Some kinetic and regulatory properties of the pea chloroplast pyruvate dehydrogenase complex

doi:10.1016/0005-2728(88)90034-5

Biochimica et Biophysica Acta (BBA) - Bioenergetics

Volume 933, Issue 2, 22 April 1988, Pages 269-275

https://doi.org/10.1016/0005-2728(88)90034-5 Get rights and content

Abstract

Results from initial rate studies of the pea chloroplast pyruvate dehydrogenase complex indicate a kinetic mechanism identical to that of bacterial and mitochondrial complexes. Interaction kinetics for all substrates resulted in parallel lines consistent with a multisite ping-pong mechanism. Product inhibition studies showed competitive inhibition between acetyl-coenzyme A and coenzyme A and between NADH and NAD. Uncompetitive inhibition was found between pyruvate and NADH or acetyl-coenzyme A, while noncompetitive inhibition was found for NAD or coenzyme A versus acetyl-coenzyme A and NADH, respectively. Activity of the chloroplast pyruvate dehydrogenase complex could be regulated by product inhibition. The plastid complex was more sensitive to the $NADH NAD$ ratio than the acetyl-coenzyme A/coenzyme A ratio. Additionally, there is the potential for fine regulation of chloroplast pyruvate dehydrogenase complex activity by intermediates and products of fatty acid synthesis.

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Citation Excerpt :
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^☆: This is journal report 10377 from the Missouri State Agricultural Experiment Station.

^∗∗: Present address: Biology Department, Davidson College, Davidson, NC 28036, U.S.A.

^∗∗∗: Present address: Seed Biosynthesis Research Unit, USDA, ARS, Northern Regional Research Center, 1815 North University Street, Peoria, IL 61604, U.S.A.

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Regular paperSome kinetic and regulatory properties of the pea chloroplast pyruvate dehydrogenase complex☆

Abstract

Biochimie

Trends Biochem. Sci.

Biochem. Biophys. Res. Commun.

Plant Sci. Lett.

Biochim. Biophys. Acta

Arch. Biochem. Biophys.

Arch. Biochem. Biophys.

J. Biol. Chem.

J. Biol. Chem.

Arch. Biochem. Biophys.

J. Plant Physiol.

J. Biol. Chem.

Curr. Top. Cell. Reg.

Arch. Biochem. Biophys.

Arch. Biochem. Biophys.

Acc. Chem. Res.

Methods Enzymol.

Plant Physiol.

Z. Naturforsch.

Z. Naturforsch.

Regular paper
Some kinetic and regulatory properties of the pea chloroplast pyruvate dehydrogenase complex☆