Carboxypeptidase - Wikipedia, the free encyclopedia
Carboxypeptidase (EC number 3.4.16 - 3.4.18) is an enzyme that hydrolyzes the carboxy-terminal (C-terminal) end of a peptide bond. Humans, animals, and plants contain several types of carboxypeptidas...
en.wikipedia.org/wiki/Carboxypeptidase
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Carboxypeptidase A - Wikipedia, the free encyclopedia
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Carboxypeptidase A usually refers to the pancreatic exopeptidase which hydrolyzes peptide bonds of C-terminal residues with aromatic or aliphatic side chains. Most scientists in the field now refer t...
en.wikipedia.org/wiki/Carboxypeptidase_A
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Carboxypeptidase and Substrate Binding ... Carboxypeptidase A is a good illustration of the induced-fit theory, because the active site changes appreciably when the substrate binds. Figures 2 and 3 show three-dimensional representations of the carboxylase protein with and without a bound substrate.
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www.chemistry.wustl.edu/~edudev/LabTutorials/Carboxypep...
www.chemistry.wustl.edu/~edudev/LabTutorials/Carboxypeptidase/carboxypeptidase.html
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In humans and pigs, the reaction occurs at pH 6.5 at the jejunal brush border membrane by folate hydrolase and is encoded by the glutamate carboxypeptidase II (GCPII) gene. Intracellular folate hydrolase with an optimal pH of 4.5 is encoded by the gamma-glutamyl hydrolase (gamma-GH) gene and predominates in rats.
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www.medscape.com/medline/abstract/17449573
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The Medscape Journal ... Glutamate Carboxypeptidase II [metabolism] ... EC 3.4.17.21 (Glutamate Carboxypeptidase II)
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www.medscape.com/medline/abstract/15836619
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Characteristics of Carboxypeptidase A from Bovine Pancreas: ... (1987) discuss the interaction of carboxypeptidase A with carbamate and carbonate esters. Suh and Kaiser (1975) report on the hydrolysis of different enantiomers of a substrate.
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www.worthington-biochem.com/COA/default.html
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In this tutorial you will be looking at the enzyme Carboxypeptidase A using the Chemscape Chime plug-in. This plug-in is very similar in functionality to Rasmol - an interactive Molecular Visualisation program.
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wbiomed.curtin.edu.au/biochem/tutorials/cpa/CPA_Chime.h...
wbiomed.curtin.edu.au/biochem/tutorials/cpa/CPA_Chime.htm
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There are 3 carboxypeptidase domains. Only the first two domains have any catalytic activity. The first domain preferentially cleaves C-terminal Arg residues, whereas the second preferentially cleaves C-terminal Lys residues.
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www.uniprot.org/uniprot/Q90240
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