Catalytic mechanism of the primary human prostaglandin F2α synthase, aldo-keto reductase 1B1 - Prostaglandin D2 synthase activity in the absence of NADP(H)

FEBS Journal

Volumn 278, Issue 8, 2011, Pages 1288-1298

  Nagata, Nanae ^a   Kusakari, Yukiko ^b   Fukunishi, Yoshifumi ^c   Inoue, Tsuyoshi ^b   Urade, Yoshihiro ^a  

^a OSAKA BIOSCIENCE INSTITUTE   (Japan)

^b OSAKA UNIVERSITY   (Japan)

^c NATIONAL INSTITUTE OF ADVANCED INDUSTRIAL SCIENCE AND TECHNOLOGY AIST   (Japan)

Author keywords

aldo keto reductase; His; prostaglandin D2 synthase; prostaglandin F2 synthase; prostaglandin H2

Indexed keywords

ALDOKETOREDUCTASE 1B1; ALDOKETOREDUCTASE 1B3; ALDOKETOREDUCTASE 1B7; ALDOKETOREDUCTASE 1C3; ASPARTIC ACID; HISTIDINE; LYSINE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; PROSTAGLANDIN D2; PROSTAGLANDIN D2 SYNTHASE; PROSTAGLANDIN H2; PROSTAGLANDIN SYNTHASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; TYROSINE; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CONCENTRATION RESPONSE; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME KINETICS; ENZYME SPECIFICITY; HEAT TREATMENT; ISOMERIZATION; MOLECULAR DOCKING; PH; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS; X RAY CRYSTALLOGRAPHY;

ALCOHOL OXIDOREDUCTASES; ANIMALS; CATALYSIS; HUMANS; INTRAMOLECULAR OXIDOREDUCTASES; LIPOCALINS; MICE; MODELS, MOLECULAR; NADP;

EID: 79953686781     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2011.08049.x     Document Type: Article

References (39)

1. Penning TM, &, Drury JE, (2007) Human aldo-keto reductases: function, gene regulation, and single nucleotide polymorphisms. Arch Biochem Biophys 464, 241-250. (Pubitemid 47214569)
2. Jez JM, Flynn TG, &, Penning TM, (1997) A new nomenclature for the aldo-keto reductase superfamily. Biochem Pharmacol 54, 639-647. (Pubitemid 27404623)
3. Hoog SS, Pawlowski JE, Alzari PM, Penning TM, &, Lewis M, (1994) Three-dimensional structure of rat liver 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase: a member of the aldo-keto reductase superfamily. Proc Natl Acad Sci USA 91, 2517-2521.
4. 2 reductase provides insight into the catalytic mechanism of aldo-ketoreductases. J Biol Chem 280, 26371-26382. (Pubitemid 41024949)
5. Wilson DK, Bohren KM, Gabbay KH, &, Quiocho FA, (1992) An unlikely sugar substrate site in the 1.65 Å structure of the human aldose reductase holoenzyme implicated in diabetic complications. Science 257, 81-84.
6. Wilson DK, Nakano T, Petrash JM, &, Quiocho FA, (1995) 1.7 Å structure of FR-1, a fibroblast growth factor-induced member of the aldo-keto reductase family, complexed with coenzyme and inhibitor. Biochemistry 34, 14323-14330. (Pubitemid 3000699)
7. Petrash JM, (2004) All in the family: aldose reductase and closely related aldo-keto reductases. Cell Mol Life Sci 61, 737-749. (Pubitemid 38659658)
8. Kubiseski TJ, Hyndman DJ, Morjana NA, &, Flynn TG, (1992) Studies on pig muscle aldose reductase. Kinetic mechanism and evidence for a slow conformational change upon coenzyme binding. J Biol Chem 267, 6510-6517.
9. 2α synthase activities of aldo-keto reductase 1B1, 1B3 and 1B7. J Biochem 145, 161-168.
10. Watanabe K, (2002) Prostaglandin F synthase. Prostaglandins Other Lipid Mediat 68-69, 401-407. (Pubitemid 35247410)
11. 2α on aqueous humor dynamics in cynomolgus monkeys. Curr Eye Res 6, 1035-1044. (Pubitemid 17135271)
12. Weber PC, (1980) Renal prostaglandins, kidney function and essential hypertension. Contrib Nephrol 23, 83-92.
13. 2α and its analogues on hair regrowth and follicular melanogenesis in a murine model. Exp Dermatol 14, 323-328. (Pubitemid 40691653)
14. McCracken JA, Custer EE, &, Lamsa JC, (1999) Luteolysis: a neuroendocrine-mediated event. Physiol Rev 79, 263-323. (Pubitemid 29210923)
15. Bresson E, Boucher-Kovalik S, Chapdelaine P, Madore E, Harvey N, Laberge PY, Leboeuf M, &, Fortier MA, (2011) The human aldose reductase AKR1B1 qualifies as the primary prostaglandin F synthase in the endometrium. J Clin Endocrinol Metab 96, 210-219.
16. 2α synthase. J Biol Chem 285, 8880-8886.
17. 2, a novel biologically active prostaglandin. Adv Prostaglandin Thromboxane Leukot Res 15, 365-367.
18. 2. Purification and properties of prostaglandin F synthetase from bovine lung. J Biol Chem 260, 7035-7041. (Pubitemid 15016094)
19. Hayaishi O, Watanabe K, Fujii Y, Nakayama K, Ohkubo H, Kuramitsu S, Kagamiyama H, &, Nakanishi S, (1988) Prostaglandin F synthetase, a dual function enzyme. Prog Clin Biol Res 274, 577-587.
20. Watanabe K, Fujii Y, Nakayama K, Ohkubo H, Kuramitsu S, Kagamiyama H, Nakanishi S, &, Hayaishi O, (1988) Structural similarity of bovine lung prostaglandin F synthase to lens epsilon-crystallin of the European common frog. Proc Natl Acad Sci USA 85, 11-15.
21. 2α synthase in Trypanosoma brucei. J Exp Med 192, 1327-1338.
22. Kubata BK, Kabututu Z, Nozaki T, Munday CJ, Fukuzumi S, Ohkubo K, Lazarus M, Maruyama T, Martin SK, Duszenko M, et al. (2002) A key role for old yellow enzyme in the metabolism of drugs by Trypanosoma cruzi. J Exp Med 196, 1241-1251. (Pubitemid 35304189)
23. Moriuchi H, Koda N, Okuda-Ashitaka E, Daiyasu H, Ogasawara K, Toh H, Ito S, Woodward DF, &, Watanabe K, (2008) Molecular characterization of a novel type of prostamide/prostaglandin F synthase, belonging to the thioredoxin-like superfamily. J Biol Chem 283, 792-801.
24. Urade Y, Fujimoto N, &, Hayaishi O, (1985) Purification and characterization of rat brain prostaglandin D synthetase. J Biol Chem 260, 12410-12415. (Pubitemid 16233440)
25. Bohren KM, Grimshaw CE, Lai CJ, Harrison DH, Ringe D, Petsko GA, &, Gabbay KH, (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. (Pubitemid 24099596)
26. Tarle I, Borhani DW, Wilson DK, Quiocho FA, &, Petrash JM, (1993) Probing the active site of human aldose reductase. Site-directed mutagenesis of Asp-43, Tyr-48, Lys-77, and His-110. J Biol Chem 268, 25687-25693. (Pubitemid 23358181)
27. Fukunishi Y, Mikami Y, &, Nakamura H, (2005) Similarities among receptor pockets and among compounds: analysis and application to in silico ligand screening. J Mol Graph Model 24, 34-45. (Pubitemid 41318116)
28. Klimacek M, Szekely M, Griessler R, &, Nidetzky B, (2001) Exploring the active site of yeast xylose reductase by site-directed mutagenesis of sequence motifs characteristic of two dehydrogenase/reductase family types. FEBS Lett 500, 149-152. (Pubitemid 32611244)
29. Schlegel BP, Jez JM, &, Penning TM, (1998) Mutagenesis of 3 alpha-hydroxysteroid dehydrogenase reveals a 'push-pull' mechanism for proton transfer in aldo-keto reductases. Biochemistry 37, 3538-3548. (Pubitemid 28125582)
30. Lefrancois-Martinez AM, Bertherat J, Val P, Tournaire C, Gallo-Payet N, Hyndman D, Veyssiere G, Bertagna X, Jean C, &, Martinez A, (2004) Decreased expression of cyclic adenosine monophosphate-regulated aldose reductase (AKR1B1) is associated with malignancy in human sporadic adrenocortical tumors. J Clin Endocrinol Metab 89, 3010-3019. (Pubitemid 38766402)
31. Lefrancois-Martinez AM, Tournaire C, Martinez A, Berger M, Daoudal S, Tritsch D, Veyssiere G, &, Jean C, (1999) Product of side-chain cleavage of cholesterol, isocaproaldehyde, is an endogenous specific substrate of mouse vas deferens protein, an aldose reductase-like protein in adrenocortical cells. J Biol Chem 274, 32875-32880. (Pubitemid 129535323)
32. Irikura D, Aritake K, Nagata N, Maruyama T, Shimamoto S, &, Urade Y, (2009) Biochemical, functional, and pharmacological characterization of AT-56, an orally active and selective inhibitor of lipocalin-type prostaglandin D synthase. J Biol Chem 284, 7623-7630.
33. Jez JM, Schlegel BP, &, Penning TM, (1996) Characterization of the substrate binding site in rat liver 3alpha-hydroxysteroid/dihydrodiol dehydrogenase. The roles of tryptophans in ligand binding and protein fluorescence. J Biol Chem 271, 30190-30198. (Pubitemid 26389662)
34. Wang J, Wolf RM, Caldwell JW, Kollman PA, &, Case DA, (2004) Development and testing of a general amber force field. J Comput Chem 25, 1157-1174.
35. Fukunishi Y, Mikami Y, &, Nakamura H, (2003) The filling potential method: a method for estimating the free energy surface for protein-ligand docking. J Phys Chem B 107, 13201-13210.
36. Gasteiger J, &, Marsili M, (1980) Iterative partial equalization of orbital electronegativity-a rapid access to atomic charges. Tetrahedron 36, 3219-3228.
37. Gasteiger J, &, Marsili M, (1978) A new model for calculating atomic charges in molecules. Tetrahedron Lett 34, 3181-3184.
38. Case DA, Darden TA, Cheatham TEI, Simmerling CL, Wang J, Duke RE, Luo R, Merz KM, Wang B, Pearlman DA, et al. (2004) AMBER 8. University of California, San Francisco, CA.
39. DeLano WL, (2005) The case for open-source software in drug discovery. Drug Discov Today 10, 213-217.