Literature DB >> 667684

Mechanisms for activation and inhibition of carboxypeptidase A catalyzed hydrolyses of peptides and esters.

J F Sebastian, W Y Lo.   

Abstract

3,3-Diphenylpropanoate (DPP) activates the carboxypeptidase A catalyzed hydrolysis of benzoylglycyl-L-phenylalanine (BzGly-L-Phe) (Ka = 2.1 x 10 (-3) M) and inhibits ester hydrolysis uncompetitively (K1 =2.1 X 10 (-3) M). A common modifier binding site located adjacent to the peptide and ester substrate binding sites is proposed. The forms of the pathways proposed for activation and inhibition are remarkably similar.

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Year:  1978        PMID: 667684     DOI: 10.1139/o78-051

Source DB:  PubMed          Journal:  Can J Biochem        ISSN: 0008-4018


  1 in total

1.  Spectroscopic studies on Arabidopsis ETHE1, a glyoxalase II-like protein.

Authors:  Meghan M Holdorf; Brian Bennett; Michael W Crowder; Christopher A Makaroff
Journal:  J Inorg Biochem       Date:  2008-06-13       Impact factor: 4.155

  1 in total

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