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...
Tallennettuna:
| Julkaisussa: | Proc Natl Acad Sci U S A |
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| Päätekijät: | , |
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
National Academy of Sciences
1981
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| Aiheet: | |
| Linkit: | 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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