Physiological substrates of human aldose and aldehyde reductases

Advances in Experimental Medicine and Biology

Volumn 414, Issue , 1997, Pages 491-497

  Vander Jagt, David L ^a   Torres, Jose E ^a   Hunsaker, Lucy A ^a   Deck, Lorraine M ^a   Royer, Robert E ^a  

^a UNIVERSITY OF NEW MEXICO SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALDEHYDE REDUCTASE; MALONALDEHYDE;

BINDING AFFINITY; BINDING KINETICS; CONFERENCE PAPER; ENZYME KINETICS; ENZYME SPECIFICITY; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; HUMAN; HUMAN CELL; PRIORITY JOURNAL; REACTION ANALYSIS;

ALDEHYDE REDUCTASE; ALDEHYDES; HUMANS; KINETICS; PHENYLGLYOXAL; SUBSTRATE SPECIFICITY;

EID: 0030901882     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: None     Document Type: Conference Paper

References (36)

1. Barski, O.A., Gabbay, K.H., Grimshaw, C.E. and Bohren, K.M.: Mechanism of human aldehyde reductase: Characterization of the active site pocket. Biochemistry 34(1995) 11264-11275.
2. Bohren, K.M., Grimshaw, C.E., Lai, C-J., Harrison, D.H., Ringe, D., Petsko, G.A. and Gabbay, K.H.: Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the reduction reaction of human aldose reductase: Enzyme kinetics and crystal structure of the Y48H mutant enzyme. Biochemistry 33 (1994) 2021-2032.
3. Bucala, R. and Cerami, A.: Advanced glycosylation: chemistry, biology and implications for diabetes and aging. Adv. Pharmacol. 23 (1992) 1-34.
4. Daly, A.K. and Mantle, T.J.: The kinetic mechanism of the major form of ox kidney aldehyde reductase with D-glucuronic acid. Biochem. J. 205 (1982) 381-388.
5. Davidson, W.S. and Flynn, T.G.: Kinetics and mechanism of aldehyde reductase from pig kidney. Biochem. J. 177 (1979) 595-601.
6. El-Kabbani, O., Judge, K., Ginell, S.L., Myles, D.A.A., DeLucas, L.J. and Flynn, T.G.: Structure of porcine aldehyde reductase holoenzyme. Nature Structural Biology 2 (1995) 687-692.
7. Esterbauer, H. and Weger, W.: Synthesis of homologous 4-hydroxy-2-alkenals II. Monatsh. Chem. 98 (1967) 1994-2000.
8. Esterbauer, H., Schaur, R.J. and Zollner, H.: Chemistry and biochemistry of 4-hydroxynonenal, malondialdehyde and related aldehydes. Free Radical Biol. Med. 11 (1991) 81-128.
9. Feather, M.S., Flynn, T.G., Munro, K.A., Kubisecki, T.J. and Walton, D.J.: Catalysis of reduction of carbohydrate 2-oxoaldehydes (osones) by mammalian aldose reductase and aldehyde reductase. Biochim. Biophys. Acta 1244 (1995) 10-16.
10. Glomb, M.A. and Monnier, V.M.: Mechanism of protein modification by glyoxal and glycoaldehyde, reactive intermediates of the Mailard reaction. J. Biol. Chem. 270 (1995) 10017-10026.
11. Grimshaw, C.E.: Aldose reductase: Model for a new paradigm of enzymic perfection in detoxification catalysis. Biochemistry 31 (1992) 10139-10145.
12. Grimshaw, C.E. and Mather, E.J.: Immunoquantitation of aldose reductase in human tissues. Anal. Biochem. 176 (1989) 66-71.
13. Grimshaw, C.E., Shahbaz, M. and Putney, C.G.: Mechanistic basis for non-linear kinetics of aldehyde reduction catalyzed by aldose reductase. Biochemistry 29 (1990) 9947-9955.
14. Hirsch, J., Petrokova, E. and Feather, M.S.: The reaction of some dicarbonyl sugars with aminoguanidine. Carbohydrate Res. 232 (1992) 125-130.
15. Kador, P.F. and Kinoshita, J.H.: Role of aldose reductase in the development of diabetes- associated complications. Am. J. Med. 79 (1985) 8-12.
16. Knecht, K.J., Feather, M.S. and Baynes, J.W.: Detection of 3-deoxyfructose and 3- deoxyglucosone in human urine and plasma: evidence for intermediate stages of the Maillard reaction in vivo. Arch. Biochem. Biophys. 294 (1992) 130-137.
17. Kubisecki, T.J., Hyndman, D.J., Morjana, N.A. and Flynn, T.G.: Studies of pig muscle aldose reductase . Kinetic mechanism and evidence for a slow conformational change upon coenzyme binding. J. Biol. Chem. 267 (1992) 6510-6517.
18. Marnett, L.J. and Tuttle, M.A.: Comparison of the mutagenicities of malondialdehyde and the side products formed during its chemical synthesis. Cancer Res. 40 (1980) 276-282.
19. Matsuura, K., Deyashiki, Y., Bunai, Y, Ohya, I. and Hara, A.: Aldose reductase is a major reductase for isocaproaldehyde, a product of side-chain cleavage of cholesterol, in human and animal adrenal glands. Arch. Biochem. Biophys. 328 (1996) 265-271.
20. Mitchell, D.Y. and Petersen, D.R.: Inhibition of rat hepatic mitochondrial aldehyde dehydrogenase-mediated acetaldehyde oxidation by trans-4-hydroxy-2-nonenal. Hepatology 13 (1991) 728-734.
21. Petrash, J.M., Tarle, I., Wilson, D.K. and Quiocho, F.A.: Aldose reductase catalysis and crystallography. Insights from recent advances in enzyme structure and function. Diabetes 43 (1994) 955-959.
22. Rondeau, J-M., Tete-Favier, F., Podjarny, A., Reymann, J-M., Barth, P., Biellmann, J-F. and Moras, D.: Novel NADPH-binding domain revealed by the crystal structure of aldose reductase. Nature 355 (1992) 469-472.
23. Robinson, B., Hunsaker, L.A., Stangebye, L.A. and Vander Jagt, D.L.: Aldose and aldehyde reductases from human kidney cortex and medulla. Biochim. Biophys. Acta 1203 (1993) 260-266.
24. Tabakoff, B., Anderson, R. and Alivisatos, S.G.A.: Enzymatic reduction of "biogenic" aldehydes in brain. Mol. Pharmacol. 9 (1973) 428-437.
25. Turner, A.J. and Tipton, K.F.: The characterization of two reduced nicotinamide-adenine dinucleotide phosphate-linked aldehyde reductases from pig brain. Biochem. J. 130 (1972) 765-772.
26. Vander Jagt, D.L., Han, L-P and Lehman, C.H.: Effects of substituents on the rates of disproportionation of substituted phenylglyoxals in alkaline solution. J. Org. Chem. (1972) 4100-4104.
27. Vander Jagt, D.L.: The Glyoxalase System, in Glutathione: Chemical, Biochemical, and Medical Aspects-Part A, D. Dolphin, R. Poulson, and O. Avramovic, eds., 1989, J. Wiley, New York, pp. 598-641.
28. Vander Jagt, D.L., Hunsaker, L.A., Robinson, B., Stangebye, L.A. and Deck, L.M.: Aldehyde and aldose reductases from human placenta. J. Biol. Chem. 265 (1990a) 10912-10918.
29. Vander Jagt, D.L., Robinson, B., Taylor, K.K. and Hunsaker, L.A.: Aldose reductase from human skeletal and heart muscle. J. Biol. Chem. 265 (1990b) 20982-20987.
30. Vander Jagt, D.L., Robinson, B., Taylor, K.K. and Hunsaker, L.A.: Reduction of trioses by NADPH-dependent aldo-keto reductases. Aldose reductase, methylglyoxal, and diabetic complications. J. Biol. Chem. 267 (1992) 4364-4369.
31. Vander Jagt, D.L., Hunsaker, L.A., Deck, L.M., Chamblee, B.B. and Royer, R.E.: Ketoaldehyde detoxification enzymes and protection against the Maillard reaction, in Maillard Reactions in Chemistry, Food, and Health, T.P. Labuza, G.A. Reineccius, V.M. Monnier, J. O'Brien, and J.W. Baynes, eds., 1994, The Royal Society of Chemistry, Cambridge, pp. 314-318.
32. Vander Jagt, D.L., Kolb, N.S., Vander Jagt, T.J., Chino, J., Martinez, F.J., Hunsaker, L.A. and Royer, R.E.: Substrate specificity of human aldose reductase: identification of 4- hydroxynonenal as an endogenous substrate. Biochim. Biophys. Acts 1249 (1995) 117-126.
33. Wermuth, B., Aldo-keto reductases, in: Enzymology of Carbonyl Metabolism 2: Aldehyde Dehydrogenase, Aldo-Keto Reductases, and Alcohol Dehydrogenase, T.G. Flynn and H. Weiner, eds., 1985, A.R. Liss, New York, pp. 209-230.
34. Wilson, D.K., Bohren, K.M., Gabbay, K.H. and Quiocho, F.A.: An unlikely sugar substrate site in the 1.65A structure of the human aldose reductase holoenzyme implicated in diabetic complications. Science 257 (1992) 81-84.
35. Wilson, D.K., Tarle, I., Petrash, J.M. and Quiocho, F.A.: Refined 1.8A structure of human aldose reductase complexed with the potent inhibitor zopolrestat. Proc. Natl. Acad. Sci. USA 90 (1993) 9847-9851.
36. Wirth, H-P. and Wermuth, B.: Immunochemical characterization of aldo-keto reductases from human tissues. FEBS Lett. 187 (1985) 280-282.