The high resolution crystal structure of rat liver AKR7A1: Understanding the substrate specificites of the AKR7 family

Chemico-Biological Interactions

Volumn 143-144, Issue , 2003, Pages 289-297

  Kozma, Evelin ^a   Brown, Elaine ^a   Ellis, Elizabeth M ^b   Lapthorn, Adrian J ^a  

^a UNIVERSITY OF GLASGOW   (United Kingdom)

^b UNIVERSITY OF STRATHCLYDE   (United Kingdom)

Author keywords

AKR7; Crystal structure; Molecular modeling; Substrate specificity

Indexed keywords

AFLATOXIN B1 DIALDEHYDE; AFLATOXIN DIALDEHYDE REDUCTASE; ALDEHYDE; ALDEHYDE KETONE REDUCTASE; ARGININE; BENZALDEHYDE DERIVATIVE; CITRIC ACID; LIVER ENZYME; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; OXIDOREDUCTASE; PHTHALALDEHYDIC ACID; SUCCINIC SEMIALDEHYDE; UNCLASSIFIED DRUG;

CATALYSIS; CONFERENCE PAPER; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME KINETICS; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; MOLECULAR MODEL; NONHUMAN; PROTEIN FAMILY; RAT;

ALDEHYDE REDUCTASE; AMINO ACID SEQUENCE; ANIMALS; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; LIVER; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; RATS; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY;

EID: 0037330516     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0009-2797(02)00186-2     Document Type: Conference Paper

References (27)

1. Bohren K., Bullock B., Wermuth B., Gabbay K. The aldo-keto reductase superfamily. J. Biol. Chem. 264:1989;9547-9551.
2. Jez J.M., Flynn T.G., Penning T.M. A new nomenclature for the aldo-keto reductase superfamily. Biochem. Pharmacol. 54:1997;639-647.
3. Jez J.M., Penning T.M. The aldo-keto reductase (AKR) superfamily: an update. Chem.-Biol. Interact. 130:2001;499-525.
4. Rondeau J.M., Tete-Favier F., Podjarny A., Reymann J.M., Barth P., Biellman J.F., Moras D. Novel NADPH-binding domain revealed by the crystal structure of aldose reductase. Nature. 355:1992;469-472.
5. Wilson D.K., Bohren K.M., Gabbay K.H., Quiocho F.A. An unlikely sugar substrate site in the 1.65 Angstrom structure of the human aldose reductase holoenzyme implicated in diabetic complications. Science. 257:1992;81-84.
6. El-kabbani O., Judge K., Ginell S.L., Myles D.A.A., Delucas L.J., Flynn T.G. Structure of porcine aldehyde reductase holoenzyme. Nat. Struct. Biol. 2:1995;687-692.
7. Hoog S.S., Pawlowski J.E., Alzari P.M., Penning T.M., Lewis M. 3-Dimensional structure of rat-liver 3-alpha-hydroxysteroid dihydrodiol dehydrogenase - a member of the aldo-keto reductase superfamily. Proc. Natl. Acad. Sci. USA. 91:1994;2517-2521.
8. Hur E., Wilson D.K. The crystal structure of the GCY1 protein from S-cerevisiae suggests a divergent aldo-keto reductase catalytic mechanism. Chem.-Biol. Interact. 130:2001;527-536.
9. Khurana S., Powers D.B., Anderson S., Blaber M. Crystal structure of 2,3-diketo-D-gluconic acid reductase A complexed with NADPH at 2.1-A resolution. Proc. Natl. Acad. Sci. USA. 95:1998;6768-6773.
10. Gulbis J.M., Mann S., MacKinnon R. Structure of a voltage-dependent K+ channel beta subunit. Cell. 97:1999;943-952.
11. 1 is expressed in rat liver during carcinogenesis and following the administration of an antioxidant. Biochem. J. 292:1993;13-18.
12. Hayes J.D., Judah D.J., Neal G.E. Resistance to aflatoxin-B1 is associated with the expression of a novel aldo-keto reductase which has catalytic activity towards a cytotoxic aldehyde-containing metabolite of the toxin. Cancer Res. 53:1993;3887-3894.
13. 1 defines a subfamily of aldo-keto reductases. Proc. Natl. Acad. Sci. USA. 90:1993;10350-10354.
14. Ellis E.M., Hayes J.D. Substrate specificity of an aflatoxin-metabolizing aldehyde reductase. Biochem. J. 312:1995;535-541.
15. Kelly V.P., Ireland L.S., Ellis E.M., Hayes J.D. Purification from rat liver of a novel constitutively expressed member of the aldo-keto reductase 7 family that is widely distributed in extrahepatic tissues. Biochem. J. 348:2000;389-400.
16. 1 aldehyde reductase. Biochem. J. 332:1998;21-34.
17. 1-metabolising member of the aldo-keto reductase superfamily, AKR7A3. Carcinogenesis. 7:1999;1215-1223.
18. Hinshelwood A., McGarvie G., Ellis E. Characterisation of a novel mouse liver aldo-keto reductase AKR7A5. FEBS Lett. 523:2002;213-218.
19. Schaller M., Schaffhauser M., Sans N., Wermuth B. Cloning and expression of succinic semialdehyde reductase from human brain - Identity with aflatoxin B-1 aldehyde reductase. Eur. J. Biochem. 265:1999;1056-1060.
20. Kozma E., Brown E., Ellis E.M., Lapthorn A.J. The crystal structure of rat liver AKR7A1 - A dimeric member of the aldo-keto reductase superfamily. J. Biol. Chem. 277:2002;16285-16293.
21. Gulbis J.M., Zhou M., Mann S., MacKinnon R. Structure of the cytoplasmic beta subunit - T1 assembly of voltage dependent K+ channels. Science. 289:2000;123-127.
22. Perrakis A., Morris R., Lamzin V.S. Automated protein model building combined with iterative structure refinement. Nat. Struct. Biol. 6:1999;458-463.
23. Murshudov G.N., Vagin A.A., Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. Sect. D. 53:1997;240-255.
24. Kavanagh K.L., Klimacek M., Nidetzky B., Wilson D.K. The structure of apo and holo forms of xylose reductase, a dimeric aldo-keto reductase from Candida tenuis. Biochemistry. 41:2002;8785-8795.
25. Kelly V.P., Sherratt P.J., Crouch D.H., Hayes J.D. Novel homodimeric and heterodimeric rat gamma-hydroxybutyrate synthases that associate with the Golgi apparatus define a distinct subclass of aldo-keto reductase 7 family proteins. Biochem. J. 366:2002;847-861.
26. Nicholls A., Sharp K.A., Honig B. Protein folding and association - insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins. 11:1991;281-296.
27. Gouet P., Courcelle E., Stuart D.I., Metoz F. ESPript: multiple sequence alignments in PostScript. Bioinformatics. 15:1999;305-308.