Journal ArticleDOI
Structure and mechanism in the enzymic activity of carboxypeptidase A and relations to chemical sequence
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This article is published in Accounts of Chemical Research.The article was published on 1970-03-01. It has received 126 citations till now. The article focuses on the topics: Carboxypeptidase A & Carboxypeptidase.read more
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Cobalt (III) carboxypeptidase A: Preparation and esterase activity
TL;DR: It is demonstrated that scission of a bond to the first coordination sphere of the metal is not necessary for the hydrolysis of ester substrates in the case of Co(III) carboxypeptidase A.
Journal ArticleDOI
Mn(III)-containing acid phosphatase. Properties of Fe(III)-substituted enzyme and function of Mn(III) and Fe(III) in plant and mammalian acid phosphatases.
TL;DR: The present results indicate that Mn( III) and Fe(III) in the acid phosphatase play an important role on effective binding of phosphate and acceleration of hydrolysis of phosphomonoesters at pH 4-6.
Journal ArticleDOI
Metabolic resistance of the D-peptide RD2 developed for direct elimination of amyloid-β oligomers.
Anne Elfgen,Michelle Hupert,Kevin Bochinsky,Markus Tusche,Estibaliz González de San Román Martin,Ian Gering,Silvia Sacchi,Loredano Pollegioni,Pitter F. Huesgen,Rudolf Hartmann,Beatrix Santiago-Schübel,Janine Kutzsche,Dieter Willbold +12 more
TL;DR: The high stability and the absence of relevant human-specific metabolites support RD2 to be safe for oral administration in humans, and RD2 did not influence the activity of any of the tested enzymes.
Journal ArticleDOI
Kinetics of formation and dissociation of metallocarboxypeptidases.
TL;DR: Rate constants for dissociation of CoCPA, NiCPA, and ZnCPA were measured by loss of enzyme activity on addition of the metal ion scavenger EDTA, and values of K obtained kinetically were in good agreement with those determined by activity measurements of equilibrated solutions.
Journal ArticleDOI
Basic and Non-Basic Substrates of Carboxypeptidase B
TL;DR: The kinetics of porcine-carboxypeptidase-B-catalyzed hydrolysis of several N-blocked peptides that differ in size and in C-terminal amino acid were examined, demonstrating different kinetic behaviour of carboxypePTidases of basic and non-basic substrates.
References
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Journal ArticleDOI
Structure of hen egg-white lysozyme. A three-dimensional Fourier synthesis at 2 Angstrom resolution.
C. C. F. Blake,D. F. Koenig,D. F. Koenig,G. A. Mair,A. C. T. North,D. C. Phillips,V. R. Sarma +6 more
TL;DR: Structure of Hen Egg-White Lysozyme: A Three-dimensional Fourier Synthesis at 2 A Resolution as mentioned in this paper, 3D Fourier synthesis at 2 a resolution.
Journal ArticleDOI
Structure of Myoglobin: A Three-Dimensional Fourier Synthesis at 2 Å. Resolution
J. C. Kendrew,R. E. Dickerson,B. E. Strandberg,R G Hart,D R Davies,D. C. Phillips,V. C. Shore +6 more
Journal ArticleDOI
Structure of papain.
TL;DR: A three-dimensional X-ray study at a resolution of 2.8 A has revealed that the single polypeptide chain of 211 residues is folded into two distinct parts which are divided by a cleft as mentioned in this paper.
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Metallocarboxypeptidases: stability constants and enzymatic characteristics.
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