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PMID: 4133851 Published · ppublish English Comparative Study Journal Article

Structural and functional similarities between mitochondrial malate dehydrogenase and L-3-hydroxyacyl CoA dehydrogenase.

Noyes BE, Glatthaar BE, Garavelli JS, Bradshaw RA

Abstract

Pig heart mitochondrial malate dehydrogenase (EC 1.1.1.37), which has been obtained free of electrophoretic subforms, has been shown to have a molecular weight of 67,000 and to be composed of two polypeptide chains. Comparison of these and other properties, such as amino-acid composition, isoelectric point, and keto-substrate inhibition, with those of (L)-3-hydroxyaeyl CoA dehydrogenase (EC 1.1.1.35), another NAD(+)-dependent dehydrogenase of mitochondrial origin, suggests structural similarities of the type associated with proteins possessing common evolutionary origins. This conclusion is supported by immunological crossreactivity. In view of these observations, the dissimilarity in the stereospecificity of hydrogen transfer from cofactor to substrate catalyzed by the two enzymes is attributed to 180 degrees rotation in the binding orientation of the nicotinamide moiety of the NAD(+), rather than to gross differences in the geometry of the active site of the two enzymes.

MeSH Terms
Alcohol Oxidoreductases/analysis,metabolism Amino Acid Sequence Amino Acids/analysis Animals Coenzyme A Cross Reactions Cytoplasm/enzymology Epitopes Isoelectric Focusing Malate Dehydrogenase/analysis,metabolism Mitochondria, Muscle/enzymology Molecular Weight Myocardium/enzymology Precipitin Tests Protein Conformation Structure-Activity Relationship Swine
Chemicals
Amino Acids Epitopes Alcohol Oxidoreductases Malate Dehydrogenase Coenzyme A
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Noyes B E
Glatthaar B E
Garavelli J S
Bradshaw R A
References (36)
36 references, click to expand
  1. Factors affecting the reversible dissociation of dehydrogenases.
    Proc Natl Acad Sci U S A. 1965 May;53(5):1006-14 PMID: 4287963
  2. Structural studies of pig heart malate dehydrogenase.
    Nature. 1966 Apr 30;210(5035):489-91 PMID: 5960510
  3. Enzymatically active conformers of mitochondrial malate dehydrogenase.
    Proc Natl Acad Sci U S A. 1966 Aug;56(2):578-85 PMID: 5229979
  4. Purification and properties of tuna supernatant and mitochondrial malate dehydrogenases.
    Biochim Biophys Acta. 1967 May 16;139(1):1-15 PMID: 4962136
  5. Malate dehydrogenases. I. A survey of molecular size measured by gel filtration.
    Biochemistry. 1967 Feb;6(2):603-10 PMID: 6069046
  6. Evolution of structure and function of proteases.
    Science. 1967 Dec 29;158(3809):1638-44 PMID: 4862530
  7. A reappraisal of some structural features of bovine heart malate dehydrogenase.
    Biochem J. 1968 Oct;109(4):663-8 PMID: 5683513
  8. Heterogeneity of supernatant malate dehydrogenase.
    Biochim Biophys Acta. 1968 Aug 27;167(1):1-8 PMID: 5686293
  9. The structure, function, and evolution of alpha-lactalbumin.
    Brookhaven Symp Biol. 1968 Jun;21(1):139-54 PMID: 5719192
  10. A possible three-dimensional structure of bovine alpha-lactalbumin based on that of hen's egg-white lysozyme.
    J Mol Biol. 1969 May 28;42(1):65-86 PMID: 5817651
  11. Three-dimensional structure of tosyl-elastase.
    Nature. 1970 Feb 28;225(5235):811-6 PMID: 5415110
  12. Structure of lactate dehydrogenase at 2-8 A resolution.
    Nature. 1970 Sep 12;227(5263):1098-103 PMID: 5451100
  13. Identification of an essential, reactive histidine in pig heart mitochondrial malate dehydrogenase.
    Eur J Biochem. 1970 Sep;15(3):562-7 PMID: 5455667
  14. Selective chemical modification of malate dehydrogenase. N-ethylmaleimide modification of active center sulfhydryl residues.
    J Biol Chem. 1971 Sep 10;246(17):5491-7 PMID: 4328700
  15. Structure of crystalline -chymotrypsin. II. A preliminary report including a hypothesis for the activation mechanism.
    J Mol Biol. 1968 Jul 14;35(1):143-64 PMID: 5760561
  16. Homologies in serine proteinases.
    Philos Trans R Soc Lond B Biol Sci. 1970 Feb 12;257(813):77-87 PMID: 4399051
  17. Molecular weight studies on the supernatant malate dehydrogenase isolated from beef heart. Evidence for a proteolytic contaminant in the purified preparation.
    Biochim Biophys Acta. 1972 Jan 26;257(1):143-9 PMID: 5009824
  18. Nerve growth factor and insulin.
    Science. 1972 May 5;176(4034):482-8 PMID: 5032347
  19. Amino acid composition and subunit structure. Human placental 17 -estradiol dehydrogenase.
    Biochemistry. 1972 Jul 4;11(14):2699-703 PMID: 5045524
  20. The stereospecificity of nicotinamide-adenine dinucleotide-dependent oxidoreductases from plants.
    Biochem J. 1972 Apr;127(2):335-43 PMID: 4403953
  21. The crystal and molecular structure of DIP-inhibited bovine trypsin at2.7Angstrom resolution.
    Cold Spring Harb Symp Quant Biol. 1972;36:125-40 PMID: 4508129
  22. L-3-hydroxyacyl coenzyme A dehydrogenase from pig heart muscle. I. Purification and properties.
    J Biol Chem. 1973 May 10;248(9):3052-9 PMID: 4700451
  23. L-3-hydroxyacyl coenzyme A dehydrogenase from pig heart muscle. II. Subunit structure.
    J Biol Chem. 1973 May 10;248(9):3061-6 PMID: 4700452
  24. Polypeptide conformation of cytoplasmic malate dehydrogenase from an electron density map at 3.0 angstrom resolution.
    J Mol Biol. 1972 Dec 30;72(3):577-89 PMID: 4349759
  25. The preparation of the cytoplasmic and mitochondrial forms of malate dehydrogenase and aspartate aminotransferase from pig heart by a single procedure.
    Anal Biochem. 1974 Feb;57(2):432-51 PMID: 4819736
  26. Pyridine nucleotide transhydrogenase. VI. Mechanism and stereospecificity of the reaction in Pseudomonas fluorescens.
    J Biol Chem. 1955 Feb;212(2):941-52 PMID: 14353895
  27. Some molecular and kinetic properties of heart malic dehydrogenase.
    J Biol Chem. 1956 Jul;221(1):61-9 PMID: 13345798
  28. The enzymatic transfer of hydrogen. VII. The reaction catalyzed by beta-hydroxybutryl dehydrogenase.
    J Biol Chem. 1958 Sep;233(3):722-6 PMID: 13575444
  29. Properties of the two forms of malic dehydrogenase from beef heart.
    J Biol Chem. 1961 Jul;236:1980-5 PMID: 13708709
  30. Beef-heart malic dehydrogenases. I. Properties of the enzyme purified from extracts of acetone-dried powders.
    Biochim Biophys Acta. 1961 Nov 25;54:67-76 PMID: 13912628
  31. Properties of mitochondrial malate dehydrogenases.
    Biochim Biophys Acta. 1962 Jun 4;59:624-33 PMID: 13921031
  32. The use of cyanate for the determination of NH2-terminal residues in proteins.
    J Biol Chem. 1963 Jan;238:214-26 PMID: 13983448
  33. Physicochemical properties of pig and horse heart mitochondrial malate dehydrogenase.
    J Biol Chem. 1963 May;238:1861-8 PMID: 13984965
  34. Starch-gel electrophoresis of malate dehydrogenase.
    Biochim Biophys Acta. 1963 Jun 11;73:193-203 PMID: 13984966
  35. A MICRO-BIURET METHOD FOR ESTIMATING PROTEINS.
    Anal Biochem. 1964 Dec;9:401-10 PMID: 14239476
  36. [THE AMINO ACID COMPOSITION OF ISOZYMES OF LACTIC DEHYDROGENASES FROM HUMAN AND ANIMAL ORGANS].
    Biochem Z. 1964 Jul 8;340:80-94 PMID: 14317955
Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1974-04-00
Pages
1334-8
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC388222
Subset
IM
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