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
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thermoanaerobacter
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all-trans-retinaldehyde
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retinyl
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ethanolicus
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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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Cofactor
Cofactor 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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NAD(P)H
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strains B592 and B593, higher activities with NADP(H) than with NAD(H)
NAD+
dual cofactor dependency, NAD+ shows 60% of the activity with NADP+
NAD+
dual cofactor specificity, activity with NAD+ is 14% compared to the activity with NADP+ at pH 11.0 with 4 M KCl
NADH
in wild-type strains, NADH is the preferred cofactor for both aldehyde dehydrogenase ALDH and alcohol dehydrogenase ADH activities. In high-ethanol-producing (ethanologen) strains of Thermoanaerobacterium saccharolyticum, both ALDH and ADH activities show increased NADPH-linked activity
NADH
in wild-type strains, NADH is the preferred cofactor for both aldehyde dehydrogenase ALDH and alcohol dehydrogenase ADH activities. The AdhE protein of the ethanologenic strain of Clostridium thermocellum has acquired high NADPH-linked ADH activity while maintaining NADH-linked ALDH and ADH activities at wild-type levels
NADP+
preferred cofactor. Activity with NAD+ is 75% less than that detected with NADP+
NADP+
dual cofactor dependency, NAD+ shows 60% of the activity with NADP+
NADP+
dual cofactor specificity, activity with NAD+ is 14% compared to the activity with NADP+ at pH 11.0 with 4 M KCl
NADPH
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the specificity towards NADP(H) is determined by residues Gly198, Ser199, Arg200 and Tyr218
NADPH
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the specificity towards NADP(H) is determined by residues Gly198, Ser199, Arg200 and Tyr218
NADPH
in wild-type strains, NADH is the preferred cofactor for both aldehyde dehydrogenase ALDH and alcohol dehydrogenase ADH activities. In high-ethanol-producing (ethanologen) strains of Thermoanaerobacterium saccharolyticum, both ALDH and ADH activities show increased NADPH-linked activity
NADPH
the ethanol tolerant phenotype of Clostridium thermocellum is primarily due to a mutated bifunctional acetaldehyde-CoA/alcohol dehydrogenase gene (adhE). The mutant displays a complete loss of NADH-dependent activity with concomitant acquisition of NADPH-dependent activity