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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Metals Ions
Metals Ions on EC 1.1.1.71 - alcohol dehydrogenase [NAD(P)+]
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Ca2+
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Ca2+ has an stabilizing effect. With 1.0 mM CaCl2, the enzyme is completely stable at 0°C for 2 h and after 3.5 h almost 90% of the initial activity is retained
Co2+
Fe2+
moderately activating the reduction of butanal, but only very weak activation of oxidation of 1-butanol
Fe3+
moderately activating the reduction of butanal, but no activation of oxidation of 1-butanol
KCl
Mn2+
moderately activating the reduction of butanal, but only very weak activation of oxidation of 1-butanol
NaCl
Ni2+
required for reduction of butanal, activates, but only slightly in oxidation of 1-butanol
additional information
Co2+
moderately activating the reduction of butanal, but no activation of oxidation of 1-butanol
a preference for KCl over NaCl is observed, with best activity at 4 M KCl
KCl
maximally active with ethanol with 4 M KCl. It is maximally active with 1-propanol with 2 M KCl and with 1-butanol and 1-pentanol with 1 M KCl. Optimum activity with the secondary alcohols, 2-propanol and 2-butanol, is observed with 3 M KCl and 2 M KCl, respectively, and with isoamyl alcohol in the presence of 1 M KCl. Maximum activity with benzyl alcohol is detected with 2 M KCl. Catalyzed the reductive reaction optimally at pH 6.0 with 1 M KCl
KCl
activity increases in the presence of KCl is maintained even at concentration of 3 M
the enzyme requires high salt concentrations for its activity, a preference for KCl over NaCl is observed
NaCl
activity increases in the presence of NaCl is maintained even at concentration of 4 M
NaCl
activity is increased in the presence of NaCl and remains at the elevated level up to 4 M of NaCl. The rates of 2-propanol and 2,5-hexanediol oxidation are increased by more than 2fold after the addition of NaCl up to 1 M to the assay mixture and is retained at the increased level up to 4 M of NaCl
no activity with Ca2+, Mg2+, Zn2+, and Cu2+. The Fe2+-reconstituted Ni-PhADH is sensitively and rapidly inactivated by dioxygen gas. The activity of apoform o-PhADH is significantly lower than that of Ni2+-bound PhADH. The enzyme is inactivated by the replacement of the ferrous ion in the active site with another metal ion such as a zinc ion, which has been considered an inhibitor of iron-activating group III ADHs
additional information
metal independency is supported by the absence of a significant effect of TsAdh319 preincubation with 10 mM Me2+ for 30 min before measuring the activity in the presence of 1 mM Me2+ or EDTA
additional information
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metal independency is supported by the absence of a significant effect of TsAdh319 preincubation with 10 mM Me2+ for 30 min before measuring the activity in the presence of 1 mM Me2+ or EDTA