Abstract
Progress in the aldo-keto reductase field has been quite rapid since the solution of the 3-dimensional structure of aldose reductase (ALR2) by the French group (Rondeau et al., 1992) and the Baylor group (Wilson et al., 1992), with additional contributions from Washington University School of Medicine with BioCryst Pharmaceuticals (Borhani et al., 1992) and with Dr. Quiocho’s laboratory (Wilson et al., 1993). Most recently, a definitive assignment of the active site constellation of amino acid residues and their likely roles in the catalytic mechanism was established by the collaborative efforts of researchers at Baylor, Brandeis and The Whittier Institute (Harrison et al., 1994; Bohren et al., 1994).
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References
Appleman, J.R., Prendergast, N., Delcamp, T.J., Freisheim, J.H., and Blakely, R.L. (1988) Kinetics of formation and isomerization of Methotrexate complexes of recombinant human dihydrofolate reductase. J. Biol. Chem. 263:103004–103013.
Barshop, B.A., Wrenn, R.F., & Frieden, C. (1983) Analysis of numerical methods for computer simulation of kinetic processes: Development of KINSIM — A flexible, portable system. Anal. Biochem. 130:134–145.
Bhatnagar, A., Das, B., Gavva, S.R., Cook, P.F., and Srivastava, S.K. (1988) The kinetic mechanism of human placental aldose reductase and aldehyde reductase II. Arch. Biochem. Biophys. 261:264–274.
Bhatnagar, A., Liu, S.-Q., Ueno, N., Chakrabarti, B., and Srivastava, S.K. (1994) Human placental aldose reductase: Role of Cys-298 in substrate and inhibitor binding. Biochim. Biophys. Acta 1205:207–214.
Bohren, K.M., Page, J.L., Shankar, R., Henry, S.P., and Gabbay, K.H. (1991) Expression of human aldose and aldehyde reductase. Site-directed mutagenesis of a critical lysine 262. J. Biol. Chem. 266:24031–24037.
Bohren, K.M., Grimshaw, C.E., and Gabbay, K.H. (1992) Catalytic effectiveness of human aldose reductase. Critical role of C-terminal domain. J. Biol. Chem. 267:20965–20970.
Bohren, K.M., Grimshaw, C.E., Lai, C.-J., Harrison, D.A., Ringe, D., Petsko, G.A., and Gabbay, K.H. (1994) 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 33:2021–2032.
Borhani, D.W., Harter, T.M., and Petrash, J.M. (1992) The crystal structure of the aldose reductase-NADPH binary complex. J. Biol Chem. 267:24841–24847.
Cleland, W.W. (1975) Partition analysis and the concept of net rate constants as tools in enzyme kinetics. Biochemistry 14:3220–3224.
Cleland, W.W. (1979) Statistical analysis of enzyme kinetic data. Methods Enzymology 63:103–138.
Del Corso, A., Barsacchi, D., Giannessi, M., Tozzi, M.G., Camici, M., and Mura, U. (1989) Change in stereospecificity of bovine lens aldose reductase modified by oxidative stress. J. Biol. Chem. 264:17653–17655.
Ehrig, T., Bohren, K.M., Prendergast, F.G., and Gabbay, K.H. (1994) Mechanism of aldose reductase inhibition: Binding of NADP+7NADPH and Alrestatin-like inhibitors. Biochemistry 33:7157–7165.
Griffin, B.W, and McNatt, L.G. (1986) Characterization of the reduction of 3-acetylpyridine adenine dinu-cleotide phosphate by benzyl alcohol catalyzed by aldose reductase. Arch. Biochem. Biophys. 246:75–81.
Grimshaw, C.E., Shahbaz, M., Jahangiri, G., Putney, C.G., McKercher, S.R., and Mathur, E.J. (1989) Kinetic and structural effects of activation of bovine kidney aldose reductase. Biochemistry 28:5343–5353.
Grimshaw, C.E., Shahbaz, M., and Putney, C.G. (1990) Mechanistic basis for nonlinear kinetics of aldehyde reduction catalyzed by aldose reductase. Biochemistry 29:9947–9955.
Harrison, D.H., Bohren, K.M., Ringe, D., Petsko, G.A., and Gabbay, K.H. (1994) An anion binding site in human aldose reductase: Mechanistic implications for the binding of citrate, cacodylate and glucose 6-phosphate. Biochemistry 33:2011–2020.
Kubiseski, T.J., Hyndman, D.J., Morjana, N.A., and Flynn, T.G. (1992) Studies on pig muscle aldose reductase. Kinetic mechanism and evidence for a slow conformational change upon nucleotide binding. J. Biol. Chem. 267:6510–6517.
Liu, S.-Q., Bhatnagar, A., and Srivastava, S.K. (1992) Does Sorbinil bind to the substrate binding site of aldose reductase? Biochem. Pharmacol. 44:2427–2429.
Liu, S.-Q., Bhatnagar, A., and Srivastava, S.K. (1993) Bovine lens aldose reductase. pH-Dependence of steady-state kinetic parameters and nucleotide binding. J. Biol. Chem. 268:25494–25499.
Rondeau, J.-M., Tête-Favier, F., Podjarny, A., Reymann, J.-M., Barth, P., Biellmann, J.-F., and Moras, D. (1992) Novel NADPH-binding domain revealed by the crystal structure of aldose reductase. Nature 355:469–472.
Sato, S., and Kador, P.F. (1990) Inhibition of aldehyde reductase by aldose reductase inhibitors. Biochem. Pharmacol. 40:1033–1042.
Sekhar, V.C., and Plapp, B.V. (1988) Mechanism of binding of horse liver alcohol dehydrogenase and nicotinamide adenine dinucleotide. Biochemistry 27:5082–5088.
Sekhar, V.C., and Plapp, B.V. (1990) Rate constants for a mechanism including intermediates in the interconversion of ternary complexes for horse liver alcohol dehydrogenase. Biochemistry 29:4289–4295.
Srivastava, S.K., Hair, G.A., and Das, B. (1985) Activated and unactivated forms of human erythrocyte aldose reductase. Proc. Natl. Acad. Sci. USA 82:7222–7226.
Vander Jagt, D.L., and Hunsaker, L.A. (1993) Substrate specificity of reduced and oxidized forms of human aldose reductase. Adv. Exp. Med. Biol. 328:279–288.
Ward, W.H.J., Cook, P.N., Mirrlees, D.J., Brittain, D.R., Preston, J., Carey, F., Tuffin, D.P., and Howe, R. (1993) Inhibition of aldose reductase by (2,6-dimethylphenylsulphonyl)nitromethane: Possible implications for the nature of an inhibitor binding site and a cause of biphasic kinetics. Adv. Exp. Med. Biol. 328:301–311.
Wermuth, B. (1990) Inhibition of aldehyde reductase by carboxylic acids. Adv. Exp. Med. Biol. 284:197–204.
Wilson, D.K., Bohren, K.M., Gabbay, K.H., and Quiocho, F.A. (1992) An unlikely sugar substrate binding site in the 1.65 Å structure of human aldose reductase holoenzyme implicated in diabetic complications. Science 251:81–84.
Wilson, D.K., Tarle, I., Petrash, J.M., and Quiocho, F.A. (1993) Refined 1.8 Å structure of human aldose reductase complexed with the potent inhibitor Zopolrestat. Proc. Natl. Acad. Sci. USA 90:9847–9851.
Zimmerte, C.T., Patane, K., & Frieden, C (1987) Analysis of progress curves by simulations generated by numerical integration. Biochemistry 26:6545–6552
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Grimshaw, C.E., Lai, CJ. (1995). Stopped-Flow Studies of Human Aldose Reductase Reveal which Enzyme form Predominates During Steady-State Turnover in Either Reaction Direction. In: Weiner, H., Holmes, R.S., Wermuth, B. (eds) Enzymology and Molecular Biology of Carbonyl Metabolism 5. Advances in Experimental Medicine and Biology, vol 372. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1965-2_29
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