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Titolo:
L-butaneboronic acid binding to Aeromonas proteolytica aminopeptidase: A case of arrested development
Autore:
De Paola, CC; Bennett, B; Holz, RC; Ringe, D; Petsko, GA;
Indirizzi:
Brandeis Univ, Rosenstiel Basic Med Sci Res Ctr, Waltham, MA 02454 USA Brandeis Univ Waltham MA USA 02454 Med Sci Res Ctr, Waltham, MA 02454 USA Utah State Univ, Dept Chem & Biochem, Logan, UT 84322 USA Utah State UnivLogan UT USA 84322 pt Chem & Biochem, Logan, UT 84322 USA
Titolo Testata:
BIOCHEMISTRY
fascicolo: 28, volume: 38, anno: 1999,
pagine: 9048 - 9053
SICI:
0006-2960(19990713)38:28<9048:LABTAP>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANSITION-STATE-ANALOG; LENS LEUCINE AMINOPEPTIDASE; L-LEUCINEPHOSPHONIC ACID; 2-METAL ION MECHANISM; FREE R-VALUE; METHIONINE AMINOPEPTIDASE; PEPTIDE HYDROLYSIS; BORONIC ACIDS; INHIBITORS; CATALYSIS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
42
Recensione:
Indirizzi per estratti:
Indirizzo: Petsko, GA Brandeis Univ, Rosenstiel Basic Med Sci Res Ctr, MS029,415 South St, Waltham, MA 02454 USA Brandeis Univ MS029,415 South St Waltham MA USA02454 02454 USA
Citazione:
C.C. De Paola et al., "L-butaneboronic acid binding to Aeromonas proteolytica aminopeptidase: A case of arrested development", BIOCHEM, 38(28), 1999, pp. 9048-9053

Abstract

Hydrolases containing two metal ions connected by a bridging ligand catalyze reactions important in carcinogensis, tissue repair, post-translational modification, control and regulation of biochemical pathways, and protein degradation. The aminopeptidase from Aeromonas proteolytica serves as a paradigm for the study of such bridged bimetallic proteases since its three-dimensional structure is known to very high resolution and its catalytic reaction is amenable to spectroscopic examination. Herein, we report, the X-ray crystal structure at 1.9 Angstrom resolution of AAP complexed with 1-butaneboronic acid (BuBA). This structure suggests that this complex represents asnapshot of the proteolytic reaction in an arrested form between the Michaelis complex and the transition state. Comparison of-the structure with spectroscopic and other data allows us to conclude that the apparently structurally symmetrical dizinc site is actually asymmetric: electrostatically.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 13:06:40