Journal of Comparative Physiology B

, Volume 154, Issue 5, pp 443–448 | Cite as

Pressure-adaptive differences in NAD-dependent dehydrogenases of congeneric marine fishes living at different depths

  • Joseph F. Siebenaller


The pressure sensitivities of the apparent Michaelis constant of coenzyme were compared at 5°C for three NAD-dependent dehydrogenases purified from the white muscle of two congeneric fishes living at different depths.Sebastolobus altivelis adults are common between 550 and 1,300 m;S. alascanus adults between 180 and 440 m. Two isozymes of cytoplasmic malate dehydrogenase (MDH, EC, NAD+:l-malate oxidoreductase) and glyceraldehyde 3-phosphate dehydrogenase (GAPDH, EC, NAD+:d-glyceraldehyde 3-phosphate oxidoreductase [phosphorylating]) were compared. For these enzymes, the homologues fromS. alascanus were markedly sensitive to moderate hydrostatic pressures (Fig. 1). TheK m(NADH) ofS. alascanus MDH-1 and theK m(NAD+) ofS. alascanus GAPDG double between 1 and 68 atm and continue to increase at a slower rate up to 476 atm, the highest pressure tested. For MDH-2 ofS. alascanus, theK m(NADH) triples between 1 and 68 atm and increases at a slower rate to 340 atm; between 340 and 476 atm, theK m decreases slightly from the value at 340 atm. TheK m of coenzyme values are pressure-independent for the MDH-1 and GAPDH homologues ofS. altivelis up to 476 atm (Fig. 1). TheK m(NADH) of theS. altivelis MDH-2 is sensitive to pressure, but much less so than the homologue ofS. alascanus (Fig. 1). TheK m increases 63% between 1 and 68 atm and remains constant at this higher value at higher pressures up to 476 atm. The relative increases inK m values for theS. alascanus enzymes between 1 and 68 atm are large (Table 1). Higher pressures are not as effective in perturbing theK m of coenzyme values. Perturbation ofK m of coenzyme by moderate hydrostatic pressures (50–100 atm) may seriously impair the function of dehydrogenases ofS. alascanus at pressures experienced by the deeper-living congener in its habitat. The reduction of the pressure-sensitivity of theK m of coenzyme in NAD-dependent dehydrogenases may be an important and ubiquitous feature of adaptation to the deep sea.


NADH Hydrostatic Pressure Malate Dehydrogenase Oxamate Pressure Adaptation 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Amelunxen RE, Car DO (1975) Glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle. Methods Enzymol 41:264–267PubMedGoogle Scholar
  2. Atkinson DE (1977) Cellular energy metabolism and its regulation. Academic Press, New YorkGoogle Scholar
  3. Bailey GS, Wilson AC, Halver JE, Johnson CL (1970) Multiple forms of supernatant malate dehydrogenase in salmonid fishes. J Biol Chem 245:5927–5940PubMedGoogle Scholar
  4. Banaszak LJ, Bradshaw RA (1975) Malate dehydrogenase. In: Boyer PD (ed) The enzymes, vol 11. Academic, New York, pp 369–396Google Scholar
  5. Bergmeyer HU (1974) Methods of enzymatic analysis, vol 1. Academic Press, New YorkGoogle Scholar
  6. Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248–254PubMedCrossRefGoogle Scholar
  7. Emery KO (1960) The sea off southern California. Wiley, New YorkGoogle Scholar
  8. Everse J, Zoll EC, Kahan L, Kaplan NO (1971) Addition products of diphosphopyridine nucleotides with substrates of pyridine nucleotide-linked dehydrogenases. Bioorg Chem 1:207–233CrossRefGoogle Scholar
  9. Greaney GS, Somero GN (1980) Contributions of binding and catalytic rate constants to evolutionary modifications inK m of NADH for muscle-type (M4) lactate dehydrogenases. J Comp Physiol 137:115–121Google Scholar
  10. Harris H, Hopkinson DA (1976) Handbook of enzyme electrophoresis in human genetics. North Holland, AmsterdamGoogle Scholar
  11. Hubbs CL (1926) The supposed intergradation of the two species ofSebastolobus (A genus of Scorpaenoid fishes) of Western America. Amer Mus Novit 216:1–9Google Scholar
  12. Johnson FH, Eyring H, Stover BJ (1974) The theory of rate processes in biology and medicine. Wiley, New YorkGoogle Scholar
  13. Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685PubMedCrossRefGoogle Scholar
  14. Laidler KJ (1951) The influence of pressure on the rates of biological reactions. Arch Biochem 30:226–236PubMedGoogle Scholar
  15. Morild E (1977) Pressure variation on enzymatic reaction rates: yeast and liver alcohol dehydrogenase. Biophys Chem 6:351–362PubMedCrossRefGoogle Scholar
  16. Moser HG (1974) Development and distribution of juveniles ofSebastolobus (Pisces; Family Scorpaenidae). US Nat Mar Fish Serv Fish Bull 72:865–884Google Scholar
  17. Mustafa T, Moon TW, Hochachka PW (1971) Effects of pressure and temperatue on the catalytic and regulatory properties of muscle pyruvate kinase from an off-shore benthic fish. Am Zool 11:451–466Google Scholar
  18. Neuman RC, Kauzmann W, Zipp A (1973) Pressure dependence of weak acid ionizations in aqueous buffers. J Phys Chem 77:2687–2691CrossRefGoogle Scholar
  19. Peterson GL (1983) Determination of total protein. Methods Enzymol 91:95–119PubMedCrossRefGoogle Scholar
  20. Rossmann MG, Argos P (1978) The taxonomy of binding sites in proteins. Mol Cell Biochem 21:161–182PubMedCrossRefGoogle Scholar
  21. Schulz GE, Schirmer RH (1979) Principles of protein structure. Springer, New YorkGoogle Scholar
  22. Siebenaller JF (1978) Genetic variability in deep-sea fishes of the genusSebastolobus (Scorpaenidae). In: Battaglia B, Beardmore J (ed) Marine organisms: genetic, ecology and evolution. Plenum, New York, pp 95–122Google Scholar
  23. Siebenaller JF (1983) The pH-dependence of the effects of hydrostatic pressure on the M4-lactate dehydrogenase homologs of scorpaenid fishes. Mar Biol Lett 4:233–243Google Scholar
  24. Siebenaller JF (1984) Structural comparison of lactate dehydrogenase homologs differing in sensitivity to hydrostatic pressure. Biochim Biophys Acta (in press)Google Scholar
  25. Siebenaller JF, Somero GN (1978) Pressure-adaptive differences in lactate dehydrogenases of congeneric fishes living at different depths. Science 201:255–257PubMedCrossRefGoogle Scholar
  26. Siebenaller JF, Somero GN (1979) Pressure-adaptive differences in the binding and catalytic properties of muscle-type (M4) lactate dehydrogenases of shallow- and deep-living marine fishes. J Comp Physiol 129:295–300Google Scholar
  27. Siebenaller JF, Somero GN (1982) The maintenance of different enzyme activity levels in congeneric fishes living at different depths. Physiol Zool 55:171–179Google Scholar
  28. Somero GN, Siebenaller JF (1979) Inefficient lactate dehydrogenases of deep-sea fishes. Nature 282:100–102PubMedCrossRefGoogle Scholar
  29. Somero GN, Siebenaller JF, Hochachka PW (1983) Biochemical and physiological adaptations of deep-sea animals. In: Rowe GT (ed) The sea, vol 8. Wiley, New York, pp 261–330Google Scholar
  30. Tischler ME, Friedrichs D, Coll K, Williamson JR (1977) Pyridine nucleotide distributions and enzyme mass action ratios in hepatocytes from fed and starved rats. Arch Biochem Biophys 184:222–236PubMedCrossRefGoogle Scholar
  31. Torgerson PM, Drickamer HG, Weber G (1979) Inclusion complexes of poly-β-cyclodextrin: a model for pressure effects upon ligand-protein complexes. Biochem 18:3079–3083CrossRefGoogle Scholar
  32. Torgerson PM, Drickamer HG, Weber G (1980) Effect of hydrostatic pressure upon ethidium bromide association with transfer ribonucleic acid. Biochem 19:3957–3960CrossRefGoogle Scholar
  33. Velick SF, Furfine C (1963) Glyceraldehyde 3-phosphate dehydrogenase. In: Boyer PD, Lardy H, Myrback K (ed) The enzymes, vol 7. Academic, New York, pp 243–273Google Scholar
  34. Wheat TE, Whitt GS, Childers WF (1972) Linkage relationships between the homologous malate dehydrogenase loci in teleosts. Genetics 70:337–340PubMedGoogle Scholar
  35. Wilkinson GN (1961) Statistical estimations in enzyme kinetics. Biochem J 80:324–334PubMedGoogle Scholar
  36. Yancey PH, Somero GN (1978) Temperature dependence of intracellular pH: its role in the conservation of pyruvate apparentK m values of vertebrate lactate dehydrogenases. J Comp Physiol 125:129–134Google Scholar

Copyright information

© Springer-Verlag 1984

Authors and Affiliations

  • Joseph F. Siebenaller
    • 1
  1. 1.College of OceanographyOregon State University Marine Science CenterNewportUSA

Personalised recommendations