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Titolo:
Crystal structure of rat biliverdin reductase
Autore:
Kikuchi, A; Park, SY; Miyatake, H; Sun, DY; Sato, M; Yoshida, T; Shiro, Y;
Indirizzi:
RIKEN, Harima Inst, SPring 8, Sayo, Hyogo 6795148, Japan RIKEN Sayo HyogoJapan 6795148 Inst, SPring 8, Sayo, Hyogo 6795148, Japan Yamagata Univ, Sch Med, Cent Lab Res & Educ, Yamagata 9909585, Japan Yamagata Univ Yamagata Japan 9909585 Res & Educ, Yamagata 9909585, Japan
Titolo Testata:
NATURE STRUCTURAL BIOLOGY
fascicolo: 3, volume: 8, anno: 2001,
pagine: 221 - 225
SICI:
1072-8368(200103)8:3<221:CSORBR>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
IX-ALPHA REDUCTASE; 3-DIMENSIONAL STRUCTURE; BETA REDUCTASE; BILIRUBIN; PURIFICATION; BINDING; LIVER; SPECIFICITY; SUBSTRATE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
30
Recensione:
Indirizzi per estratti:
Indirizzo: Kikuchi, A RIKEN, Harima Inst, SPring 8, Sayo, Hyogo 6795148, Japan RIKENSayo Hyogo Japan 6795148 g 8, Sayo, Hyogo 6795148, Japan
Citazione:
A. Kikuchi et al., "Crystal structure of rat biliverdin reductase", NAT ST BIOL, 8(3), 2001, pp. 221-225

Abstract

Biliverdin reductase (BVR) is a soluble cytoplasmic enzyme that catalyzes the conversion of biliverdin to bilirubin using NADH or NADPH as electron donor. Bilirubin is a significant biological antioxidant, but it is also neurotoxic and the cause of kernicterus. In this study, we have determined thecrystal structure of rat BVR at 1.4 Angstrom resolution. The structure contains two domains: an N-terminal domain characteristic of a dinucleotide binding fold (Rossmann fold) and a C-terminal domain that is predominantly anantiparallel six-stranded beta -sheet. Based on this structure, we proposemodes of binding for NAD(P)H and biliverdin, and a possible mechanism for the enzyme.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 14/08/20 alle ore 16:56:15