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Titolo:
Structural evidence that the methionyl aminopeptidase from Escherichia coli is a mononuclear metalloprotease
Autore:
Cosper, NJ; Dsouza, VM; Scott, RA; Holz, RC;
Indirizzi:
Utah State Univ, Dept Chem & Biochem, Logan, UT 84322 USA Utah State UnivLogan UT USA 84322 pt Chem & Biochem, Logan, UT 84322 USA Univ Georgia, Dept Chem, Athens, GA 30602 USA Univ Georgia Athens GA USA 30602 Georgia, Dept Chem, Athens, GA 30602 USA
Titolo Testata:
BIOCHEMISTRY
fascicolo: 44, volume: 40, anno: 2001,
pagine: 13302 - 13309
SICI:
0006-2960(20011106)40:44<13302:SETTMA>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
CARBOXYPEPTIDASE-A; AEROMONAS-PROTEOLYTICA; EUKARYOTIC CELLS; ACTIVE-SITE; MECHANISM; BINDING; ZINC; INHIBITION; FUMAGILLIN; ENZYME;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
43
Recensione:
Indirizzi per estratti:
Indirizzo: Holz, RC Utah State Univ, Dept Chem & Biochem, Logan, UT 84322 USA Utah State Univ Logan UT USA 84322 Biochem, Logan, UT 84322 USA
Citazione:
N.J. Cosper et al., "Structural evidence that the methionyl aminopeptidase from Escherichia coli is a mononuclear metalloprotease", BIOCHEM, 40(44), 2001, pp. 13302-13309

Abstract

The Co and Fe K-edge extended X-ray absorption fine structure (EXAFS) spectra of the methionyl aminopeptidase from Escherichia coli (EcMetAP) have been recorded in the presence of I and 2 equiv of either Co(II) or Fe(II) (i.e., [Co(II)_(EcMetAP)], [Co(II)Co(II)(EcMetAP)], [Fc(Il)_(EcMetAP)], and [Fe(II)Fe(II)(EcMetAP)]). The Fourier transformed data of both [Co(II)_(EcMetAP)] and [Co(Il)Co(Il)(EcMetAP)] are dominated by a peak at ca. 2.05 Angstrom, which can be fit assuming 5 light atom (N,O) scatterers at 2.04 Angstrom. Attempts to include a Co-Co interaction (in the 2.4-4.0 Angstrom range) in the curve-fitting parameters were unsuccessful. Inclusion of multiple-scattering contributions from the outer-shell atoms of a histidine-imidazole ring resulted in reasonable Debye-Waller factors for these contributions and a slight reduction in the goodness-of-fit value (f'). These data suggest that a dinuclear Co(II) center does not exist in EcMetAP and that the firstCo atom is located in the histidine-ligated side of the active site. The EXAFS data obtained for [Fe(II)_(EcMetAP)] and [Fe(II)Fe(II)(EcMetAP)] indicate that Fe(II) binds to EcMetAP in a similar site to Co(II). Since no X-ray crystallographic data are available for any Fe(II)-substituted EcMetAP enzyme, these data provide the first glimpse at the Fe(Il) active site of MetAP enzymes. In addition, the EXAFS data for [Co(II)Co(II)(EcMetAP)] incubated with the antiangiogenesis drug fumagillin are also presented.

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Documento generato il 01/12/20 alle ore 13:13:38