Cell Bio

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spacecowboi
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Cell Bio

Post by spacecowboi » Mon Oct 10, 2011 5:21 am

Why (in detail please) in the carboxypeptidase mechanism, the weak bonds between an enzyme and a substrate will stretch the peptide bond of the substrate which lowers the bond energy?

I just want to know why in detail this happens... Thank you.

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JackBean
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Post by JackBean » Mon Oct 10, 2011 6:16 am

that's a common mechanism in enzymes, not only in carboxypeptidase. However, the point is, there are several of these "weak" bonds and their sum is strong enough to stretch the peptide causing to be better to hydrolyse.
http://www.biolib.cz/en/main/

Cis or trans? That's what matters.

spacecowboi
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Post by spacecowboi » Tue Oct 11, 2011 7:29 pm

I see that clarifies it. Also, I know it is Tyrosine that attacks carboxypeptidases C-terminus, although how is Tyrosine capable of doing so?

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JackBean
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Post by JackBean » Mon Oct 17, 2011 6:32 am

My guess would be the hydroxyl group, but I would need to see some article about this matter to explain it more deeply.
http://www.biolib.cz/en/main/

Cis or trans? That's what matters.

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