Carboxypeptidase A: Difference between revisions

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{{Sandbox_Reserved_Butler_CH462_Sp2015_#}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
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=='''Carboxypeptidase A'''==
=='''Carboxypeptidase A'''==
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
<StructureSection load='3cpa' size='340' side='right' caption='Caption for this structure' scene=''>
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== Introduction ==
Carboxypeptidase A (peptidyl-L-amino acid hydrolase, EC 3.4.17.1, often abbreviated CPA) is a metalloexopeptidase whose biological function is to cleave the C-terminal amino acid residues from polypeptide substrates. Specifically, CPA is one member of a large group of Zn{{sup|2+}}


== Biological Function ==
== Biological Function ==

Revision as of 16:08, 14 March 2017

This Sandbox is Reserved from 02/09/2015, through 05/31/2016 for use in the course "CH462: Biochemistry 2" taught by Geoffrey C. Hoops at the Butler University. This reservation includes Sandbox Reserved 1051 through Sandbox Reserved 1080.
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Carboxypeptidase ACarboxypeptidase A


Introduction

Carboxypeptidase A (peptidyl-L-amino acid hydrolase, EC 3.4.17.1, often abbreviated CPA) is a metalloexopeptidase whose biological function is to cleave the C-terminal amino acid residues from polypeptide substrates. Specifically, CPA is one member of a large group of ZnTemplate:Sup

Biological Function

Structural Overview

Mechanism of Action

Zinc Ligand(s)

Other Ligands

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Caption for this structure

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ReferencesReferences

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Geoffrey C. Hoops, Michael Melbardis, Douglas Schnell, Thomas Baldwin, Michal Harel