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Titolo:
METAL-BINDING AND ACTIVE-SITE STRUCTURE OF DI-ZINC STREPTOMYCES-GRISEUS AMINOPEPTIDASE
Autore:
LIN LY; PARK HI; MING LJ;
Indirizzi:
UNIV S FLORIDA,DEPT CHEM TAMPA FL 33620 UNIV S FLORIDA,DEPT CHEM TAMPA FL 33620 UNIV S FLORIDA,INST BIOMOL SCI TAMPA FL 33620
Titolo Testata:
JBIC. Journal of biological inorganic chemistry
fascicolo: 6, volume: 2, anno: 1997,
pagine: 744 - 749
SICI:
0949-8257(1997)2:6<744:MAASOD>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
LENS LEUCINE AMINOPEPTIDASE; NUCLEAR-MAGNETIC-RESONANCE; SUPEROXIDE-DISMUTASE; H-1-NMR SPECTROSCOPY; COPPER(II) COMPLEXES; CARBOXYPEPTIDASE-A; MECHANISM; ENZYME; DERIVATIVES; RESOLUTION;
Keywords:
AMINOPEPTIDASE; STREPTOMYCES; DINUCLEAR; NMR; CO2+; CU2+;
Tipo documento:
Article
Natura:
Periodico
Citazioni:
40
Recensione:
Indirizzi per estratti:
Citazione:
L.Y. Lin et al., "METAL-BINDING AND ACTIVE-SITE STRUCTURE OF DI-ZINC STREPTOMYCES-GRISEUS AMINOPEPTIDASE", JBIC. Journal of biological inorganic chemistry, 2(6), 1997, pp. 744-749

Abstract

Streptomyces griseus aminopeptidase has been characterized to have a dinuclear active site and to follow a dinuclear hydrolytic mechanism by means of activity assay, optical, and NMR spectroscopy. A sequentialbinding of Co2+ to the dinuclear sites in 20 mM Mes buffer at pH 6.1 has also been established. The results from these studies suggest thatthe two metal sites have a five-coordination sphere, with at least one coordinated His each. A di-Cu2+-substituted derivative of the enzymehas been prepared which exhibits a H-1 NMR spectrum with sharp hyperfine-shifted signals, again indicating the presence of a dinuclear active site. This H-1 NMR spectrum with sharp hyperfine-shifted features represents a first of its kind for a di-Cu2+ center in metalloproteins.

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Documento generato il 14/07/20 alle ore 03:37:19