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Binding of ligands to the active site of carboxypeptidase A.

We compare the detailed binding modes of the 39-amino acid inhibitor from potatoes, glycyl-L-tyrosine, the ester analogue CH3OC6H4(CO)CH2CH(CO2(-))C6H5, and indole acetate to the exopeptidase carboxypeptidase A (EC 3.4.17.1). In the potato inhibitor, cleavage of the COOH-terminal glycine-39 leaves a...

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Bibliografske podrobnosti
izdano v:Proc Natl Acad Sci U S A
Principais autores: Rees, D C, Lipscomb, W N
Format: Artigo
Jezik:Inglês
Izdano: National Academy of Sciences 1981
Teme:
Online dostop:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC348764/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/6946483/
https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.78.9.5455
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