References
- Jez JM, Bennett MJ, Schlegel BP, et al. Jez JM, Bennett MJ, Schlegel BP, Lewis M, Penning TM. Comparative anatomy of the aldo-keto reductase superfamily. Biochem. J.1997;326 (Pt 3):625–636.
- Kallberg Y, Oppermann U, Jörnvall H, et al. Short-chain dehydrogenases/reductases (SDRs). Eur. J. Biochem.2002;269:4409–4417.
- Ueda S, Oda M, Imamura S, et al. Steady-state kinetic properties of 3α-hydroxysteroid dehydrogenase from Pseudomonas sp. B-0831: steroid substrate specificity and nucleotide cofactor dependency. J. Biol. Macromol..2004;4:23–28.
- Ueda S, Oda M, Imamura S, et al. Carbonyl reductase activity of a pluripotent enzyme, 3α-hydroxysteroid dehydrogenase from Pseudomonas sp. B-0831. J. Biol. Macromol.2004;4:29–32.
- Ueda S, Oda M, Imamura S, et al. Transient-phase kinetic studies on the nucleotide binding to 3α-hydroxysteroid dehydrogenase from Pseudomonas sp. B-0831 using fluorescence stopped-flow procedures. Eur. J. Biochem. 2004;271:1774–1780.
- Ueda S, Oda M, Imamura S, et al. Kinetic study of the enzymatic cycling reaction conducted with 3α-hydroxysteroid dehydrogenase in the presence of excessive thio-NAD+ and NADH. Anal. Biochem.2004;332:84–89.
- Kataoka S, Nakamura S, Ohkubo T, et al. Crystallization and preliminary X-ray analysis of the complex of NADH and 3α-hydroxysteroid dehydrogenase from Pseudomonas sp. B-0831. Acta Crystallogr. F. 2006;62:569–571.
- Nakamura S, Oda M, Kataoka S, et al. Apo- and holo-structures of 3α-hydroxysteroid dehydrogenase from Pseudomonas sp. B-0831. Loop-helix transition induced by coenzyme binding. J. Biol. Chem. 2006;281:31876–31884.
- Inaba S, Numoto N, Ogawa S, et al. Crystal structures and thermodynamic analysis reveal distinct mechanisms of CD28 phosphopeptide binding to the Src homology 2 (SH2) domains of three adaptor proteins. J. Biol. Chem.2017;292:1052–1060.
- Oda M, Inaba S, Kamiya N, et al. Structural and thermodynamic characterization of endo-1,3-β-glucanase: insights into the substrate recognition mechanism. BBA - Proteins and Proteomics. 2018;1866:415–425.
- Grimm C, Maser E, Möbus E, et al. The crystal structure of 3α-hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni shows a novel oligomerization pattern within the short chain dehydrogenase/reductase family. J. Biol. Chem. 2000;275:41333–41339.
- Hwang CC, Chang YH, Hsu CN, et al. Mechanistic roles of ser-114, tyr-155, and lys-159 in 3α-hydroxysteroid dehydrogenase/carbonyl reductase from comamonas testosteroni. J. Biol. Chem. 2005;280:3522–3528.
- Chang YH, Huang TJ, Chuang LY, et al. Role of S114 in the NADH-induced conformational change and catalysis of 3α-hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni. Biochim. Biophys. Acta. 2009;1794:1459–1466.
- Chang YH, Wang CZ, Chiu CC, et al. Contributions of active site residues to cofactor binding and catalysis of 3α-hydroxysteroid dehydrogenase/carbonyl reductase. Biochim. Biophys. Acta. 2010;1804:235–241.