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Titolo:
Metal ion binding and activation of Streptomyces griseus dinuclear aminopeptidase: cadmium(II) binding as a model
Autore:
Hasselgren, C; Park, HI; Ming, LJ;
Indirizzi:
Univ S Florida, Inst Biomol Sci, Tampa, FL 33620 USA Univ S Florida TampaFL USA 33620 a, Inst Biomol Sci, Tampa, FL 33620 USA Univ S Florida, Dept Chem, Tampa, FL 33620 USA Univ S Florida Tampa FL USA 33620 Florida, Dept Chem, Tampa, FL 33620 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY
fascicolo: 2, volume: 6, anno: 2001,
pagine: 120 - 127
SICI:
0949-8257(200102)6:2<120:MIBAAO>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
AEROMONAS-PROTEOLYTICA AMINOPEPTIDASE; LENS LEUCINE AMINOPEPTIDASE; ZINC SUPEROXIDE-DISMUTASE; BOVINE LENS; CRYSTAL-STRUCTURE; DERIVATIVES; ENZYME; REFINEMENT; HYDROLYSIS; NICKEL(II);
Keywords:
aminopeptidase; dinuclear; metal binding; streptomyces; cadmium;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
28
Recensione:
Indirizzi per estratti:
Indirizzo: Ming, LJ Chalmers Univ Technol, Dept Inorgan Chem, S-41296 Gothenburg, Sweden Chalmers Univ Technol Gothenburg Sweden S-41296 henburg, Sweden
Citazione:
C. Hasselgren et al., "Metal ion binding and activation of Streptomyces griseus dinuclear aminopeptidase: cadmium(II) binding as a model", J BIOL I CH, 6(2), 2001, pp. 120-127

Abstract

A detailed metal binding and activation of the dinuclear aminopeptidase from Streptomyces griseus (sAP) has been analyzed and modeled by means of metal titration as well as kinetic and thermodynamic techniques using Cd2+ as a probe. Cd2+ binds to the two metal-binding sites in a sequential manner to produce a very active Cd2+-substituted derivative, particularly in the presence of Ca2+ (53% and 90%, respectively, relative to the activities of the native form in terms of k(cat)/K-m under the same conditions). The first stepwise formation constant for the binding of metal to the dinuclear site (to form M-sAP) was found to determine the metal-binding selectivity, regardless of the magnitude of the second stepwise formation constant (to form M,M-sAP from M-sAP). Interestingly, despite the seemingly very different binding profiles for different metal ions under different conditions, all of them can be well described and fitted by the sequential binding model. In addition, Ca2+ was found to significantly affect metal binding, inhibition, and entropy of activation of this enzyme, and its role in sAP action is re-evaluated.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/07/20 alle ore 04:59:25