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.

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

     1 Oxidoreductases

         1.1 Acting on the CH-OH group of donors

             1.1.1 With NAD⁺ or NADP⁺ as acceptor

                1.1.1.71 alcohol dehydrogenase [NAD(P)+]

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All data fields related to EC 1.1.1.71

Results	in table
5	Activating Compound
20	AA Sequence
1	CAS Registry Number
16	Cloned(Commentary)
61	Cofactor
4	Crystallization (Commentary)
58	Disease/ Diagnostics
11	General Information
1	General Stability
51	Inhibitors
38	kcat/KM [mM/s]
2	Ki Value [mM]
112	KM Value [mM]
6	Localization
19	Metals/Ions
17	Molecular Weight [Da]
51	Natural Substrates/ Products (Substrates)
38	Organic Solvent Stability
76	Organism
31	pH Optimum
8	pH Range
3	pH Stability
1	pI Value
21	Protein Variants
19	Purification (Commentary)
7	Reaction
3	Reaction Type
66	Reference
26	Source Tissue
25	Specific Activity [micromol/min/mg]
7	Storage Stability
393	Substrates and Products (Substrate)
24	Subunits
73	Synonyms
1	Systematic Name
13	Temperature Optimum [°C]
5	Temperature Range [°C]
24	Temperature Stability [°C]
51	Turnover Number [1/s]

General Information

General Information 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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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

evolution

7 entries

malfunction

2 entries

physiological function

2 entries

evolution

Thermoanaerobacter ethanolicus

-

ADHs structure and function comparisons, SDR family enzymes structure-function comparisons, overview

760921

evolution

Pyrococcus horikoshii

O58517

NAD(P)-dependent group III alcohol dehydrogenases (ADHs), well known as iron-activated enzymes

761529

evolution

Pyrococcus horikoshii DSM 12428

-

NAD(P)-dependent group III alcohol dehydrogenases (ADHs), well known as iron-activated enzymes

-

evolution

Pyrococcus horikoshii NBRC 100139

-

NAD(P)-dependent group III alcohol dehydrogenases (ADHs), well known as iron-activated enzymes

-

evolution

Pyrococcus horikoshii JCM 9974

-

NAD(P)-dependent group III alcohol dehydrogenases (ADHs), well known as iron-activated enzymes

-

evolution

Pyrococcus horikoshii ATCC 700860

-

NAD(P)-dependent group III alcohol dehydrogenases (ADHs), well known as iron-activated enzymes

-

evolution

Pyrococcus horikoshii OT-3

-

NAD(P)-dependent group III alcohol dehydrogenases (ADHs), well known as iron-activated enzymes

-

malfunction

Starmerella magnoliae

-

the optimized ADHA variant shows a 7fold higher oxidative activity, a 26°C increased stability, and is applied to develop an efficient chlorolactol oxidation process

760769

malfunction

Starmerella magnoliae DSMZ 70638

-

the optimized ADHA variant shows a 7fold higher oxidative activity, a 26°C increased stability, and is applied to develop an efficient chlorolactol oxidation process

-

physiological function

Starmerella magnoliae

-

enzyme ADHA from Candida magnoliae strain DSMZ 70638 is identified to efficiently catalyze the regioselective hydroxy-lactone oxidations to hydroxy-lactones. Hydroxy-lactones are common intermediates in industrial processes to cholesterol lowering (va)statin drugs. ADH catalyzed oxidations can be developed to efficient and safe processes, but the ADHA wild-type enzyme is not productive enough in chlorolactol oxidation

760769

physiological function

Starmerella magnoliae DSMZ 70638

-

enzyme ADHA from Candida magnoliae strain DSMZ 70638 is identified to efficiently catalyze the regioselective hydroxy-lactone oxidations to hydroxy-lactones. Hydroxy-lactones are common intermediates in industrial processes to cholesterol lowering (va)statin drugs. ADH catalyzed oxidations can be developed to efficient and safe processes, but the ADHA wild-type enzyme is not productive enough in chlorolactol oxidation

-