1.3.1.20 A36D production by site-directed mutagenesis 684150 1.3.1.20 A36D shows a decreased kcat value compared to the wild type enzyme 684150 1.3.1.20 C145S same sensitivity to SH-reagents as wild-type 349250 1.3.1.20 C170A kinetically similar to wild-type 349257 1.3.1.20 C193S no sensitivity to SH-reagents remaining 349250 1.3.1.20 C217A 4fold increase in Km for 5alpha-androstan-3,17-dione and 2fold increase in Km for NADH 349257 1.3.1.20 C87S DD1 mutant 349261 1.3.1.20 D280A production by site-directed mutagenesis 684150 1.3.1.20 D280A shows a decreased kcat value compared to the wild type enzyme 684150 1.3.1.20 D50N low dehydrogenase activity 349250 1.3.1.20 F154A production by site-directed mutagenesis 684150 1.3.1.20 F154A shows a decreased kcat value compared to the wild type enzyme 684150 1.3.1.20 F279A production by site-directed mutagenesis 684150 1.3.1.20 F279A shows a decreased kcat value compared to the wild type enzyme 684150 1.3.1.20 F279A the mutation affects inhibition and substrate affinity 686023 1.3.1.20 H117Q increased reductase activity 349250 1.3.1.20 H76Q production by site-directed mutagenesis 684150 1.3.1.20 H76Q shows a decreased kcat value compared to the wild type enzyme 684150 1.3.1.20 H79Q production by site-directed mutagenesis 684150 1.3.1.20 H79Q shows a decreased kcat value compared to the wild type enzyme 684150 1.3.1.20 H79Q site-directed mutagenesis, moderate activity with 190fold increase in Km-value, inhibition by MgCl2 and potassium phosphate 286127 1.3.1.20 K84N low dehydrogenase activity, no remaining reductase activity 349250 1.3.1.20 K97M mutant shows almost complete abrogation in activity for D-xylose oxidation and NADP+, and very poor activity with camphorquinone reduction and NADPH 686023 1.3.1.20 K97M production by site-directed mutagenesis 684150 1.3.1.20 K97M shows a decreased kcat value compared to the wild type enzyme 684150 1.3.1.20 K97R mutant shows almost complete abrogation in activity for D-xylose oxidation and NADP+, and very poor activity with camphorquinone reduction and NADPH 686023 1.3.1.20 K97R production by site-directed mutagenesis 684150 1.3.1.20 K97R shows a decreased kcat value compared to the wild type enzyme 684150 1.3.1.20 L311V native mutant with C to G replacement in DNA at position 931 349252 1.3.1.20 L54V DD1 mutant, increase in activity towards (S)-indan-1-ol and bile-acids, increased Km for trans-benzene dihydrodiol 349261 1.3.1.20 additional information CDD1-4 mutant consisting of DD1 with C-terminal end of DD4 shows 10-37fold increase in Km for indan-1-ol and 1,2,3,4-tetrahydronaphth-1-ol and significantly decreased activity towards androstanes, higher activity with bile-acids and 5beta-steroid than DD1 349261 1.3.1.20 additional information CDD4-1 mutant consisting of DD4 with C-terminal end of DD1shows new stereospecificity toward indan-1-ol stereomers and increased Km-values with bile acids and 3-hydroxysteroids compared to DD4 349261 1.3.1.20 additional information constitutive overexpression of enzyme in 2008 cells leads to induction of cisplatin resistance. In cisplatin-resistant cell-line 2008/C13*, differential expression of enzyme and four more genes is found 656043 1.3.1.20 additional information knock down of enzyme isoform DHH1 expression by siRNA in CL-3 cells results in 1.4- to 2.2fold increase in DNA-benzo[a]pyrene adducts 673371 1.3.1.20 additional information overexpression of enzyme in lung adenocarcinoma cell lines results in a much higher resistance to doxorubicin, cisplatin and irradiation. Isoforms DDH2 and DDH1 transfectants show higher drug and radiation resistance than DDH3 transfectants 671358 1.3.1.20 additional information sequence analysis 349257 1.3.1.20 additional information sequence analysis reveals high sequence homology between dimeric mammalian dihydrodiol dehydrogenases, but no homology with monomeric or cis-dihydrodiol-specific enzymes 286127 1.3.1.20 Q172L DD1 mutant 349261 1.3.1.20 R148A activity and temperature stability are similar to the wild type enzyme 689972 1.3.1.20 R148A mutagenesis is performed using a QuickChange site-directed mutagenesis kit, dehydrogenase activity is comparable to that of the wild type 701119 1.3.1.20 R148A/R202A mutagenesis is performed using a QuickChange site-directedmutagenesis kit 701119 1.3.1.20 R148A/R202A very low activity, the Vmax value of the mutant enzyme is 3.7fold lower than the wild type enzyme, displays significant temperature sensitivity 689972 1.3.1.20 R170H DD1 mutant 349261 1.3.1.20 R202A activity and temperature stability are similar to the wild type enzyme 689972 1.3.1.20 R202A mutagenesis is performed using a QuickChange site-directed mutagenesis kit, dehydrogenase activity is comparable to that of the wild type 701119 1.3.1.20 R37A production by site-directed mutagenesis 684150 1.3.1.20 R37A shows a decreased kcat value compared to the wild type enzyme 684150 1.3.1.20 R37D production by site-directed mutagenesis 684150 1.3.1.20 R37D shows a decreased kcat value compared to the wild type enzyme 684150 1.3.1.20 R41A production by site-directed mutagenesis 684150 1.3.1.20 R41A shows a decreased kcat value compared to the wild type enzyme 684150 1.3.1.20 R41D production by site-directed mutagenesis 684150 1.3.1.20 R41D shows a decreased kcat value compared to the wild type enzyme 684150 1.3.1.20 R47H DD1 mutant 349261 1.3.1.20 S145C native mutant with C to G replacement in DNA at position 434, no significant effect on activity 349252 1.3.1.20 S145C/L311V constructed double mutant with 3 to 5fold decreased activity for xenobiotic and steroidal substrates 349252 1.3.1.20 T38V DD1 mutant 349261 1.3.1.20 V151M DD1 mutant 349261 1.3.1.20 W125A the mutation affects inhibition and substrate affinity 686023 1.3.1.20 W125Y production by site-directed mutagenesis 684150 1.3.1.20 W125Y shows a decreased kcat value compared to the wild type enzyme 684150 1.3.1.20 W254A production by site-directed mutagenesis 684150 1.3.1.20 W254A shows a decreased kcat value compared to the wild type enzyme 684150 1.3.1.20 W254A the mutation affects inhibition and substrate affinity 686023 1.3.1.20 W254Y production by site-directed mutagenesis 684150 1.3.1.20 W254Y shows a decreased kcat value compared to the wild type enzyme 684150 1.3.1.20 Y180F site-directed mutagenesis, very low activity 286127 1.3.1.20 Y55F very low dehydrogenase activity 349250 1.3.1.20 Y55H decreased dehydrogenase activity, significant increased in reductase activity 349250