Abstract
The activity of the pI 5 isozyme of horse liver aldehyde dehydrogenase is markedly enhanced by some divalent metal ions (Ca, Mn, Mg), inhibited by others (Fe, Cu, Cd), totally inhibited by Hg, and not significantly affected by still others (Zn, Ni, Co). Steady-state kinetics show that with 0.5 mM Mg or Mn a 2-fold activation of the velocity measured at pH 7.5 occurs when propionaldehyde is the substrate. In the pre-steady state, the magnitude burst of NADH formulation is increased from 2 moles formed per mole of tetrameric enzyme to 4 moles formed in the presence of Mg. The stoichiometry of coenzyme (NADH, NAD, ε-NAD) binding is also increased from essentially 2 moles binding to 4 moles binding per mole enzyme in the presence of Mg. It appears that the enzyme exhibits half of the site reactivity in the absence of metal but has a full complement of catalytic sites in the presence.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Diwan, J. J., Daze, M., Richardson, R., and Aronson, D., 1979, Kinetics of Mg2+ flux into rat liver mitochondria, Biochemistry, 18: 2590
Eckfeldt, J., Mope, L., Takio, K., and Yonetani, T., 1976, Horse liver aldehyde dehydrogenase: Purification, characterization and localization of the two isozymes, J. Biol. Chem, 251: 236.
Feldman, R. I. and Weiner, H., 1972a, Horse liver aldehyde dehydrogenase. I. Purification and characterization, J. Biol. Chem., 247: 260.
Feldman, R. I. and Weiner, H., 1972b, Horse liver aldehyde dehydrogenase. II. Kinetics and mechanistic implications of the dehydrogenase and esterase activity., J. Biol. Chem. 247: 267
Venteicher, R., Mope, L., and Yonetani, T., 1977, Metal ion effectors of horse liver aldehyde dehydrogenase. In: “Alcohol and Aldehyde Metabolizing Systems,” Vol. II, R. G. Thurman et al., ed., Academic Press, New York.
Weiner, H., Brown, C. S., Sanny, C. G., and Hu, J. H. J., 1976, Activation and inhibitors of horse liver aldehyde dehydrogenase, Fed. Proc., 35: 1499.
Weiner, H., King, P., Hu, J. H. J., and Bensch, W. R., 1974, Mechanistic and enzymatic properties of liver aldehyde dehydrogenase. In: “Alcohol and Aldehyde Metabolizing Systems,” Vol. 1, R. G. Thurman et al., ed., Academic Press, New York.
Weiner, H., Hu, J. H. J., and Sanny, C. G., 1976, Rate limiting steps for the esterase and dehydrogenase reaction catalyzed by horse liver aldehyde dehydrogenase, J. Biol. Chem., 251: 3857.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1980 Springer Science+Business Media New York
About this chapter
Cite this chapter
Takahashi, K., Brown, C.S., Weiner, H. (1980). Mechanism of the Magnesium Ion Activation of the Catalytic Activity of Horse Liver Aldehyde Dehydrogenase. In: Thurman, R.G. (eds) Alcohol and Aldehyde Metabolizing Systems-IV. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-1419-7_19
Download citation
DOI: https://doi.org/10.1007/978-1-4757-1419-7_19
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4757-1421-0
Online ISBN: 978-1-4757-1419-7
eBook Packages: Springer Book Archive