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. 1985 Apr 15;227(2):621–627. doi: 10.1042/bj2270621

Kinetic studies with the low-Km aldehyde reductase from ox brain.

C M Ryle, K F Tipton
PMCID: PMC1144882  PMID: 3890832

Abstract

Initial-rate studies of the low-Km aldehyde reductase-catalysed reduction of pyridine-3-aldehyde by NADPH gave families of parallel double-reciprocal plots, consistent with a double-displacement mechanism being obeyed. Studies on the variation of the initial velocity with the concentration of a mixture of the two substrates were also consistent with a double-displacement mechanism. In contrast, the initial-rate data indicated that a sequential mechanism was followed when NADH was used as the coenzyme. Product-inhibition studies, however, indicated that a compulsory-order mechanism was followed in which NADPH bound before pyridine-3-aldehyde with a ternary complex being formed and the release of pyrid-3-ylcarbinol before NADP+. The apparently parallel double-reciprocal plots obtained in the initial-rate studies with NADPH and pyridine-3-aldehyde were thus attributed to the apparent dissociation constant for the binary complex between the enzyme and coenzyme being finite but very low.

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Selected References

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

  1. Boghosian R. A., McGuinness E. T. Pig brain aldose reductase: a kinetic study using the centrifugal fast analyzer. Int J Biochem. 1981;13(8):909–914. doi: 10.1016/0020-711x(81)90017-3. [DOI] [PubMed] [Google Scholar]
  2. Branlant G. Properties of an aldose reductase from pig lens. Comparative studies of an aldehyde reductase from pig lens. Eur J Biochem. 1982 Dec;129(1):99–104. doi: 10.1111/j.1432-1033.1982.tb07026.x. [DOI] [PubMed] [Google Scholar]
  3. Cleland W. W. The statistical analysis of enzyme kinetic data. Adv Enzymol Relat Areas Mol Biol. 1967;29:1–32. doi: 10.1002/9780470122747.ch1. [DOI] [PubMed] [Google Scholar]
  4. Cromlish J. A., Flynn T. G. Purification and characterization of two aldose reductase isoenzymes from rabbit muscle. J Biol Chem. 1983 Mar 10;258(5):3416–3424. [PubMed] [Google Scholar]
  5. Daly A. K., Mantle T. J. Purification and characterization of the multiple forms of aldehyde reductase in ox kidney. Biochem J. 1982 Aug 1;205(2):373–380. doi: 10.1042/bj2050373. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Davidson W. S., Flynn T. G. Compositional relatedness of aldehyde reductases from several species. J Mol Evol. 1979 Dec;14(4):251–258. doi: 10.1007/BF01732492. [DOI] [PubMed] [Google Scholar]
  7. Doughty C. C., Conrad S. M. A reaction mechanism for aldose reductase from lens. Biochim Biophys Acta. 1982 Nov 19;708(3):358–364. doi: 10.1016/0167-4838(82)90449-6. [DOI] [PubMed] [Google Scholar]
  8. FLORINI J. R., VESTLING C. S. Graphical determination of the dissociation constants for two-substrate enzyme systems. Biochim Biophys Acta. 1957 Sep;25(3):575–578. doi: 10.1016/0006-3002(57)90529-2. [DOI] [PubMed] [Google Scholar]
  9. Flynn T. G. Aldehyde reductases: monomeric NADPH-dependent oxidoreductases with multifunctional potential. Biochem Pharmacol. 1982 Sep 1;31(17):2705–2712. doi: 10.1016/0006-2952(82)90123-x. [DOI] [PubMed] [Google Scholar]
  10. Gabbay K. H. Hyperglycemia, polyol metabolism, and complications of diabetes mellitus. Annu Rev Med. 1975;26:521–536. doi: 10.1146/annurev.me.26.020175.002513. [DOI] [PubMed] [Google Scholar]
  11. Halder A. B., Crabbe M. J. Bovine lens aldehyde reductase (aldose reductase). Purification, kinetics and mechanism. Biochem J. 1984 Apr 1;219(1):33–39. doi: 10.1042/bj2190033. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Hara A., Deyashiki Y., Nakayama T., Sawada H. Isolation and characterization of multiforms of aldehyde reductase in chicken kidney. Eur J Biochem. 1983 Jun 1;133(1):207–214. doi: 10.1111/j.1432-1033.1983.tb07449.x. [DOI] [PubMed] [Google Scholar]
  13. Houslay M. D., Tipton K. F. The nature of the electrophoretically separable multiple forms of rat liver monoamine oxidase. Biochem J. 1973 Sep;135(1):173–186. doi: 10.1042/bj1350173. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. O'Brien M. M., Schofield P. J. Polyol-pathway enzymes of human brain. Partial purification and properties of aldose reductase and hexonate dehydrogenase. Biochem J. 1980 Apr 1;187(1):21–30. doi: 10.1042/bj1870021. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Pettersson G. Asymptotic properties of enzymatic rate equations of the Wong-Hanes type. Acta Chem Scand. 1970;24(4):1271–1274. doi: 10.3891/acta.chem.scand.24-1271. [DOI] [PubMed] [Google Scholar]
  16. Ryle C. M., Dowling T. G., Tipton K. F. Purification and properties of low-Km aldehyde reductase from ox brain. Biochim Biophys Acta. 1984 Dec 7;791(2):155–163. doi: 10.1016/0167-4838(84)90005-0. [DOI] [PubMed] [Google Scholar]
  17. Tipton K. F., Houslay M. D., Turner A. J. Metabolism of aldehydes in brain. Essays Neurochem Neuropharmacol. 1977;1:103–138. [PubMed] [Google Scholar]
  18. Toews C. J. The kinetics and reaction mechanism of the nicotinamide-adenine dinucleotide phosphate-specific glycerol dehydrogenase of rat skeletal muscle. Biochem J. 1967 Dec;105(3):1067–1073. doi: 10.1042/bj1051067. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Tulsiani D. R., Touster Resolution and partial characterization of two aldehyde reductases of mammalian liver. J Biol Chem. 1977 Apr 25;252(8):2545–2550. [PubMed] [Google Scholar]
  20. Turner A. J., Illingworth J. A., Tipton K. F. Simulation of biogenic amine metabolism in the brain. Biochem J. 1974 Nov;144(2):353–360. doi: 10.1042/bj1440353. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Turner A. J., Tipton K. F. The characterization of two reduced nicotinamide-adenine dinucleotide phosphate-linked aldehyde reductases from pig brain. Biochem J. 1972 Dec;130(3):765–772. doi: 10.1042/bj1300765. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. WILKINSON G. N. Statistical estimations in enzyme kinetics. Biochem J. 1961 Aug;80:324–332. doi: 10.1042/bj0800324. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Wermuth B., Bürgisser H., Bohren K., von Wartburg J. P. Purification and characterization of human-brain aldose reductase. Eur J Biochem. 1982 Oct;127(2):279–284. doi: 10.1111/j.1432-1033.1982.tb06867.x. [DOI] [PubMed] [Google Scholar]

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