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Titolo:
REGULATION OF HEXOKINASE-I - CRYSTAL-STRUCTURE OF RECOMBINANT HUMAN BRAIN HEXOKINASE COMPLEXED WITH GLUCOSE AND PHOSPHATE
Autore:
ALESHIN AE; ZENG CB; BARTUNIK HD; FROMM HJ; HONZATKO RB;
Indirizzi:
IOWA STATE UNIV SCI & TECHNOL,DEPT BIOCHEM & BIOPHYS AMES IA 50011 IOWA STATE UNIV SCI & TECHNOL,DEPT BIOCHEM & BIOPHYS AMES IA 50011 DESY,MPG,ASMB,MAX PLANCK RES UNIT STRUCT MOL BIOL D-22603 HAMBURG GERMANY
Titolo Testata:
Journal of Molecular Biology
fascicolo: 2, volume: 282, anno: 1998,
pagine: 345 - 357
SICI:
0022-2836(1998)282:2<345:ROH-CO>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
C-TERMINAL HALVES; PERMEABILITY TRANSITION PORE; ADENYLATE TRANSLOCATOR; MITOCHONDRIAL PORIN; SITE; MACROMOLECULES; BINDING; PHOSPHORYLATION; PURIFICATION; MUTAGENESIS;
Keywords:
HEXOKINASE I; BRAIN HEXOKINASE; X-RAY STRUCTURE; GLYCOLYSIS; ALLOSTERIC ENZYME;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
47
Recensione:
Indirizzi per estratti:
Citazione:
A.E. Aleshin et al., "REGULATION OF HEXOKINASE-I - CRYSTAL-STRUCTURE OF RECOMBINANT HUMAN BRAIN HEXOKINASE COMPLEXED WITH GLUCOSE AND PHOSPHATE", Journal of Molecular Biology, 282(2), 1998, pp. 345-357

Abstract

Hexokinase I, the pacemaker of glycolysis in brain tissue and red blood cells, is comprised of two similar domains fused into a single polypeptide chain. The C-terminal half of hexokinase I is catalytically active, whereas the N-terminal half is necessary for the relief of product inhibition by phosphate. A crystalline complex of recombinant humanhexokinase I with glucose and phosphate (2.8 Angstrom resolution) reveals a single binding site for phosphate and glucose at the N-terminalhalf of the enzyme. Glucose and phosphate stabilize the N-terminal half in a closed conformation. Unexpectedly, glucose binds weakly to theC-terminal half of the enzyme and does not by itself stabilize a closed conformation. Evidently a stable, closed C-terminal half requires either ATP or glucose 6-phosphate along with glucose. The crystal structure here, in conjunction with other studies in crystallography and directed mutation, puts the phosphate regulatory site at the N-terminal half, the site of potent product inhibition at the C-terminal half, and a secondary site for the weak interaction of glucose 6-phosphate at the N-terminal half of the enzyme. The relevance of crystal structuresof hexokinase I to the properties of monomeric hexokinase I and oligomers of hexokinase I bound to the surface of mitochondria is discussed. (C) 1998 Academic Press.

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Documento generato il 19/09/20 alle ore 11:58:25