Carboxypeptidase A: Difference between revisions
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{{Sandbox_Reserved_Butler_CH462_Sp2015_#}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | {{Sandbox_Reserved_Butler_CH462_Sp2015_#}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | ||
=='''Carboxypeptidase A'''== | =='''Carboxypeptidase A'''== | ||
<StructureSection load=' | <StructureSection load='3cpa' size='340' side='right' caption='Caption for this structure' scene=''> | ||
== 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
IntroductionCarboxypeptidase 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 FunctionStructural OverviewMechanism of ActionZinc Ligand(s)Other LigandsThis is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
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