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Titolo:
Vanadium(V) complexes in enzyme systems: aqueous chemistry, inhibition andmolecular modeling in inhibitor design
Autore:
Bhattacharyya, S; Tracey, AS;
Indirizzi:
Simon Fraser Univ, Dept Chem, Burnaby, BC V5A 1S6, Canada Simon Fraser Univ Burnaby BC Canada V5A 1S6 , Burnaby, BC V5A 1S6, Canada Simon Fraser Univ, Inst Biochem & Mol Biol, Burnaby, BC V5A 1S6, Canada Simon Fraser Univ Burnaby BC Canada V5A 1S6 , Burnaby, BC V5A 1S6, Canada
Titolo Testata:
JOURNAL OF INORGANIC BIOCHEMISTRY
fascicolo: 1, volume: 85, anno: 2001,
pagine: 9 - 13
SICI:
0162-0134(200105)85:1<9:VCIESA>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-TYROSINE PHOSPHATASES; TRANSITION-STATE ANALOGS; INSULIN-RECEPTOR KINASE; INTACT-CELLS; VANADATE; BIS(N,N-DIMETHYLHYDROXAMIDO)HYDROXOOXOVANADATE; N,N-DIMETHYLHYDROXYLAMINE; RIBONUCLEASE; OXYANIONS; LAR;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Physical, Chemical & Earth Sciences
Citazioni:
25
Recensione:
Indirizzi per estratti:
Indirizzo: Tracey, AS Simon Fraser Univ, Dept Chem, Burnaby, BC V5A 1S6, Canada SimonFraser Univ Burnaby BC Canada V5A 1S6 BC V5A 1S6, Canada
Citazione:
S. Bhattacharyya e A.S. Tracey, "Vanadium(V) complexes in enzyme systems: aqueous chemistry, inhibition andmolecular modeling in inhibitor design", J INORG BIO, 85(1), 2001, pp. 9-13

Abstract

Vanadate in aqueous solution is known to influence a number of enzyme-catalyzed reactions. Such effects are well known to carry over to living systems where numerous responses to the influence of vanadium have been well-documented; perhaps the most studied being the insulin-mimetic effect. Studies of the aqueous chemistry of vanadate provide an insight into the mechanismsby which vanadate affects enzyme systems and suggests methods for the elucidation of specific types of responses. Studies of the corresponding enzymes provide complementary information that suggests model vanadate systems bestudied and provides clues as to functional groups that might be utilized in the development of selective enzyme inhibition. The insulin-mimetic effect is thought by many workers to originate in the effectiveness of vanadiumas an inhibitor of protein tyrosine phosphatase (PTPase) activity. One, ormore PTPases regulate the phosphotyrosine levels of the insulin receptor kinase domain. Appropriate ligands allow modification of the reactivity and function of vanadate. For instance, although the complex, ((CH3)(2)NO)(2)V(O)OH, is not quite as good an inhibitor of PTPase activity as is vanadate, it is much more effective in cell cultures for increasing glucose transportand glycogen synthesis. Studies of the chemistry of this complex provide an explanation of the efficacy of this compound as a PTPase inhibitor that is supported by computer modeling studies. Computer calculations using X-raydata of known PTPases as a basis for homology modeling then suggests functionality that needs to be addressed in developing selective PTPase inhibitors. (C) 2001 Elsevier Science B.V. All rights reserved.

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Documento generato il 28/03/20 alle ore 23:16:46