Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1976 Nov 15;160(2):253–262. doi: 10.1042/bj1600253

Nicotinamide-adenine dinucleotide-linked "malic" enzyme in flight muscle of the tse-tse fly (Glossina) and other insects.

J B Hoek, D J Pearson, N K Olembo
PMCID: PMC1164231  PMID: 12751

Abstract

1. A high activity of NAD-linked "malic" enzyme was found in homogenates of flight muscle of different species of tse-tse fly (Glossina). The activity was the same as, or higher than, that of malate dehydrogenase and more than 20-fold that of NADP-linked "malic" enzyme. A similar enzyme was found in the flight muscle of all other insects investigated, but at much lower activities. 2. ACa2+-stimulated oxaloacetate decarboxylase activity was present in all insect flight-muscle preparations investigated, in constant proportion to the NAD-linked "malic" enzyme. 3. A partial purification of the NAD-linked "malic" enzyme from Glossina was effected by DEAE-cellulose chromatography, which separated the enzyme from malate dehydrogenase and NADP-linked "malic" enzyme, but not from oxaloacetate decarboxylase. 4. The intracellular localization of the NAD-linked "malic" enzyme was predominantly mitochondrial; latency studies suggested a localization in the mitochondrial matrix space. 5. Studies on the partially purified enzyme demonstrated that it had a pH optimum between 7.6 and 7.9. It required Mg2+ or Mn2+ for activity; Ca2+ was not effective. The maximum rate was the same with either cation, but the concentration of Mn2+ required was 100 times less than that of Mg2+. Acitivity with NADP was only 1-3% of that with NAD, unless very high (greater than 10mM) concentrations of Mn2+ were present. 6. It is suggested that the NAD-linked "malic" enzyme functions in the proline-oxidation pathway predominant in tse-tse fly flight muscle.

Full text

PDF
253

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Brosemer R. W., Veerabhadrappa P. S. Pathway of proline oxidation in insect flight muscle. Biochim Biophys Acta. 1965 Oct 25;110(1):102–112. doi: 10.1016/s0926-6593(65)80099-6. [DOI] [PubMed] [Google Scholar]
  2. Bursell E. Oxaloacetic carboxylase in flight musculature of the tsetse fly. Comp Biochem Physiol. 1965 Nov;16(3):259–266. doi: 10.1016/0010-406x(65)90323-3. [DOI] [PubMed] [Google Scholar]
  3. Bursell E. The conversion of glutamate to alanine in the tsetse fly (Glossina morsitans). Comp Biochem Physiol. 1967 Dec;23(3):825–829. doi: 10.1016/0010-406x(67)90344-1. [DOI] [PubMed] [Google Scholar]
  4. Crabtree B., Newsholme E. A. The activities of proline dehydrogenase, glutamate dehydrogenase, aspartate-oxoglutarate aminotransferase and alanine-oxoglutarate aminotransferase in some insect flight muscles. Biochem J. 1970 May;117(5):1019–1021. doi: 10.1042/bj1171019. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. DE DUVE C., PRESSMAN B. C., GIANETTO R., WATTIAUX R., APPELMANS F. Tissue fractionation studies. 6. Intracellular distribution patterns of enzymes in rat-liver tissue. Biochem J. 1955 Aug;60(4):604–617. doi: 10.1042/bj0600604. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Fodge D. W., Gracy R. W., Harris B. G. Studies on enzymes from parasitic helminths. I. Purification and physical properties of malic enzyme from the muscle tissue of Ascaris suum. Biochim Biophys Acta. 1972 May 12;268(2):271–284. doi: 10.1016/0005-2744(72)90322-1. [DOI] [PubMed] [Google Scholar]
  7. Frenkel R. Regulation and physiological functions of malic enzymes. Curr Top Cell Regul. 1975;9:157–181. doi: 10.1016/b978-0-12-152809-6.50012-3. [DOI] [PubMed] [Google Scholar]
  8. Hansford R. G., Johnson R. N. The nature and control of the tricarboxylate cycle in beetle flight muscle. Biochem J. 1975 Jun;148(3):389–401. doi: 10.1042/bj1480389. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. KORKES S., DEL CAMPILLO A., OCHOA S. Biosynthesis of dicarboxylic acids by carbon dioxide fixation. IV. Isolation and properties of an adaptive "malic" enzyme from Lactobacillus arabinosus. J Biol Chem. 1950 Dec;187(2):891–905. [PubMed] [Google Scholar]
  10. LEWIS S. E., PRICE G. M. Malic enzyme activity in blowfly muscle. Nature. 1956 May 5;177(4514):842–843. doi: 10.1038/177842a0. [DOI] [PubMed] [Google Scholar]
  11. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  12. Lin R. C., Davis E. J. Malic enzymes of rabbit heart mitochondria. Separation and comparison of some characteristics of a nicotinamide adenine dinucleotide-preferring and a nicotinamide adenine dinucleotide phosphate-specific enzyme. J Biol Chem. 1974 Jun 25;249(12):3867–3875. [PubMed] [Google Scholar]
  13. Macrae A. R. Isolation and properties of a 'malic' enzyme from cauliflower bud mitochondria. Biochem J. 1971 May;122(4):495–501. doi: 10.1042/bj1220495. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Norden D. A., Paterson D. J. Carbohydrate metabolism in flight muscle of the tsetse fly (Glossina) and the blowfly (Sarcophaga). Comp Biochem Physiol. 1969 Dec 1;31(5):819–827. doi: 10.1016/0010-406x(69)92082-9. [DOI] [PubMed] [Google Scholar]
  15. OCHOA S., STERN J. R., SCHNEIDER M. C. Enzymatic synthesis of citric acid. II. Crystalline condensing enzyme. J Biol Chem. 1951 Dec;193(2):691–702. [PubMed] [Google Scholar]
  16. SAZ H. J., HUBBARD J. A. The oxidative decarboxylation of malate by Ascaris lumbricoides. J Biol Chem. 1957 Apr;225(2):921–933. [PubMed] [Google Scholar]
  17. Sauer L. A. An NAD- and NADP-dependent malic enzyme with regulatory properties in rat liver and adrenal cortex mitochondrial fractions. Biochem Biophys Res Commun. 1973 Jan 23;50(2):524–531. doi: 10.1016/0006-291x(73)90871-1. [DOI] [PubMed] [Google Scholar]
  18. Sauer L. A. Mitochondrial NAD-dependent malic enzyme: a new regulatory enzyme. FEBS Lett. 1973 Jul 1;33(2):251–255. doi: 10.1016/0014-5793(73)80205-4. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES