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Titolo:
Influence of allosteric effectors on the kinetics and equilibrium binding of phosphoenolpyruvate (PEP) to phosphoenolpyruvate carboxylase (PEPC) fromZea mays
Autore:
Frank, J; Clarke, RJ; Vater, J; Holzwarth, JF;
Indirizzi:
Fritz Haber Inst, Max Planck Soc, D-14195 Berlin, Germany Fritz Haber Inst Berlin Germany D-14195 nck Soc, D-14195 Berlin, Germany Univ Sydney, Sch Chem, Sydney, NSW 2006, Australia Univ Sydney Sydney NSWAustralia 2006 h Chem, Sydney, NSW 2006, Australia Tech Univ Berlin, Max Volmer Inst Biophys Chem & Biochem, D-10587 Berlin, Germany Tech Univ Berlin Berlin Germany D-10587 Biochem, D-10587 Berlin, Germany
Titolo Testata:
BIOPHYSICAL CHEMISTRY
fascicolo: 1-2, volume: 92, anno: 2001,
pagine: 53 - 64
SICI:
0301-4622(20010830)92:1-2<53:IOAEOT>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
YEAST GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; NICOTINAMIDE-ADENINE DINUCLEOTIDE; CO-OPERATIVE BINDING; 40 DEGREESC; PH 8.5; MAIZE; RUBISCO; INVIVO;
Keywords:
phosphoenolpyruvate carboxylase (PEPC); kinetics of phosphoenolpyruvate binding; enzyme kinetics; allosteric enzyme regulation; fast reaction techniques;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Physical, Chemical & Earth Sciences
Citazioni:
30
Recensione:
Indirizzi per estratti:
Indirizzo: Frank, J Fritz Haber Inst, Max Planck Soc, Faradayweg 4-6, D-14195 Berlin,Germany Fritz Haber Inst Faradayweg 4-6 Berlin Germany D-14195 , Germany
Citazione:
J. Frank et al., "Influence of allosteric effectors on the kinetics and equilibrium binding of phosphoenolpyruvate (PEP) to phosphoenolpyruvate carboxylase (PEPC) fromZea mays", BIOPHYS CH, 92(1-2), 2001, pp. 53-64

Abstract

Phosphoenolpyruvate carboxylase (PEPC) the carbon dioxide processing enzyme of C-4 plants, shows the features of an allosteric enzyme. Allosteric activators such as D-glucose-6-phosphate and glycine increase the affinity of PEPC for its substrate PEP at pH 8.0 and pH 7.0. Allosteric inhibitors likeL-malate and L-aspartate predominantly decrease the affinity of the carboxylase for PEP at pH 7.0. This was demonstrated by determination of the enzymatic activity and stopped flow (SF) fluorimetry. The binding reaction of PEP to PEPC from Zea mays was measured using the fluorescence probe 2-p-toluidinonaphthalene-6-sulfonate (TNS). The kinetics are described by an allosteric mechanism with a fast reversible bimolecular binding step of PEP to a high affinity (tensed) form of PEPC, which is in equilibrium with its low affinity (relaxed) form. The influence of allosteric effectors on the conformational transition step is demonstrated in support of the description of the kinetics of PEPC by applying a concerted allosteric mechanism as introduced by Monod, Wyman and Changeux. In summary, we present data for the influence of allosteric activators on the kinetics of PEP binding to PEPC and onthe concentration dependence of the isomerisation reaction between two allosteric forms of PEPC. (C) 2001 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/10/20 alle ore 13:23:26