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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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Bibliografski detalji
Glavni autori: Bennett, Brian, Antholine, William E., D’souza, Ventris M., Chen, Guanjing, Ustinyuk, Leila, Holz, Richard C.
Format: Artigo
Jezik:Inglês
Izdano: 2002
Teme:
Online pristup: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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