1.1.1.71: alcohol dehydrogenase [NAD(P)+]
This is an abbreviated version!
For detailed information about alcohol dehydrogenase [NAD(P)+], go to the full flat file.
Word Map on EC 1.1.1.71
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1.1.1.71
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retinoids
-
thermoanaerobacter
-
all-trans-retinaldehyde
-
retinyl
-
ethanolicus
-
all-trans-retinol
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r-1-phenylethanol
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cyp26a1
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akr1b10
- 1.1.1.71
-
retinoids
- thermoanaerobacter
- all-trans-retinaldehyde
-
retinyl
-
ethanolicus
- all-trans-retinol
-
r-1-phenylethanol
-
cyp26a1
- akr1b10
Reaction
Synonyms
ADH, ADH12, ADH2, Adh319, AdhA, AdhE, alcohol dehydrogenase, aldehyde reductase (NADPH/NADH), DHRS3, HvADH2, HVO_B0071, NAD(P)+-dependent alcohol dehydrogenase, NAD(P)H-dependent ADH, NAD(P)H-dependent aldehyde reductase, NADPH-dependent ADHA, NADPH-dependent alcohol dehydrogenase, PH0743, PhADH, RADH, retinal reductase, retinal short-chain dehydrogenase/reductase member 3, retinaldehyde reductase, Retinol dehydrogenase, retinol-active alcohol dehydrogenase, retSDR1, TeSADH, TsAdh319, Tsib_0319, VNG_2617G, YqhD
ECTree
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Reference
Reference on EC 1.1.1.71 - alcohol dehydrogenase [NAD(P)+]
for references in articles please use BRENDA:EC1.1.1.71
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Hirschberg, D.; Cederlund, E.; Crosas, B.; Jonsson, A.; Tryggvason, S.; Farres, J.; Pares, X.; Bergmann, T.; Jörnvall, H.
N-terminal acetylation in a third protein family of vertebrate alcohol dehydrogenase/retinal reductase found through a proteomics approach in enzyme characterization
Cell. Mol. Life Sci.
58
1323-1326
2001
Gallus gallus
Korkhin, Y.; Kalb(Giloa), A.J.; Peretz, M.; Bogin, O.; Burstein, Y.; Frolow, F.
NADP-dependent bacterial alcohol dehydrogenases: crystal structure, cofactor-binding and cofactor specificity of the ADHs of Clostridium beijerinckii and Thermoanaerobacter brockii
J. Mol. Biol.
278
967-981
1998
Clostridium beijerinckii, Thermoanaerobacter brockii
Wales, M.R.; Fewson, C.A.
NADP-dependent alcohol dehydrogenases in bacteria and yeast: purification and partial characterization of the enzymes from Acinetobacter calcoaceticus and Saccharomyces cerevisiae
Microbiology
140
173-183
1994
Acinetobacter calcoaceticus, Bacillus subtilis, Bacillus subtilis NCIMB 3610, Escherichia coli, Escherichia coli ML30, Mycobacterium tuberculosis, Pseudomonas aeruginosa, Pseudomonas putida, Pseudomonas putida NCIMB 9494, Rhodococcus rhodochrous, Rhodococcus rhodochrous NCIMB 13259, Rhodotorula graminis, Rhodotorula graminis KGX 39, Saccharomyces cerevisiae, Saccharomyces cerevisiae D273-10B, Streptomyces rimosus, Streptomyces rimosus 4018
Brophy, P.M.; Crowley, P.; Barrett, J.
A novel NADPH/NADH-dependent aldehyde reduction enzyme isolated from the tapeworm Moniezia expansa
FEBS Lett.
263
305-307
1990
Moniezia expansa
Hiu, S.F.; Zhu, C.X.; Yan R.T.; Chen, J.S.
Butanol-ethanol dehydrogenase and butanol-ethanol-isopropanol dehydrogenase: different alcohol dehydrogenases in two strains of Clostridium beijerinckii (Clostridium butylicium)
Appl. Environ. Microbiol.
53
697-703
1987
Clostridium beijerinckii
Hatanaka, A.; Kajiwara, T.; Tomohiro, S.
Purification and properties of alcohol dehydrogenase from Leuconostoc mesenteroides
Agric. Biol. Chem.
38
1819-1833
1974
Leuconostoc mesenteroides, Leuconostoc mesenteroides IFO 3426
-
Rhodes, M.J.C.
Co-factor specificity of plant alcohol dehydrogenase
Phytochemistry
12
307-314
1973
Cucumis melo
-
Fidge, N.H.; Goodman, D.S.
The enzymatic reduction of retinal to retinol in rat intestine
J. Biol. Chem.
243
4372-4379
1968
Rattus norvegicus
Belyaeva, O.V.; Kedishvili, N.Y.
Human pancreas protein 2 (PAN2) has a retinal reductase activity and is ubiquitously expressed in human tissues
FEBS Lett.
531
489-493
2002
Homo sapiens (Q9HBH5)
Montesano, M.; Hyytiainen, H.; Wettstein, R.; Palva, E.T.
A novel potato defence-related alcohol:NADP+ oxidoreductase induced in response to Erwinia carotovora
Plant Mol. Biol.
52
177-189
2003
Solanum tuberosum (Q8H0L8)
Thomas, S.; Prabhu, R.; Balasubramanian, K.A.
Retinoid metabolism in the rat small intestine
Br. J. Nutr.
93
59-63
2005
Rattus norvegicus
Timpson, L.M.; Alsafadi, D.; Mac Donnchadha, C.; Liddell, S.; Sharkey, M.A.; Paradisi, F.
Characterization of alcohol dehydrogenase (ADH12) from Haloarcula marismortui, an extreme halophile from the Dead Sea
Extremophiles
16
57-66
2012
Haloarcula marismortui (Q5V676), Haloarcula marismortui
Lyashenko, A.V.; Bezsudnova, E.Y.; Gumerov, V.M.; Lashkov, A.A.; Mardanov, A.V.; Mikhailov, A.M.; Polyakov, K.M.; Popov, V.O.; Ravin, N.V.; Skryabin, K.G.; Zabolotniy, V.K.; Stekhanova, T.N.; Kovalchuk, M.V.
Expression, purification and crystallization of a thermostable short-chain alcohol dehydrogenase from the archaeon Thermococcus sibiricus
Acta Crystallogr. Sect. F
66
655-657
2010
Thermococcus sibiricus (C6A190), Thermococcus sibiricus DSM 12597 (C6A190)
Stekhanova, T.N.; Bezsudnova, E.Y.; Mardanov, A.V.; Gumerov, V.M.; Artemova, N.; Kleymenov, S.Y.; Popov, V.O.
Sodium chloride-induced modulation of the activity and thermal stability of short-chain oxidoreductase from the archaeon Thermococcus sibiricus
Appl. Biochem. Biotechnol.
171
1877-1889
2013
Thermococcus sibiricus (C6A190), Thermococcus sibiricus DSM 12597 (C6A190)
Stekhanova, T.N.; Mardanov, A.V.; Bezsudnova, E.Y.; Gumerov, V.M.; Ravin, N.V.; Skryabin, K.G.; Popov, V.O.
Characterization of a thermostable short-chain alcohol dehydrogenase from the hyperthermophilic archaeon Thermococcus sibiricus
Appl. Environ. Microbiol.
76
4096-4098
2010
Thermococcus sibiricus (C6A190), Thermococcus sibiricus, Thermococcus sibiricus DSM 12597 (C6A190)
Timpson, L.M.; Liliensiek, A.K.; Alsafadi, D.; Cassidy, J.; Sharkeym M.A.; Liddell, S.; Allers, T.; Paradisi, F.
A comparison of two novel alcohol dehydrogenase enzymes (ADH1 and ADH2) from the extreme halophile Haloferax volcanii
Appl. Microbiol. Biotechnol.
97
195-203
2012
Haloferax volcanii (D4GP73), Haloferax volcanii DSM 3757 (D4GP73)
Liliensiek, A.K.; Cassidy, J.; Gucciardo, G.; Whitely, C.; Paradisi, F.
Heterologous overexpression, purification and characterisation of an alcohol dehydrogenase (ADH2) from Halobacterium sp. NRC-1
Mol. Biotechnol.
55
143-149
2013
Halobacterium salinarum (Q9HMB6), Halobacterium salinarum NRC 1 (Q9HMB6), Halobacterium sp. (Q9HMB6), Halobacterium sp. NRC-1 (Q9HMB6)
Wu, X.; Zhang, C.; Orita, I.; Imanaka, T.; Fukui, T.; Xing, X.H.
Thermostable alcohol dehydrogenase from Thermococcus kodakarensis KOD1 for enantioselective bioconversion of aromatic secondary alcohols
Appl. Environ. Microbiol.
79
2209-2217
2013
Thermococcus kodakarensis
Elleuche, S.; Fodor, K.; von der Heyde, A.; Klippel, B.; Wilmanns, M.; Antranikian, G.
Group III alcohol dehydrogenase from Pectobacterium atrosepticum: insights into enzymatic activity and organization of the metal ion-containing region
Appl. Microbiol. Biotechnol.
98
4041-4051
2014
Pectobacterium atrosepticum (U6CL97), Pectobacterium atrosepticum DSM18077 (U6CL97)
Zheng, T.; Olson, D.G.; Tian, L.; Bomble, Y.J.; Himmel, M.E.; Lo, J.; Hon, S.; Shaw, A.J.; van Dijken, J.P.; Lynd, L.R.
Cofactor specificity of the bifunctional alcohol and aldehyde dehydrogenase (AdhE) in wild-type and mutant Clostridium thermocellum and Thermoanaerobacterium saccharolyticum
J. Bacteriol.
197
2610-2619
2015
Acetivibrio thermocellus (A0A0H3W5U9), Thermoanaerobacterium saccharolyticum (A0A0H3W5V0)
Brown, S.D.; Guss, A.M.; Karpinets, T.V.; Parks, J.M.; Smolin, N.; Yang, S.; Land, M.L.; Klingeman, D.M.; Bhandiwad, A.; Rodriguez, M. Jr.; Raman, B.; Shao, X.; Mielenz, J.R.; Smith, J.C.; Keller, M.; Lynd, L.R.
Mutant alcohol dehydrogenase leads to improved ethanol tolerance in Clostridium thermocellum
Proc. Natl. Acad. Sci. USA
108
13752-71375
2011
Acetivibrio thermocellus (A0A0H3W5U9)
Holec, C.; Neufeld, K.; Pietruszka, J.
P450 BM3 monooxygenase as an efficient NAD(P)H-oxidase for regeneration of nicotinamide cofactors in ADH-catalysed preparative scale biotransformations
Adv. Synth. Catal.
358
1810-1819
2016
Thermoanaerobacter brockii, Equus caballus, Ralstonia sp.
-
Kulig, J.; Frese, A.; Kroutil, W.; Pohl, M.; Rother, D.
Biochemical characterization of an alcohol dehydrogenase from Ralstonia sp.
Biotechnol. Bioeng.
110
1838-1848
2013
Ralstonia sp., Ralstonia sp. DSM 6428
Lundova, T.; Zemanova, L.; Malcekova, B.; Skarka, A.; Stambergova, H.; Havrankova, J.; Safr, M.; Wsol, V.
Molecular and biochemical characterisation of human short-chain dehydrogenase/reductase member 3 (DHRS3)
Chem. Biol. Interact.
234
178-187
2015
Homo sapiens
Ma, C.W.; Zhang, L.; Dai, J.Y;, Xiu, Z.L.
Characterization and cofactor binding mechanism of a novel NAD(P)H-dependent aldehyde reductase from Klebsiella pneumoniae DSM2026
J. Microbiol. Biotechnol.
23
1699-1707
2013
Klebsiella pneumoniae, Klebsiella pneumoniae DSM2026
Brummund, J.; Sonke, T.; Mueller, M.
Process Development for biocatalytic oxidations applying alcohol dehydrogenases
Org. Process Res. Dev.
19
1590-1595
2015
Rhodococcus ruber
-
Bartsch, S.; Brummund, J.; Koepke, S.; Straatman, H.; Vogel, A.; Schuermann, M.
Optimization of alcohol dehydrogenase for industrial scale oxidation of lactols
Biotechnol. J.
15
e2000171
2020
Starmerella magnoliae, Starmerella magnoliae DSMZ 70638
An, J.; Nie, Y.; Xu, Y.
Structural insights into alcohol dehydrogenases catalyzing asymmetric reductions
Crit. Rev. Biotechnol.
39
366-379
2019
Thermoanaerobacter ethanolicus
Sugimoto, C.; Takeda, K.; Kariya, Y.; Matsumura, H.; Yohda, M.; Ohno, H.; Nakamura, N.
A method of expression for an oxygen-tolerant group III alcohol dehydrogenase from Pyrococcus horikoshii OT3
J. Biol. Inorg. Chem.
22
527-534
2017
Pyrococcus horikoshii (O58517), Pyrococcus horikoshii ATCC 700860 (O58517), Pyrococcus horikoshii DSM 12428 (O58517), Pyrococcus horikoshii JCM 9974 (O58517), Pyrococcus horikoshii NBRC 100139 (O58517), Pyrococcus horikoshii OT-3 (O58517)
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