Journal ArticleDOI
The effect of modifiers on the hydrolysis of esters and peptides by carboxypeptidase A
TLDR
Previous reports concerning these phenomena of N-substituted products of hydrolysis of certain synthetic peptide and ester substrates are extended and relates them to the kinetic data currently available on carboxypeptidase catalysis.About:
This article is published in Biochemical and Biophysical Research Communications.The article was published on 1968-05-23. It has received 35 citations till now. The article focuses on the topics: Carboxypeptidase A & Carboxypeptidase.read more
Citations
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Book ChapterDOI
Carboxypeptidase A: a protein and an enzyme.
TL;DR: This chapter discusses the relationship of the three-dimensional structures of bovine carboxypeptidase A, and of its complexes with substrates and inhibitors, to the functional behavior of this enzyme.
Book
Adp-Ribosylation of Proteins
TL;DR: The role of Lysine Residues in the Catalytic Function and DNA Binding of Poly(ADP-Ribose) Polymerase as Determined by the Covalent Modification of the Enzyme Protein with Methyl Acetimidate is studied.
Journal ArticleDOI
Kinetics of carboxypeptidase A. II. Inhibitors of the hydrolysis of oligopeptides.
David S. Auld,Bert L. Vallee +1 more
Journal ArticleDOI
Kinetics of carboxypeptidase A. pH dependence of tripeptide hydrolysis catalyzed by zinc, cobalt, and manganese enzymes
David S. Auld,Bert L. Vallee +1 more
Journal ArticleDOI
Inhibitors and activators of ADP-ribosylation reactions.
Marek Banasik,Kunihiro Ueda +1 more
TL;DR: Several potent inhibitors of arginine-specific mono(ADP-ribosyl)transferases and activators of poly(ADp-ribose) synthetase are found.
References
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Journal ArticleDOI
Kinetics of carboxypeptidase A. I. Hydrolysis of carbobenzoxyglycyl-l-phenylalanine, benzoylglycyl-l-phenylalanine, and hippuryl-dl-beta-phenyllactic acid by metal-substituted and acetylated carboxypeptidases.
Journal ArticleDOI
The Reaction of Carboxypeptidase A with Hippuryl-DL-β-Phenyllactate*
Journal ArticleDOI
The kinetics of some carboxypeptidase A and acetylcarboxypeptidase A catalyzed hydrolyses.
Journal ArticleDOI
The Structure of Carboxypeptidase A V. STUDIES OF ENZYME-SUBSTRATE AND ENZYME-INHIBITOR COMPLEXES AT 6 A RESOLUTION
TL;DR: Model peptide substrates and inhibitors are shown at 6 A resolution to bind to crystalline carboxypeptidase Aα in regions near the zinc atom, and there appears to be a structural change in the enzyme when substrates are bound to the native or modified enzyme.
Related Papers (5)
Kinetics of carboxypeptidase A. I. Hydrolysis of carbobenzoxyglycyl-l-phenylalanine, benzoylglycyl-l-phenylalanine, and hippuryl-dl-beta-phenyllactic acid by metal-substituted and acetylated carboxypeptidases.
Kinetics of carboxypeptidase A. II. Inhibitors of the hydrolysis of oligopeptides.
David S. Auld,Bert L. Vallee +1 more