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  Influence of allosteric effectors on the kinetics and equilibrium binding of phosphoenolpyruvate (PEP) to phosphoenolpyruvate carboxylase (PEPC) from Zea mays

Frank, J., Clarke, R. J., Vater, J., & Holzwarth, J. F. (2001). Influence of allosteric effectors on the kinetics and equilibrium binding of phosphoenolpyruvate (PEP) to phosphoenolpyruvate carboxylase (PEPC) from Zea mays. Biophysical Chemistry, 92(1-2), 53-64. doi:10.1016/S0301-4622(01)00185-5.

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 Creators:
Frank, Joachim1, Author              
Clarke, Ronald J.2, Author
Vater, Joachim, Author
Holzwarth, Josef F.1, Author              
Affiliations:
1Physical Chemistry, Fritz Haber Institute, Max Planck Society, ou_634546              
2Max Planck Society, ou_persistent13              

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Free keywords: Phosphoenolpyruvate carboxylase (PEPC); Kinetics of phosphoenolpyruvate binding; Enzyme kinetics; Allosteric enzyme regulation; Fast reaction techniques
 Abstract: Phosphoenolpyruvate carboxylase (PEPC) the carbon dioxide processing enzyme of C4 plants, shows the features of an allosteric enzyme. Allosteric activators such as -glucose-6-phosphate and glycine increase the affinity of PEPC for its substrate PEP at pH 8.0 and pH 7.0. Allosteric inhibitors like -malate and -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 on the concentration dependence of the isomerisation reaction between two allosteric forms of PEPC.

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Language(s): eng - English
 Dates: 2001-06-042001-03-122001-06-072001-08-232001-09-30
 Publication Status: Published in print
 Pages: 12
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 289226
DOI: 10.1016/S0301-4622(01)00185-5
 Degree: -

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Title: Biophysical Chemistry
  Other : Biophys. Chem.
Source Genre: Journal
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Publ. Info: Amsterdam, Netherlands : Elsevier
Pages: 12 Volume / Issue: 92 (1-2) Sequence Number: - Start / End Page: 53 - 64 Identifier: ISSN: 0301-4622
CoNE: https://pure.mpg.de/cone/journals/resource/954925509389