Cited by 102Mitochondrial Function and PathologyBiochemical Acid Research StudiesEnzyme Structure and Function

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Role of Oxalacetate in the Regulation of Mammalian Succinate Dehydrogenase

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Ackrell, Brian A.C., Kearney, Edna B., Mayr, Maria·1974·Journal of Biological Chemistry

DOI 10.1016/s0021-9258(19)42790-7

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Abstract

Abstract In most procedures for the isolation of membrane-bound or soluble succinate dehydrogenase, the enzyme is obtained largely in the deactivated form. As judged by the quantity of oxalacetate enzymatically determined in perchlorate extracts, the deactivated form contains tightly bound oxalacetate in 1:1 proportion to the enzyme (equated with histidyl flavin content) in particles. A somewhat lower ratio has been obtained for soluble preparations of the enzyme. The oxalacetate is bound very tightly: it is not displaced by succinate or malonate in the cold, nor released by precipitation or gel exclusion of the enzyme, and it does not react with malate dehydrogenase. It is released, however, on denaturation of the enzyme with perchloric acid or under conditions which favor conversion of the enzyme to the activated form. If the enzyme is freed from oxalacetate by activation with bromide and gel exclusion, treatment of the oxalacetate-free fully active enzyme with very low concentrations of l- or d-malate or oxalacetate leads to deactivation and concomitant formation of tightly bound oxalacetate in the same molar ratio found in the enzyme as isolated from heart mitochondria. Dissociation of the complex formed in this manner requires the same experimental conditions as those needed for dissociation of the complex as found in the isolated enzyme. The activation energies for activation and for release of oxalacetate are the same but vary with the type of activator used. The first order rate constant for activation by a variety of agents is about twice that measured for the dissociation of tightly bound oxalacetate. Moreover, with some activators oxalacetate release shows a considerable lag behind recovery of catalytic activity. It is suggested that the presence of oxalacetate in the deactivated enzyme is not the cause of its lack of catalytic activity but a consequence of the deactivated conformation. Further observations are described which suggest that a deactivation-activation cycle may also occur in the absence of oxalacetate.

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Authors: Ackrell, B. A. C., Kearney, E. B., & Mayr, M.
Affiliations: San Francisco VA Medical Center (US)
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1974-04
Volume: 249
Issue: 7
Pages: 2021-2027
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1016/s0021-9258(19)42790-7
OpenAlex: W1558696651
Cited by: 102
References: 17
Citations by year: 2026: 1 · 2025: 1 · 2021: 3 · 2020: 3 · 2019: 3 · 2017: 1 · 2016: 2 · 2015: 2 · 2014: 2 · 2013: 4 · 2012: 6
FWCI: 3.64
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 16992 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Biochemical Acid Research Studies
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Keywords: succinate dehydrogenase, oxaloacetate, enzyme inactivation, enzyme activation, heart mitochondria, enzyme conformation, malate, enzyme regulation
MeSH terms: Allosteric Regulation, Animals, Bromides, Catalysis, Cattle, Electron Transport, Enzyme Activation, Flavins, Histidine, Hydrogen-Ion Concentration, Kinetics, Malates, Malonates, Mitochondria, Muscle, Myocardium, Osmolar Concentration, Oxaloacetates, Protein Binding, Protein Conformation, Solubility, Succinate Dehydrogenase, Thermodynamics

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Role of Oxalacetate in the Regulation of Mammalian Succinate Dehydrogenase

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