Arginine 276 controls the directional preference of AKR1C9 (rat liver 3α-hydroxysteroid dehydrogenase) in human embryonic kidney 293 cells

Endocrinology

Volumn 147, Issue 4, 2006, Pages 1591-1597

  Papari Zareei, Mahboubeh ^a   Brandmaier, Andrew ^a   Auchus, Richard J ^a  

^a UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

3ALPHA HYDROXYSTEROID DEHYDROGENASE; ANDROSTANEDIOL; ANDROSTANOLONE; ARGININE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

AEROBIC METABOLISM; ANIMAL EXPERIMENT; ARTICLE; CATALYSIS; CELL CULTURE; CELL STRAIN HEK293; CHEMICAL REACTION; CONTROLLED STUDY; HUMAN; HUMAN CELL; KIDNEY CELL; MUTATION; NONHUMAN; PRIORITY JOURNAL; RAT; REDUCTION; SITE DIRECTED MUTAGENESIS; STEROID METABOLISM;

ANDROSTENEDIOL; ANIMALS; ARGININE; CELLS, CULTURED; DIHYDROTESTOSTERONE; HUMANS; KIDNEY; NADP; OXIDOREDUCTASES; RATS; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 33645498223     PISSN: 00137227     EISSN: 00137227     Source Type: Journal    
DOI: 10.1210/en.2005-1141     Document Type: Article

References (29)

1. Duax WL, Ghosh D, Pletnev V 2000 Steroid dehydrogenase structures, mechanism of action, and disease. Vitam Horm 58:121-148
2. Jornvall H, Persson B, Krook M, Atrian S, Gonzalez-Duarte R, Jeffery J, Ghosh D 1995 Short-chain dehydrogenases/reductases (SDR). Biochemistry 34:6003-6013
3. Jez JM, Penning TM 2001 The aldo-keto reductase (AKR) superfamily: an update. Chem Biol Interact 130-132:499-525
4. Miettinen MM, Mustonen MV, Poutanen MH, Isomaa VV, Vihko RK 1996 Human 17β-hydroxysteroid dehydrogenase type 1 and type 2 isoenzymes have opposite activities in cultured cells and characteristic cell- and tissue-specific expression. Biochem J 314:839-845
5. Luu-The V, Zhang Y, Poirier D, Labrie F 1995 Characteristics of human types 1, 2 and 3 17β-hydroxysteroid dehydrogenase activities: oxidation/reduction and inhibition. J Steroid Biochem Mol Biol 55:581-587
6. Tremblay Y, Ringler GE, Morel Y, Mohandas TK, Labrie F, Strauss III JF, Miller WL 1989 Regulation of the gene for estrogenic 17-ketosteroid reductase lying on chromosome 17cen®q25. J Biol Chem 264:20458-20462
7. Geissler WM, Davis DL, Wu L, Bradshaw KD, Patel S, Mendonça BB, Elliston KO, Wilson JD, Russell DW, Andersson S 1994 Male pseudohermaphroiditism caused by mutations of testicular 17β-hydroxysteroid dehydrogenase 3. Nat Genet 7:34-39
8. Wu L, Einstein M, Geissler WM, Chan HK, Ellison KO, Andersson S 1993 Expression cloning and characterization of human 17β-hydrosteroid dehydrogenase type 2, a microsomal enzyme possessing 20α-hydroxysteroid dehydrogenase activity. J Biol Chem 268:12964-12969
9. Khan N, Sharma KK, Andersson S, Auchus RJ 2004 Human 17β- hydroxysteroid dehydrogenases types 1, 2, and 3 catalyze bi-directional equilibrium reactions, rather than unidirectional metabolism, in HEK-293 cells. Arch Biochem Biophys 429:50-59
10. Agarwal AK, Auchus RJ 2005 Minireview: cellular redox state regulates hydroxysteroid dehydrogenase activity and intracellular hormone potency. Endocrinology 146:2531-2538
11. Veech RL, Eggleston LV, Krebs HA 1969 The redox state of free nicotinamide-adenine dinucleotide phosphate in the cytoplasm of rat liver. Biochem J 115:609-619
12. Williamson DH, Lund P, Krebs HA 1967 The redox state of free nicotinamide-adenine dinucleotide in the cytoplasm and mitochondria of rat liver. Biochem J 103:514-527
13. Rossmann MG, Ford GC, Watson HC, Banaszak LJ 1972 Molecular symmetry of glyceraldehyde-3-phosphate dehydrogenase. J Mol Biol 64:237-245
14. Duax WL, Pletnev V, Addlagatta A, Bruenn J, Weeks CM 2003 Rational proteomics I. Fingerprint identification and cofactor specificity in the short-chain oxidoreductase (SCOR) enzyme family. Proteins 53:931-943
15. Huang YW, Pineau I, Chang HJ, Azzi A, Bellemare V, Laberge S, Lin SX 2001 Critical residues for the specificity of cofactors and substrates in human estrogenic 17β-hydroxysteroid dehydrogenase 1: variants designed from the three-dimensional structure of the enzyme. Mol Endocrinol 15:2010-2020
16. Hoog SS, Pawlowski JE, Alzari PM, Penning TM, Lewis M 1994 Three-dimensional structure of rat liver 3α-hydroxysteroid/dihydrodiol dehydrogenase: a member of the aldo-keto reductase superfamily. Proc Natl Acad Sci USA 91:2517-2521
17. Ratnam K, Ma H, Penning TM 1999 The arginine 276 anchor for NADP(H) dictates fluorescence kinetic transients in 3α-hydroxysteroid dehydrogenase, a representative aldo-keto reductase. Biochemistry 38:7856-7864
18. Heredia VV, Penning TM 2004 Dissection of the physiological interconversion of 5α-DHT and 3α-diol by rat 3α-HSD via transient kinetics shows that the chemical step is rate-determining: effect of mutating cofactor and substrate-binding pocket residues on catalysis. Biochemistry 43:12028-12037
19. Agarwal AK 2003 Cortisol metabolism and visceral obesity: role of 11β-hydroxysteroid dehydrogenase type I enzyme and reduced co-factor NADPH. Endocr Res 29:411-418
20. Merker MP, Bongard RD, Kettenhofen NJ, Okamoto Y, Dawson CA 2002 Intracellular redox status affects transplasma membrane electron transport in pulmonary arterial endothelial cells. Am J Physiol Lung Cell Mol Physiol 282:L36-L43
21. Hyndman D, Bauman DR, Heredia VV, Penning TM 2003 The aldo-keto reductase superfamily homepage. Chem Biol Interact 143-144:621-631
22. Ghosh D, Wawrzak Z, Weeks CM, Duax WL, Erman M 1994 The refined three-dimensional structure of 3α, 20β-hydroxysteroid dehydrogenase and possible roles of the residues conserved in short-chain dehydrogenases. Structure 2:629-640
23. Ghosh D, Pletnev VZ, Zhu DW, Wawrzak Z, Duax WL, Pangborn W, Labrie F, Lin SX 1995 Structure of human estrogenic 17β-hydroxysteroid dehydrogenase at 2.20 Å resolution. Structure 3:503-513
24. Pletnev V, Weeks CM, Duax WL 2004 Rational proteomics II: Electrostatic nature of cofactor preference in the short-chain oxidoreductase (SCOR) enzyme family. Proteins 57:294-301
25. Thomas JL, Duax WL, Addlagatta A, Brandt S, Fuller RR, Norris W 2003 Structure/function relationships responsible for coenzyme specificity and the isomerase activity of human type 1 3β-hydroxysteroid dehydrogenase/ isomerase. J Biol Chem 278:35483-35490
26. Askonas LJ, Ricigliano JW, Penning TM 1991 The kinetic mechanism catalysed by homogeneous rat liver 3α-hydroxysteroid dehydrogenase. Evidence for binary and ternary dead-end complexes containing non-steroidal antiinflammatory drugs. Biochem J 278:835-841
27. Rizner TL, Lin HK, Peehl DM, Steckelbroeck S, Bauman DR, Penning TM 2003 Human type 3 3α-hydroxysteroid dehydrogenase (aldo-keto reductase 1C2) and androgen metabolism in prostate cells. Endocrinology 144:2922-2932
28. Penning TM, Burczynski ME, Jez JM, Hung CF, Lin HK, Ma H, Moore M, Palackal N, Ratnam K 2000 Human 3α-hydroxysteroid dehydrogenase isoforms (AKR1C1-AKR1C4) of the aldo-keto reductase superfamily: functional plasticity and tissue distribution reveals roles in the inactivation and formation of male and female sex hormones. Biochem J 351:67-77
29. Steckelbroeck S, Jin Y, Gopishetty S, Oyesanmi B, Penning TM 2004 Human cytosolic 3α-hydroxysteroid dehydrogenases of the aldo-keto reductase superfamily display significant 3β-hydroxysteroid dehydrogenase activity: implications for steroid hormone metabolism and action. J Biol Chem 279:10784-10795