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1.2.1.3: aldehyde dehydrogenase (NAD+)

This is an abbreviated version!
For detailed information about aldehyde dehydrogenase (NAD+), go to the full flat file.

Word Map on EC 1.2.1.3

Reaction

an aldehyde
+
NAD+
 +
H2O
=
a carboxylate
 +
NADH
 +
H+

Synonyms

ADH, AdhE, AHD-M1, ALD1A1, ALD4, ALD6, ALDDH, aldehyde dehydrogenase, aldehyde dehydrogenase (NAD), aldehyde dehydrogenase 1, aldehyde dehydrogenase 16, aldehyde dehydrogenase 1A1, aldehyde dehydrogenase 1A3, aldehyde dehydrogenase 1B1, aldehyde dehydrogenase 2, aldehyde dehydrogenase 3A1, aldehyde dehydrogenase 6, aldehyde dehydrogenase 7A1, aldehyde dehydrogenase class 1, aldehyde dehydrogenase type 2, Aldehyde dehydrogenase [NAD+], Aldehyde dehydrogenase, cytosolic, Aldehyde dehydrogenase, microsomal, aldehyde dehydrogenase-2, aldehyde dehydrogenase7, aldehyde:NAD+ oxidoreductase, ALDH, ALDH 2, ALDH I, ALDH II, ALDH-2, ALDH-E1, ALDH-E2, ALDH1, ALDH1-NL, ALDH16, ALDH1A1, Aldh1a2, Aldh1a3, Aldh1a7, Aldh1b1, ALDH2, ALDH2(1), ALDH2(2), ALDH2(3), ALDH22A1, ALDH2B8, ALDH2C4, ALDH3A1, ALDH3A2, Aldh3b1, ALDH3H1, ALDH3I1, ALDH5A, ALDH7, Aldh7a1, ALDH7B4, Aldh8a1, ALDHI, ALDHTt, ALDHX, ALHDII, Allergen Alt a 10, aryl-aldehyde dehydrogenases, BADH, benzaldehyde dehydrogenase, Brassica turgor-responsive/drought-induced gene 26 protein, Bt-Aldh, Btg-26, class 1 aldehyde dehydrogenase, class 2 aldehyde dehydrogenase, class I ALDH, CoA-independent aldehyde dehydrogenase, coniferyl-aldehyde dehydrogenase, Cphy_1178, EC 1.1.1.70, ETA-crystallin, FeaB-K-12, gamma-aminobutyraldehyde dehydrogenase, hALDH2, HsALDH16A1, irreversible NAD+-dependent aldehyde dehydrogenase, K(+)-ACDH, K(+)-activated acetaldehyde dehydrogenase, KGSADH, LsALDH16, m-methylbenzaldehyde dehydrogenase, Matured fruit 60 kDa protein, MF-60, Mg(2+)-ACDH, Mg(2+)-activated acetaldehyde dehydrogenase, mitochondrial aldehyde dehydrogenase, More, NAD+-dependent aldehyde dehydrogenase, NAD+-dependent ALDH, NAD+-linked aldehyde dehydrogenase, NAD+-pimelic semialdehyde-dependent aldehyde dehydrogenase, NAD+-specific ALDH, NAD-aldehyde dehydrogenase, NAD-dependent 4-hydroxynonenal dehydrogenase, NAD-dependent aldehyde dehydrogenase, NAD-linked aldehyde dehydrogenase, Non-lens ALDH1, p-ALDH2, P51, phenylacetaldehyde dehydrogenase, PhnN, phnY, phosphonoacetaldehyde dehydrogenase, phosphonoacetaldehyde oxidase, PM-ALDH9, PnAA dehydrogenase, propionaldehyde dehydrogenase, PuuC, R-aminobutyraldehyde dehydrogenase, RALDH, RALDH(II), RalDH1, Retinal dehydrogenase, retinal dehydrogenase type I, sALDH, salvery aldehyde dehydrogenase, ThnG, TTC0513, Turgor-responsive protein 26G, yALDH, YneI

ECTree

     1 Oxidoreductases
         1.2 Acting on the aldehyde or oxo group of donors
             1.2.1 With NAD+ or NADP+ as acceptor
                1.2.1.3 aldehyde dehydrogenase (NAD+)

Engineering

Engineering on EC 1.2.1.3 - aldehyde dehydrogenase (NAD+)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C247S
-
the mutant shows slightly reduced activity compared to the wild type enzyme
C253S
-
the mutation abolishes enzymatic activity
C45S
-
the mutant shows stongly reduced activity compared to the wild type enzyme
E149D
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E149D/I200G
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E149D/I200V
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E149N
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E149N/I200G
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E149N/I200V
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E149Q
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E149Q/I200G
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E149Q/I200V
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E149T
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E149T/I200G
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E149T/I200V
the mutant shows a good catalysis with NADP+ compared to the wild type enzyme
E149T/V178R/I200V
the mutant uses NADP+ with almost 7fold higher catalytic efficiency compared to NAD+
I200G
I200V
C289D
-
enzyme activity is nearly abolished in this mutant
C289P
-
enzyme activity is nearly abolished in this mutant
C289R
-
enzyme activity is nearly abolished in this mutant
E255D
-
the mutant enzyme shows severely diminished activity
E255K
-
the mutant enzyme shows severely diminished activity
A505P
-
site-directed mutagenesis, the mutant enzyme exhibits a profound kinetic defect characterized by markedly elevated Michaelis constants for alpha-aminoadipate semialdehyde, suggesting that the mutated residue is important for substrate binding. The mutant enzyme is defective in tetramer formation, and shows highly reduced activity compared to wild-type
A505P/Q506K
-
site-directed mutagenesis, the mutant enzyme exhibits a profound kinetic defect characterized by markedly elevated Michaelis constants for alpha-aminoadipate semialdehyde, suggesting that the mutated residues are important for substrate binding. The mutant enzyme is defective in tetramer formation, and shows highly reduced activity compared to wild-type. Structure analysis of the protomer of ALDH7A1 with the mutated residues Ala505 and Gln506, PDB ID 4ZUL
ALDH-H3tail
-
aldehyde dehydrogenase class 1 with the addition of the C-terminal tail of class 3, KM-value for propionaldehyde is 2.6fold higher than the KM-value of the wild-type enzyme, KM-value for NAD+ is 2fold higher than the KM-value of the wild-type enzyme
ALDH1-5AA
-
aldehyde dehydrogenase class 1 with the addition of five amino acids at the C-terminus, KM-value for propionaldehyde is 67% of the KM-value of the wild-type enzyme, KM-value for NAD+ is 73% of the KM-value of the wild-type enzyme
C302S
D80G
-
KM-value for propionaldehyde is 24% of the KM-value of the wild-type enzyme, KM-value for NAD+ is 32% of the KM-value of the wild-type enzyme
D80G/S82A
E268Q
the mutant shows 1.39% residual dehydrogenase activity at pH 9.0 and 0.88% residual dehydrogenase activity at pH 7.5 compared to the wild type enzyme. The mutant exhibits virtually unaffected rates of nitroglycerin denitration despite low dehydrogenase and esterase activities. The mutant exhibits about 50% lower rates of superoxide formation than the wild type enzyme
E399Q
mutant is not inhibited by MgCl2
E487K
K487E
Q506K
-
site-directed mutagenesis, the mutant enzyme exhibits a profound kinetic defect characterized by markedly elevated Michaelis constants for alpha-aminoadipate semialdehyde, suggesting that the mutated residue is important for substrate binding. The mutant enzyme is defective in tetramer formation, and shows highly reduced activity compared to wild-type
R264E
-
turnover-number is about 6% of that of the native enzyme, Km-value is about 20fold higher than the Km-value of the wild-type enzyme
R264Q
-
turnover-number is about 50% of that of the native enzyme, Km-value is about 1.6fold higher than the Km-value of the wild-type enzyme
R475E
-
turnover-number is about 9% of that of the native enzyme, Km-value is about 35fold higher than the Km-value of the wild-type enzyme
R475E/R264E
-
turnover-number is about 2% of that of the native enzyme, Km-value is about 430fold higher than the Km-value of the wild-type enzyme
R475Q
R475Q/R264Q
-
Km-value is about 35fold higher than the KM-value of the wild-type enzyme
R84Q
-
KM-value for propionaldehyde is 5.8fold higher than the Km-value of the wild-type enzyme, KM-value for NAD+ is 36% of the KM-value of the wild-type enzyme
S31T/V63A/T244S/E479D
generated by random mutagenesis and selected for insensivity to Mg2+ inhibition
S33C/T244S/C463S
generated by random mutagenesis and selected for insensivity to Mg2+ inhibition
S82A
-
KM-value for propionaldehyde is 36% of the KM-value of the wild-type enzyme, KM-value for NAD+ is 15% of the KM-value of the wild-type enzyme
T244S
the T244S mutation is not inhibited by Mg2+. The mutant shows a decreasing Km for NAD+ binding with increasing Mg2+ concentration. chloroacetaldehyde is a better substrate for the mutant enzyme than acetaldehyde in the presence of Mg2+ which is similar to the Mg2+-dependent ALDH2
T244S/D391E
generated by random mutagenesis and selected for insensivity to Mg2+ inhibition
C295A
-
site-directed mutagenesis, inactive mutant
S74A
-
half-life of the mutant enzyme at 50°C is 1 min compared to the half-life of the native enzyme of 1 min. Mutation diminishes NAD+ binding, affecting both the on and the off rates, as well as the rate-limiting step. About 100fold higher Km-value for NAD+
S74C
-
about 70fold higher Km-value for NAD+
S74T
-
about 100fold higher Km-value for NAD+
E385A
N158A
R108A
R290A
R447A
C274A
-
the mutation leads to a drastic loss of the activity
C274S
-
the mutation leads to a drastic loss of the activity
E240A
-
the mutation leads to a drastic loss of the activity
E240S
-
the mutation leads to a drastic loss of the activity
E370Q
-
the mutation results in decreased activity (higher Km and lower kcat values toward NAD+ and acetaldehyde than the wild type enzyme)
I168A
-
the mutation results in no obvious change of kinetics properties toward acetaldehyde and a comparable increase of affinity toward NAD+
K165Q
-
the mutation results in decreased activity (higher Km and lower kcat values toward NAD+ and acetaldehyde than the wild type enzyme)
N142A
-
the mutation results in decreased activity (higher Km and lower kcat values toward NAD+ and acetaldehyde than the wild type enzyme)
C274A
-
the mutation leads to a drastic loss of the activity
-
C274S
-
the mutation leads to a drastic loss of the activity
-
E240A
-
the mutation leads to a drastic loss of the activity
-
E370Q
-
the mutation results in decreased activity (higher Km and lower kcat values toward NAD+ and acetaldehyde than the wild type enzyme)
-
K165Q
-
the mutation results in decreased activity (higher Km and lower kcat values toward NAD+ and acetaldehyde than the wild type enzyme)
-
additional information