptide former. Dithiothreitol acts irreversibly to inhibit the enzyme and thioglycolate is a weak, reversible inhibitor. Peptide hydrolase C is also inhibited by DIPF, and no consistent indication of metal ion or sulphydryl group involvement was observed. L‐leucyl‐β‐naphthylamidase apears to be a metalloenzyme. It is mildly inhibited by some chelating agents and is stimulated by Ni 2+ after prior treatment with EDTA. The enzyme is moderately inhibited by PCMPS and exhibits variable responses to different sulphydryl compounds.