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1.1.1.1: alcohol dehydrogenase

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

Word Map on EC 1.1.1.1

Reaction

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

Synonyms

(R)-specific alcohol dehydrogenase, 40 kDa allergen, Aadh1, acetaldehyde-alcohol dehydrogenase, 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, ADHES77, ADS1, AFPDH, alcohol dehydrogenase, alcohol dehydrogenase (NAD), alcohol dehydrogenase 1, alcohol dehydrogenase 10, alcohol dehydrogenase 2, alcohol dehydrogenase 3, alcohol dehydrogenase 5, alcohol dehydrogenase class-P, alcohol dehydrogenase D, alcohol dehydrogenase GroES domain protein, 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, alpha-ketoaldehyde dehydrogenase, anti-Prelog reductase, APE2239, APE_2239.1, ARAD1B16786p, bi-functional alcohol/aldehyde dehydrogenase, bifunctional acetaldehyde-alcohol dehydrogenase, 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, glutathione-dependent formaldehyde dehydrogenase/alcohol dehydrogenase, GSH-FDH, GSH-FDH/ADH, HLAD, hLADH, HpADH3, HtADH, HvADH1, HVO_2428, iron-containing alcohol dehydrogenase, KlADH4, KlDH3, KmADH3, KmADH4, LSADH, medium chain alcohol dehydrogenase, medium-chain NAD+-dependent ADH, medium-chain secondary alcohol dehydrogenase, MGD, More, NAD(H)-dependent alcohol dehydrogenase, NAD+-ADH, NAD+-dependent (S)-stereospecific alcohol dehydrogenase, NAD+-dependent alcohol dehydrogenase, NAD+-dependent SDR, NAD+-linked alcohol dehydrogenase 1, NAD+-linked methylglyoxal 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, NADH-dependent anti-Prelog specific ADH, NADH:p-NTF-reductase, Octanol dehydrogenase, Pcal_1311, PF0991 protein, PF1960, PFADH, primary alcohol dehydrogenase, Retinol dehydrogenase, SaADH, SaADH2, Saci_1232, SADH, SCAD, sec-ADH A, short-chain ADH, short-chain dehydrogenase/reductase, short-chain NAD(H)-dependent dehydrogenase/reductase, slr1192, 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, YIM1, YLL056C, YMR152W, Ymr152wp

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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
P704L/H734R
C243S
site-directed mutagenesis, the mutant shows increased specific activity, the mutation at Cys243 does not significantly affect ADH kinetic efficiency
C47S
site-directed mutagenesis, the mutation Ser causes an almost complete loss of the enzyme activity
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
G211C
-
mutant enzyme exhibits almost complete reversals in cofactor specificity
G211InsA
-
with NADP+, the mutant enzyme shows a 29-fold increase in kcat as compared to the wild-type enzyme
G211InsC
-
with NAD+, the mutant enzyme exhibits 6-fold decrease in kcat as compared to wild-type enzyme. Mutant enzyme exhibits almost complete reversals in cofactor specificity
G211InsG
-
with NAD+, the mutant enzyme exhibits 2.5-fold enhancement in kcat over the wild-type enzyme. Activity with NADP+ exceeds that of the wild type enzyme
G211InsS
-
with NAD+, the mutant enzyme exhibits 2.5-fold enhancement in kcat over the wild-type enzyme. With NADP+, the mutant enzyme shows a 29-fold increase in kcat as compared to the wild-type enzyme
G211S
-
with NAD+, the mutant enzyme exhibits 1.5-fold enhancement in kcat over the wild-type. Activity with NADP+ exceeds that of the wild type enzyme
H255R
-
the H255R single mutant exhibits an increased binding affinity toward NADP+ and a concomitant reduction in affinity for NAD+. The apparent kcat for H255R is about 60% of that of the wild-type with NAD+, but it is sixfold higher than the wild-type with NADP+. Position 255 is important for recognizing NADP(H), but is not the sole determinant of cofactor specificity
K249G
-
catalytic efficiency increases 5fold for NADH, the efficiency with NADPH increases more than 30fold in comparison to the wild-type
K249G/H255R
-
the catalytic efficiency with NADH increases 4fold, the efficiency with NADPH increases more than 16fold. In the oxidation reaction, the kcat with NAD+ improves by 15fold for the double mutant over the wild type enzyme. With NADP+ the kcat is nearly two orders of magnitude larger than the wild-type. Mutant exhibits significantly improved activity and broadened cofactor specificity as compared to the wild-type enzyme
F43H
-
site-directed mutagenesis, mutant C1 variant
F43H/Y54L
-
site-directed mutagenesis, mutant C1B1 variant
F43T/Y54G/L119Y/F282W
-
site-directed mutagenesis, mutant B1F4 variant
H39Y/F43H/Y54F/Y294F/W295A
-
site-directed mutagenesis, mutant A2C2B1 variant
H39Y/F43S/Y294F/W295A
-
site-directed mutagenesis, mutant A2C3 variant
W295A
-
site-directed mutagenesis, mutant A1 variant
Y294F/W295A
Y54G/L119Y
-
site-directed mutagenesis, mutant B1 variant
H39Y/F43H/Y54F/Y294F/W295A
-
site-directed mutagenesis, mutant A2C2B1 variant
-
W295A
-
site-directed mutagenesis, mutant A1 variant
-
Y294F/W295A
E97C
-
shows the same activity but a reduced thermostability with respect to the wild type recombinant protein
N249Y
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
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
M294L
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
-
I151V
polymorphism of the commercial yeast ADH (Saccharomyces pastorianus) compared to the laboratory strain Saccharomyces cerevisiae, in the V58T, Q127E, Q147E, and I151V substitutions, the removal of the methyl group has only weak effects on the structure of the neighboring residues
Q127E
polymorphism of the commercial yeast ADH (Saccharomyces pastorianus) compared to the laboratory strain Saccharomyces cerevisiae, in the V58T, Q127E, Q147E, and I151V substitutions, not readily distinguishable at the current resolutions, and the local structure is not significantly altered
Q147E
polymorphism of the commercial yeast ADH (Saccharomyces pastorianus) compared to the laboratory strain Saccharomyces cerevisiae, in the V58T, Q127E, Q147E, and I151V substitutions, not readily distinguishable at the current resolutions, and the local structure is not significantly altered
V58T
polymorphism of the commercial yeast ADH (Saccharomyces pastorianus) compared to the laboratory strain Saccharomyces cerevisiae, in the V58T, Q127E, Q147E, and I151V substitutions, not readily distinguishable at the current resolutions, and the local structure is not significantly altered
additional information