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Titolo:
Structure of human cystathionine beta-synthase: a unique pyridoxal 5 '-phosphate-dependent heme protein
Autore:
Meier, M; Janosik, M; Kery, V; Kraus, JP; Burkhard, P;
Indirizzi:
Univ Basel, ME Muller Inst Struct Biol, Biozentrum, CH-4056 Basel, Switzerland Univ Basel Basel Switzerland CH-4056 zentrum, CH-4056 Basel, Switzerland Univ Colorado, Sch Med, Dept Pediat, Denver, CO 80262 USA Univ Colorado Denver CO USA 80262 Med, Dept Pediat, Denver, CO 80262 USA Univ Colorado, Sch Med, Dept Cellular & Struct Biol, Denver, CO 80262 USA Univ Colorado Denver CO USA 80262 lar & Struct Biol, Denver, CO 80262 USA
Titolo Testata:
EMBO JOURNAL
fascicolo: 15, volume: 20, anno: 2001,
pagine: 3910 - 3916
SICI:
0261-4189(20010801)20:15<3910:SOHCBA>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
O-ACETYLSERINE SULFHYDRYLASE; SALMONELLA-TYPHIMURIUM; 3-DIMENSIONAL STRUCTURE; TRYPTOPHAN SYNTHASE; CRYSTAL-STRUCTURE; HOMOCYSTINURIA; BINDING; TRANSSULFURATION; DEAMINASE; LIGAND;
Keywords:
cystathionine beta-synthase; cysteine biosynthesis; heme protein; pyridoxal 5 '-phosphate; X-ray crystal structure;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
34
Recensione:
Indirizzi per estratti:
Indirizzo: Burkhard, P Univ Basel, ME Muller Inst Struct Biol, Biozentrum, Klingelbergstr 70, CH-4056 Basel, Switzerland Univ Basel Klingelbergstr 70 Basel Switzerland CH-4056 erland
Citazione:
M. Meier et al., "Structure of human cystathionine beta-synthase: a unique pyridoxal 5 '-phosphate-dependent heme protein", EMBO J, 20(15), 2001, pp. 3910-3916

Abstract

Cystathionine beta -synthase (CBS) is a unique heme-containing enzyme thatcatalyzes a pyridoxal 5 ' -phosphate (PLP)-dependent condensation of serine and homocysteine to give cystathionine. Deficiency of CBS leads to homocystinuria, an inherited disease of sulfur metabolism characterized by increased levels of the toxic metabolite homocysteine. Here we present the X-ray crystal structure of a truncated form of the enzyme. CBS shares the same fold with O-acetylserine sulfhydrylase but it contains an additional N-terminal heme binding site. This heme binding motif together with a spatially adjacent oxidoreductase active site motif could explain the regulation of its enzyme activity by redox changes.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/09/20 alle ore 00:29:44