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Structurally Distinct Active Sites in the Copper(II)-Substituted Aminopeptidases from Aeromonas proteolytica and Escherichia coli
The aminopeptidase from Aeromonas proteolytica (AAP) was titrated with copper, which bound sequentially at two distinct sites. Both the mono- and disubstituted forms of AAP exhibited catalytic hyperactivity relative to the native dizinc enzyme. Monosubstituted AAP exhibited an axial Cu(II) EPR spect...
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| Autori principali: | , , , , , |
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| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
2002
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2669718/ https://ncbi.nlm.nih.gov/pubmed/12405829 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/ja026341p |
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