Structures important in mammalian 11β- and 17β-hydroxysteroid dehydrogenases
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[1] I. Tsigelny,et al. Adding a positive charge at residue 46 of Drosophila alcohol dehydrogenase increases cofactor specificity for NADP+ , 1994, FEBS letters.
[2] Michael E. Baker,et al. Sequence analysis of steroid- and prostaglandin-metabolizing enzymes: Application to understanding catalysis , 1994, Steroids.
[3] Xenobiotic Ketone Reductase. Purification and Properties of an NADPH-dependent Carbonyl Reductase from Human Brain , 1980 .
[4] M. Baker,et al. Site-specific mutagenesis of Drosophila alcohol dehydrogenase: evidence for involvement of tyrosine-152 and lysine-156 in catalysis. , 1993, Biochemistry.
[5] D. Ghosh,et al. The refined three-dimensional structure of 3α,20β-hydroxysteroid dehydrogenase and possible roles of the residues conserved in short-chain dehydrogenases , 1994 .
[6] J. L. Napoli,et al. Cloning of a cDNA for Liver Microsomal Retinol Dehydrogenase , 1995, The Journal of Biological Chemistry.
[7] G M Maggiora,et al. Energetics of the structure of the four-alpha-helix bundle in proteins. , 1988, Proceedings of the National Academy of Sciences of the United States of America.
[8] N. Xuong,et al. The crystallographic structure of a human dihydropteridine reductase NADH binary complex expressed in Escherichia coli by a cDNA constructed from its rat homologue. , 1994, The Journal of biological chemistry.
[9] I. Tsigelny,et al. Amino acids important in enzyme activity and dimer stability for Drosophila alcohol dehydrogenase. , 1995, The Biochemical journal.
[10] B. Wermuth. Purification and properties of an NADPH-dependent carbonyl reductase from human brain. Relationship to prostaglandin 9-ketoreductase and xenobiotic ketone reductase. , 1981, The Journal of biological chemistry.
[11] Z. Chen,et al. Role of aspartic acid 38 in the cofactor specificity of Drosophila alcohol dehydrogenase. , 1991, European journal of biochemistry.
[12] H. Erdjument-Bromage,et al. Molecular cloning and characterization of (R)-3-hydroxybutyrate dehydrogenase from human heart. , 1992, The Journal of biological chemistry.
[13] P. Terpstra,et al. Prediction of the Occurrence of the ADP-binding βαβ-fold in Proteins, Using an Amino Acid Sequence Fingerprint , 1986 .
[14] C. Branden,et al. Introduction to protein structure , 1991 .
[15] F. R. Salemme,et al. Structural and functional diversity in 4-α-helical proteins , 1980, Nature.
[16] K. O. Elliston,et al. Expression cloning and characterization of human 17 beta-hydroxysteroid dehydrogenase type 2, a microsomal enzyme possessing 20 alpha-hydroxysteroid dehydrogenase activity. , 1993, The Journal of biological chemistry.
[17] Z. Krozowski,et al. Cloning and tissue distribution of the human 1 lβ-hydroxysteroid dehydrogenase type 2 enzyme , 1994, Molecular and Cellular Endocrinology.
[18] G. Marfany,et al. Effect of site‐directed mutagenesis on conserved positions of Drosophila alcohol dehydrogenase , 1993, FEBS letters.
[19] S. Beverley,et al. A member of the aldoketo reductase family confers methotrexate resistance in Leishmania. , 1992, The Journal of biological chemistry.
[20] L. Ribas de Pouplana,et al. The active site architecture of a short-chain dehydrogenase defined by site-directed mutagenesis and structure modeling. , 1994, Biochemistry.
[21] H. Jörnvall,et al. Carboxyethyllysine in a protein: native carbonyl reductase/NADP(+)-dependent prostaglandin dehydrogenase. , 1993, Proceedings of the National Academy of Sciences of the United States of America.
[22] M Krook,et al. Characteristics of short-chain alcohol dehydrogenases and related enzymes. , 1991, European journal of biochemistry.
[23] P. White,et al. Tyr-179 and Lys-183 are essential for enzymatic activity of 11 beta-hydroxysteroid dehydrogenase. , 1992, Biochemical and biophysical research communications.
[24] S. Atrian,et al. Protein engineering of Drosophila alcohol dehydrogenase The hydroxyl group of Tyr152 is involved in the active site of the enzyme , 1992, FEBS letters.
[25] Michael E. Baker,et al. Genealogy of regulation of human sex and adrenal function, prostaglandin action, snapdragon and petunia flower colors, antibiotics, and nitrogen fixation: functional diversity from two ancestral dehydrogenases , 1991, Steroids.
[26] U. Hellman,et al. The Retinal Pigment Epithelial-specific 11-cis Retinol Dehydrogenase Belongs to the Family of Short Chain Alcohol Dehydrogenases (*) , 1995, The Journal of Biological Chemistry.
[27] N. Xuong,et al. Crystal structure of rat liver dihydropteridine reductase. , 1992, Proceedings of the National Academy of Sciences of the United States of America.
[28] M. Ouellette,et al. A novel antifolate resistance gene on the amplified H circle of Leishmania. , 1992, The EMBO journal.
[29] N L Harris,et al. Four helix bundle diversity in globular proteins. , 1994, Journal of molecular biology.
[30] K. O. Elliston,et al. Male pseudohermaphroditism caused by mutations of testicular 17β–hydroxysteroid dehydrogenase 3 , 1994, Nature Genetics.
[31] A. Lesk,et al. The relation between the divergence of sequence and structure in proteins. , 1986, The EMBO journal.
[32] M. Poutanen,et al. Site-directed mutagenesis of the putative active site of human 17 beta-hydroxysteroid dehydrogenase type 1. , 1994, The Biochemical journal.
[33] J M Whiteley,et al. Structural and mechanistic characteristics of dihydropteridine reductase: a member of the Tyr-(Xaa)3-Lys-containing family of reductases and dehydrogenases. , 1994, Proceedings of the National Academy of Sciences of the United States of America.
[34] M. Baker,et al. Protochlorophyllide reductase is homologous to human carbonyl reductase and pig 20 beta-hydroxysteroid dehydrogenase. , 1994, The Biochemical journal.
[35] R. Vihko,et al. Genomic organization and DNA sequences of human 17β‐hydroxysteroid dehydrogenase genes and flanking regions , 1992 .
[36] F E Cohen,et al. Modeling protein structures: construction and their applications , 1993, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.
[37] Z. Chen,et al. Site-directed mutagenesis of glycine-14 and two "critical" cysteinyl residues in Drosophila alcohol dehydrogenase. , 1990, Biochemistry.
[38] H. Tai,et al. Site-directed mutagenesis of the conserved tyrosine 151 of human placental NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase yields a catalytically inactive enzyme. , 1991, Biochemical and biophysical research communications.
[39] A. Place,et al. Partial correction of structural defects in alcohol dehydrogenase through interallelic complementation in Drosophila melanogaster. , 1987, Genetics.
[40] F. Leenders,et al. Molecular cloning and amino acid sequence of the porcine 17β‐estradiol dehydrogenase , 1994 .
[41] H. Jörnvall,et al. Three‐dimensional model of NAD+‐dependent 15‐hydroxyprostaglandin dehydrogenase and relationships to the NADP+‐dependent enzyme (carbonyl reductase) , 1993, FEBS letters.
[42] Z. Krozowski,et al. 11β-Hydroxysteroid dehydrogenase and the short-chain alcohol dehydrogenase (SCAD) superfamily , 1992, Molecular and Cellular Endocrinology.
[43] J. Greer,et al. Comparative modeling of homologous proteins. , 1991, Methods in enzymology.
[44] D. Thatcher. The complete amino acid sequence of three alcohol dehydrogenase alleloenzymes (AdhN-11, AdhS and AdhUF) from the fruitfly Drosophila melanogaster. , 1980, The Biochemical journal.
[45] D. Ghosh,et al. Three-dimensional structure of holo 3 alpha,20 beta-hydroxysteroid dehydrogenase: a member of a short-chain dehydrogenase family. , 1991, Proceedings of the National Academy of Sciences of the United States of America.
[46] R. Wierenga,et al. INTERACTION OF PYROPHOSPHATE MOIETIES WITH ALPHA-HELIXES IN DINUCLEOTIDE BINDING-PROTEINS , 1985 .
[47] M. Baker,et al. A common ancestor for human placental 17β‐hydroxysteroid dehydrogenase, Streptomyces coelicolor actIII protein, and Drosophila melanogaster alcohol dehydrogenase , 1990, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.
[48] W. Trommer,et al. Coenzyme binding by 3-hydroxybutyrate dehydrogenase, a lipid-requiring enzyme: lecithin acts as an allosteric modulator to enhance the affinity for coenzyme. , 1989, Biochemistry.