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Specialty Chemistry Forums => Biochemistry and Chemical Biology Forum => Topic started by: littlejoker on January 07, 2017, 03:51:56 AM

Title: About carboxypeptidase
Post by: littlejoker on January 07, 2017, 03:51:56 AM
Can a carboxypeptidase cleave the peptide bond at C-terminal of an amidated peptide?
Title: Re: About carboxypeptidase
Post by: AWK on January 07, 2017, 05:54:28 AM
https://en.wiki2.org/wiki/Carboxypeptidase+Newton
https://en.wiki2.org/wiki/Dipeptidyl_carboxypeptidase+Newton
Title: Re: About carboxypeptidase
Post by: littlejoker on January 07, 2017, 09:22:31 AM
Thank you.
So it cannot cleave blocked peptides, right?
Title: Re: About carboxypeptidase
Post by: AWK on January 07, 2017, 10:51:38 AM
Peptides may be blocked in different ways. Name of enzyme itself informs you which group should be free,
Title: Re: About carboxypeptidase
Post by: Babcock_Hall on January 07, 2017, 02:13:09 PM
At the active site of carboxypeptidase A is an arginine residue that is positioned to bind to the carboxylate residue of the C-terminal amino acid residue.  Without the charge, my prediction is that the rate would be much slower, but one would have to answer this question empirically for each type of carboxypeptidase.  One place to start a search for such information might be BRENDA.