The role of Cys-298 in aldose reductase function

Journal of Biological Chemistry

Volumn 286, Issue 8, 2011, Pages 6336-6344

  Balendiran, Ganesaratnam K ^a   Sawaya, Michael R ^b   Schwarz, Frederick P ^c   Ponniah, Gomathinayagam ^d   Cuckovich, Richard ^a   Verma, Malkhey ^e   Cascio, Duilio ^b  

^a YOUNGSTOWN STATE UNIVERSITY   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c NATIONAL INSTITUTE OF STANDARDS AND TECHNOLOGY   (United States)

^d MERCK RESEARCH LABORATORIES   (United States)

^e UNIVERSITY OF MANCHESTER   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ALDOSE REDUCTASE; BINDING CONSTANT; BINDING POCKETS; CATALYTIC RATES; HEAT CAPACITY CHANGE; ISOTHERMAL TITRATION CALORIMETRY; OXIDATIVE MODIFICATION; OXIDOREDUCTASES; REDUCED SENSITIVITY; SIDE CHAINS; SUGAR METABOLISM; SULFUR ATOMS; VARIOUS SUBSTRATES; WILD TYPES; X RAY CRYSTAL STRUCTURES;

AMINO ACIDS; HYDROGEN; HYDROGEN BONDS; OXYGEN; RATE CONSTANTS; SPECIFIC HEAT; SUGARS; SULFUR;

AMIDES;

ALDEHYDE REDUCTASE; CYSTEINE; NICOTINAMIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SERINE; TYROSINE;

AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; BINDING SITE; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME SUBSTRATE; HYDROGEN BOND; ISOTHERMAL TITRATION CALORIMETRY; MUTANT; OXIDATION; PRIORITY JOURNAL; WILD TYPE;

ALDEHYDE REDUCTASE; AMINO ACID SUBSTITUTION; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; CYSTEINE; DIABETES MELLITUS; ENZYME ACTIVATION; HUMANS; HYDROGEN BONDING; MUTATION, MISSENSE; NADP; OXIDATION-REDUCTION; PROTEIN STRUCTURE, TERTIARY;

EID: 79953195540     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.154195     Document Type: Article

References (39)

1. Flynn, T. G. (1982) Biochem. Pharmacol. 31, 2705-2712
2. Gabbay, K. H. (1973) N. Engl. J. Med. 288, 831-836
3. Jaspan, J. (1986) Drugs 32, 23-29
4. Greene, D. A., Lattimer, S. A., and Sima, A. A. (1987) N. Engl. J. Med. 316, 599-606
5. Kinoshita, J. H., and Nishimura, C. (1988) Diabetes Metab. Rev. 4, 323-337
6. Newfield, R. S., Polak, M., Marchase, R., and Czernichow, P. (1997) Diabetologia 40, B62-B64
7. Caprio, S., Wong, S., Alberti, K. G., and King, G. (1997) Diabetologia 40, B78-B82
8. Lorenzi, M. (2007) Exp. Diabetes Res. 2007, 61038
9. Das, B., and Srivastava, S. K. (1985) Diabetes 34, 1145-1151
10. Grimshaw, C. E., and Lai, C. J. (1996) Arch. Biochem. Biophys. 327, 89-97
11. Grimshaw, C. E., Shahbaz, M., Jahangiri, G., Putney, C. G., McKercher, S. R., and Mathur, E. J. (1989) Biochemistry 28, 5343-5353
12. Srivastava, S. K., Ansari, N. H., Hair, G. A., Awasthi, S., and Das, B. (1986) Metabolism 35, 114-118
13. Srivastava, S. K., Hair, G. A., and Das, B. (1985) Proc. Natl. Acad. Sci. U.S.A. 82, 7222-7226
14. Cappiello, M., Voltarelli, M., Cecconi, I., Vilardo, P. G., Dal Monte, M., Marini, I., Del Corso, A., Wilson, D. K., Quiocho, F. A., Petrash, J. M., and Mura, U. (1996) J. Biol. Chem. 271, 33539-33544
15. Dixit, B. L., Balendiran, G. K., Watowich, S. J., Srivastava, S., Ramana, K. V., Petrash, J. M., Bhatnagar, A., and Srivastava, S. K. (2000) J. Biol. Chem. 275, 21587-21595
16. Bohren, K. M., and Gabbay, K. H. (1993) Adv. Exp. Med. Biol. 328, 267-277
17. Petrash, J. M., Harter, T. M., Devine, C. S., Olins, P. O., Bhatnagar, A., Liu, S., and Srivastava, S. K. (1992) J. Biol. Chem. 267, 24833-24840
18. Srivastava, S., Chandra, A., Ansari, N. H., Srivastava, S. K., and Bhatnagar, A. (1998) Biochem. J. 329, 469-475
19. Grimshaw, C. E., Shahbaz, M., and Putney, C. G. (1990) Biochemistry 29, 9947-9955
20. Kubiseski, T. J., Hyndman, D. J., Morjana, N. A., and Flynn, T. G. (1992) J. Biol. Chem. 267, 6510-6517
21. Grimshaw, C. E., Bohren, K. M., Lai, C. J., and Gabbay, K. H. (1995) Biochemistry 34, 14356-14365
22. Del Corso, A., Camici, M., and Mura, U. (1987) Biochem. Biophys. Res. Comm. 148, 369-375
23. Bradford, M. M. (1976) Anal. Biochem. 72, 248-254
24. Nishimura, C., Yamaoka, T., Mizutani, M., Yamashita, K., Akera, T., and Tanimoto, T. (1991) Biochim. Biophys. Acta 1078, 171-178
25. Balendiran, G. K., and Rajkumar, B. (2005) Biochem. Pharmacol. 70, 1653-1663
26. Liu, S. Q., Bhatnagar, A., and Srivastava, S. K. (1992) Biochem. Pharmacol. 44, 2427-2429
27. Wiseman, T., Williston, S., Brandts, J. F., and Lin, L. N. (1989) Anal. Biochem. 179, 131-137
28. Otwinowski, Z., and Minor, W. (1997) Methods Enzymol. 276, 307-326
29. Kissinger, C. R., Gehlhaar, D. K., Smith, B. A., and Bouzida, D. (2001) Acta Crystallogr. D Biol. Crystallogr. 57, 1474-1479
30. Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J. S., Kuszewski, J., Nilges, M., Pannu, N. S., Read, R. J., Rice, L. M., Simonson, T., and Warren, G. L. (1998) Acta Crystallogr. D Biol. Crystallogr. 54, 905-921
31. Emsley, P., and Cowtan, K. (2004) Acta Crystallogr. D Biol. Crystallogr. 60, 2126-2132
32. Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997) Acta Crystallogr. D Biol. Crystallogr. 53, 240-255
33. Laskowski, R. A., McArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) J. Appl. Crystallogr. 26, 283-291
34. Colovos, C., and Yeates, T. O. (1993) Protein Sci. 2, 1511-1519
35. Lüthy, R., Bowie, J. U., and Eisenberg, D. (1992) Nature 356, 83-85
36. Wilson, D. K., Bohren, K. M., Gabbay, K. H., and Quiocho, F. A. (1992) Science 257, 81-84
37. Privalov, P. L., and Makhatadze, G. I. (1992) J. Mol. Biol. 224, 715-723
38. Spolar, R. S., Livingstone, J. R., and Record, M. T., Jr. (1992) Biochemistry 31, 3947-3955
39. Ippolito, J. A., Alexander, R. S., and Christianson, D. W. (1990) J. Mol. Biol. 215, 457-471