1.1.1.1: alcohol dehydrogenase

This is an abbreviated version, for detailed information about alcohol dehydrogenase, go to the full flat file.

Reaction

a primary alcohol
+
NAD+
=
an aldehyde
+
NADH
+
H+

Synonyms

(R)-specific alcohol dehydrogenase, 40 kDa allergen, Aadh1, ADH, ADH 1, ADH class III, ADH I, ADH II, ADH-10, ADH-A, ADH-A2, ADH-B2, ADH-C2, ADH-HT, ADH-I, ADH1, ADH1B, ADH1C, ADH1C*1, ADH1C*2, Adh1p, ADH2, ADH3, ADH4, ADH5, ADH6Hp, ADH8, AdhA, AdhB, AdhC, AdhD, AdhE, ADS1, AFPDH, alcohol dehydrogenase, alcohol dehydrogenase (NAD), alcohol dehydrogenase 1, alcohol dehydrogenase 10, alcohol dehydrogenase 2, alcohol dehydrogenase 3, alcohol dehydrogenase 5, alcohol dehydrogenase I, alcohol dehydrogenase II, Alcohol dehydrogenase-B2, alcohol dependent dehydrogenase, alcohol-aldehyde/ketone oxidoreductase, NAD+-dependent, alcohol:NAD+ oxidoreductase, aldehyde dehydrogenase, aldehyde reductase, aldehyde/alcohol dehydrogenase, ALDH, aliphatic alcohol dehydrogenase, APE2239, APE_2239.1, ARAD1B16786p, bifunctional alcohol/aldehyde dehydrogenase, CHY1186, class I ADH, class I ALDH, class II ADH, class III ADH, class III alcohol dehydrogenase, class IV ADH, Cm-ADH2, Cthe_0423, DADH, dehydrogenase, alcohol, ethanol dehydrogenase, FALDH, FDH, Gastric alcohol dehydrogenase, Glutathione-dependent formaldehyde dehydrogenase, GSH-FDH, HLAD, HpADH3, HtADH, HvADH1, HVO_2428, iron-containing alcohol dehydrogenase, KlADH4, KlDH3, KmADH3, KmADH4, long-chain alkyl alcohol dehydrogenase, LSADH, medium chain alcohol dehydrogenase, medium-chain NAD+-dependent ADH, medium-chain secondary alcohol dehydrogenase, NAD(H)-dependent alcohol dehydrogenase, NAD+-ADH, NAD+-dependent (S)-stereospecific alcohol dehydrogenase, NAD+-dependent alcohol dehydrogenase, NAD-dependent alcohol dehydrogenase, NAD-dependent medium-chain ADH, NAD-specific aromatic alcohol dehydrogenase, NADH-alcohol dehydrogenase, NADH-aldehyde dehydrogenase, NADH-dependent alcohol dehydrogenase, Octanol dehydrogenase, PF0991 protein, PF1960, primary alcohol dehydrogenase, Retinol dehydrogenase, SaADH, SaADH2, Saci_1232, SADH, SCAD, sec-ADH A, short-chain ADH, short-chain NAD(H)-dependent dehydrogenase/reductase, SSADH, SsADH-10, SSO2536, ST0053, Ta1316 ADH, TaDH, TBADH, Teth39_0206, Teth39_0218, Teth514_0627, TK0845, Tsac_0416, Y-ADH, YADH, YADH-1, yeast alcohol dehydrogenase

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.1 alcohol dehydrogenase

Engineering

Engineering on EC 1.1.1.1 - alcohol dehydrogenase

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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H51Q
-
site-directed mutagenesis, shifting of pH dependency, increased activity at pH 8.0, decrease of the rate of isomerization of the enzyme-NAD+ complex, which becomes the limiting step for ethanol oxidation
H51Q/K228R
-
site-directed mutagenesis, kinetic effects
W54L
-
less active than the wild-type enzyme with ethanol, 1-propanol and 1-butanol. With 1-pentanol and 1-hexanol the mutant enzyme is a better catalyst than the wild-type enzyme
C257L
-
mutation introduced to improve stability under oxidzing conditions. Mutant exhibits prolonged stability and an elevated inactivation temperature
V260A
-
kinetic parameters and temperature dependencies similar to wild-type
W49F/W167Y
-
kinetic parameters and temperature dependencies similar to wild-type
W49F/W167Y/V260A
-
kinetic parameters and temperature dependencies similar to wild-type
W49F/W87F
-
kinetic parameters and temperature dependencies similar to wild-type
W49F/W87F/V260A
-
kinetic parameters and temperature dependencies similar to wild-type
W87A
-
mutation results in a loss of the Arrhenius break seen at 30°C for the wild-type enzyme and an increase in cold lability due to destabilization of the active tetrameric form. Kinetic isotope effects are nearly temperature-independent over the experimental temperature range, and similar in magnitude to those measured above 30°C for the wild-type enzyme
W87F
-
investigation on protein dynamics on the microsecond time scale. Mutant exhibits a fast, temperature-independent microsecond decrease in fluorescence followed by a slower full recovery of the initial fluorescence. The results rule out an ionizing histidine as the origin of the fluorescence quenching. A Trp49-containing dimer interface may act as a conduit for thermally activated structural change within the protein interior
W87F/H43A
-
investigation on protein dynamics on the microsecond time scale. Mutant exhibits a fast, temperature-independent microsecond decrease in fluorescence followed by a slower full recovery of the initial fluorescence. The results rule out an ionizing histidine as the origin of the fluorescence quenching. A Trp49-containing dimer interface may act as a conduit for thermally activated structural change within the protein interior
Y25A/W49F/W167Y
-
kinetic parameters and temperature dependencies similar to wild-type
Y25A/W49F/W167Y/V260A
-
kinetic parameters and temperature dependencies similar to wild-type
Y25A/W49F/W87F
-
kinetic parameters and temperature dependencies similar to wild-type
Y25A/W49F/W87F/V260A
-
kinetic parameters and temperature dependencies similar to wild-type
A93F
-
isozyme alphaalpha, altered active site structure and inhibitor binding
S48T
-
isozyme gamma(2)gamma(2), altered active site structure and inhibitor binding
V141L
-
isozyme gamma(2)gamma(2), altered active site structure and inhibitor binding
P47A
site-directed mutagenesis, about 100fold increased activity compared to the wild-type enzyme
P47H
site-directed mutagenesis, about 100fold increased activity compared to the wild-type enzyme
P47Q
site-directed mutagenesis, about 100fold increased activity compared to the wild-type enzyme
G223D
-
unaltered cofactor specificity compared to the wild-type enzyme
G223D/T224I
-
highly reduced activity with NADP+ compared to the wild-type enzyme, wild-type-like activity with NAD+
G223D/T224I/H225N
-
altered cofactor specificity, highly reduced activity with NADP+ compared to the wild-type enzyme, wild-type-like activity with NAD+
H225N
-
unaltered cofactor specificity compared to the wild-type enzyme
T224I
-
unaltered cofactor specificity compared to the wild-type enzyme
P704L/H734R
D223G
-
highly reduced activity compared to the wild-type enzyme
D223G/G225R
-
nearly inactive mutant
D49N
-
highly reduced activity compared to the wild-type enzyme
DELTAA200/A201L
-
highly reduced activity compared to the wild-type enzyme
E68Q
-
highly reduced activity compared to the wild-type enzyme
G204A
-
nearly inactive mutant
G224I
-
reduced activity compared to the wild-type enzyme
G225R
-
reduced activity compared to the wild-type enzyme
H47R
-
reduced activity compared to the wild-type enzyme
H51E
-
highly reduced activity compared to the wild-type enzyme
H51Q
-
reduced activity compared to the wild-type enzyme
L203A
-
reduced activity compared to the wild-type enzyme
L203A/T178S
-
reduced activity compared to the wild-type enzyme
S110P/Y295C
-
mutant is able to catalyze the NADH-dependent reduction of 5-hydroxymethylfurfural, an inhibitor of yeast fermentation, best activity among the mutants isolated
S198F
-
highly reduced activity compared to the wild-type enzyme
S269I
-
nearly inactive mutant
T48A
-
inactive mutant
T48C
-
inactive mutant
T48S
-
reduced activity compared to the wild-type enzyme
T48S/T93A
-
reduced activity compared to the wild-type enzyme
T48S/W57M/W93A
-
reduced activity compared to the wild-type enzyme
W57L
-
reduced activity compared to the wild-type enzyme
W57M
-
slightly reduced activity compared to the wild-type enzyme
W93A
-
reduced activity compared to the wild-type enzyme
Y295C
-
mutant is able to catalyze the NADH-dependent reduction of 5-hydroxymethylfurfural, an inhibitor of yeast fermentation
S110P/Y295C
-
mutant is able to catalyze the NADH-dependent reduction of 5-hydroxymethylfurfural, an inhibitor of yeast fermentation, best activity among the mutants isolated
-
Y295C
-
mutant is able to catalyze the NADH-dependent reduction of 5-hydroxymethylfurfural, an inhibitor of yeast fermentation
-
E97C
-
shows the same activity but a reduced thermostability with respect to the wild type recombinant protein
W95L
-
the mutant displays no apparent activity with short-chain primary and secondary alcohols and poor activity with aromatic substrates and coenzyme, the substitution affects the structural stability of the archaeal ADH, decreasing its thermal stability without relevant changes in secondary structure, optimum pH is at about pH 10
W95L/N249Y
-
the mutant exhibits higher activity but decreased affinity toward aliphatic alcohols, aldehydes as well as NAD+ and NADH compared to the wild type enzyme, optimum pH is at about pH 8.6
additional information