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Information on EC 1.2.1.65 - salicylaldehyde dehydrogenase
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1.2.1.65 salicylaldehyde dehydrogenaseIUBMB Comments
Involved in the naphthalene degradation pathway in some bacteria.
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Word Map
- 1.2.1.65
- salicylate
- naphthalene
- dioxygenase
- catechol
- 1,2-dihydroxynaphthalene
-
naphthalene-degrading
- phenanthrene
-
cis,cis-muconic
- trans-o-hydroxybenzylidenepyruvate
- gentisate
-
catechol-1,2-dioxygenase
- pyrene
-
1-hydroxy-2-naphthoic
- o-phthalate
- 1-naphthol
-
2-hydroxymuconic
-
1,2-dioxygenase
- carbaryl
-
coal
-
dihydrodiol
- environmental protection
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
salicylaldehyde dehydrogenase, saldh, saldan, nad+-dependent salicylaldehyde dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
NahF
NahV
sALDH
salicylaldehyde dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
salicylaldehyde + NAD+ + H2O = salicylate + NADH + 2 H+
-
-
-
-
salicylaldehyde + NAD+ + H2O = salicylate + NADH + 2 H+
catalytic mechanism, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
-
-
-
-
oxidation
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
salicylaldehyde:NAD+ oxidoreductase
Involved in the naphthalene degradation pathway in some bacteria.
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CAS REGISTRY NUMBER
COMMENTARY
55354-34-2
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-naphthaldehyde + NAD+ + H2O
1-naphthoate + NADH + 2 H+
-
low activity
-
-
?
2-carboxybenzaldehyde + NAD+ + H2O
2-carboxybenzoate + NADH + 2 H+
-
very low activity
-
-
?
2-chlorobenzaldehyde + NAD+ + H2O
2-chlorobenzoate + NADH + 2 H+
-
low activity
-
-
?
2-methoxybenzaldehyde + NAD+ + H2O
2-methoxybenzoate + NADH + 2 H+
-
low activity
-
-
?
2-naphthaldehyde + NAD+ + H2O
2-naphthoate + NADH + 2 H+
-
moderate activity
-
-
?
2-nitrobenzaldehyde + NAD+ + H2O
2-nitrobenzoate + NADH + 2 H+
-
low activity
-
-
?
3-carboxybenzaldehyde + NAD+ + H2O
3-carboxybenzoate + NADH + 2 H+
-
very low activity
-
-
?
3-chlorobenzaldehyde + NAD+ + H2O
3-chlorobenzoate + NADH + 2 H+
-
moderate activity
-
-
?
3-hydroxybenzaldehyde + NAD+ + H2O
3-hydroxybenzoate + NADH + 2 H+
-
low to moderate activity
-
-
?
3-methoxybenzaldehyde + NAD+ + H2O
3-methoxybenzoate + NADH + 2 H+
-
moderate activity
-
-
?
3-nitrobenzaldehyde + NAD+ + H2O
3-nitrobenzoate + NADH + 2 H+
-
low activity
-
-
?
4-carboxybenzaldehyde + NAD+ + H2O
4-carboxybenzoate + NADH + 2 H+
-
very low activity
-
-
?
4-chlorobenzaldehyde + NAD+ + H2O
4-chlorobenzoate + NADH + 2 H+
-
high activity
-
-
?
4-hydroxybenzaldehyde + NAD+ + H2O
4-hydroxybenzoate + NADH + 2 H+
-
low activity
-
-
?
4-methoxybenzaldehyde + NAD+ + H2O
4-methoxybenzoate + NADH + 2 H+
-
low activity
-
-
?
4-nitrobenzaldehyde + NAD+ + H2O
4-nitrobenzoate + NADH + 2 H+
-
moderate activity
-
-
?
glutaraldehyde + NAD+ + H2O
glutarate + NADH + 2 H+
-
very low activity
-
-
?
isovaleraldehyde + NAD+ + H2O
isovalerate + NADH + 2 H+
-
very low activity
-
-
?
m-nitrobenzaldehyde + NAD+ + H2O
m-nitrobenzoate + NADH + H+
-
-
-
?
o-nitrobenzaldehyde + NAD+ + H2O
o-nitrobenzoate + NADH + H+
-
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH + 2 H+
-
very low activity
-
-
?
5-chlorosalicylaldehyde + NAD+ + H2O
5-chlorosalicylate + NADH + H+
-
-
-
?
5-chlorosalicylaldehyde + NAD+ + H2O
5-chlorosalicylate + NADH + H+
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + 2 H+
-
moderate to high activity
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + 2 H+
highest substrate specificity for benzaldehyde
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + 2 H+
highest substrate specificity for benzaldehyde
-
-
?
caprylic aldehyde + NAD+ + H2O
caprylic acid + NADH + H+
-
-
-
?
caprylic aldehyde + NAD+ + H2O
caprylic acid + NADH + H+
-
-
-
?
glutaraldehyde + NAD+ + H2O
glutarate + NADH + H+
-
-
-
?
o-methoxybenzaldehyde + NAD+ + H2O
o-methoxybenzoate + NADH + H+
-
-
-
?
o-methoxybenzaldehyde + NAD+ + H2O
o-methoxybenzoate + NADH + H+
-
-
-
?
salicylaldehyde + NAD+ + H2O
salicylate + NADH
-
intermediate in the degradation pathway of naphthalene to catechol
-
?
salicylaldehyde + NAD+ + H2O
salicylate + NADH
-
intermediate in the degradation pathway of naphthalene to catechol
-
?
salicylaldehyde + NAD+ + H2O
salicylate + NADH
-
intermediate in the degradation pathway of naphthalene to catechol
-
?
salicylaldehyde + NAD+ + H2O
salicylate + NADH
-
intermediate in the degradation pathway of naphthalene to catechol
-
?
salicylaldehyde + NAD+ + H2O
salicylate + NADH + 2 H+
-
-
-
?
salicylaldehyde + NAD+ + H2O
salicylate + NADH + 2 H+
amino acids Asn149 and Glu250 may bind salicylaldehyde
-
-
?
salicylaldehyde + NAD+ + H2O
salicylate + NADH + 2 H+
-
conversion of salicylaldehyde to salicylate in Pseudomonas putida ND6 is mediated by two isofunctional, inducible, plasmid-encoded enzymes, NahF and NahV
-
-
?
salicylaldehyde + NAD+ + H2O
salicylate + NADH + 2 H+
-
conversion of salicylaldehyde to salicylate in Pseudomonas putida ND6 is mediated by two isofunctional, inducible, plasmid-encoded enzymes, NahF and NahV
-
-
?
salicylaldehyde + NAD+ + H2O
salicylate + NADH + 2 H+
second highest substrate specificity for benzaldehyde
-
-
?
salicylaldehyde + NAD+ + H2O
salicylate + NADH + 2 H+
second highest substrate specificity for benzaldehyde
-
-
?
salicylaldehyde + NAD+ + H2O
salicylate + NADH + H+
best substrate
-
-
?
salicylaldehyde + NAD+ + H2O
salicylate + NADH + H+
-
activity assay
-
-
?
additional information
?
-
-
nah operon in Pseudomonas putida, which is present on the 83 kb metabolic plasmid NAH7 includes nahF gene coding for salicylaldehyde dehydrogenase
-
-
?
additional information
?
-
-
nahV mRNA levels are 3fold lower than the nahF mRNA levels in the wild-type ND6 strain
-
-
?
additional information
?
-
-
nah operon in Pseudomonas putida, which is present on the 83 kb metabolic plasmid NAH7 includes nahF gene coding for salicylaldehyde dehydrogenase
-
-
?
additional information
?
-
-
nahV mRNA levels are 3fold lower than the nahF mRNA levels in the wild-type ND6 strain
-
-
?
additional information
?
-
-
the enzyme shows maximum activity on salicylaldehyde and very poor activity on aliphatic aldehydes. The preferences of substrate (derivatives of benzaldehyde) for enzyme SALDH are dependent on nature, position and group of substituents. Enzyme SALDH prefers: (1) hydroxyl derivative at ortho and meta position, (2) chloro and nitro derivative at meta and para position, and (3) methoxy at meta position. The carboxyl group substitution is poorly preferred. Enzyme SALDH also shows activity on di-aromatic aldehydes. Substrate specificity, overview
-
-
?
additional information
?
-
the enzyme's salicylaldehyde dehydrogenase specific activity is higher than its aldehyde dehydrogenase specific activity
-
-
-
additional information
?
-
-
the enzyme's salicylaldehyde dehydrogenase specific activity is higher than its aldehyde dehydrogenase specific activity
-
-
-
additional information
?
-
the enzyme's salicylaldehyde dehydrogenase specific activity is higher than its aldehyde dehydrogenase specific activity
-
-
-
additional information
?
-
-
the enzyme's salicylaldehyde dehydrogenase specific activity is higher than its aldehyde dehydrogenase specific activity
-
-
-
additional information
?
-
-
involved in the degradation of acenaphthylene
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
involved in the degradation of acenaphthylene
-
-
?
salicylaldehyde + NAD+ + H2O
salicylate + NADH
-
intermediate in the degradation pathway of naphthalene to catechol
-
?
salicylaldehyde + NAD+ + H2O
salicylate + NADH
-
intermediate in the degradation pathway of naphthalene to catechol
-
?
salicylaldehyde + NAD+ + H2O
salicylate + NADH
-
intermediate in the degradation pathway of naphthalene to catechol
-
?
salicylaldehyde + NAD+ + H2O
salicylate + NADH
-
intermediate in the degradation pathway of naphthalene to catechol
-
?
salicylaldehyde + NAD+ + H2O
salicylate + NADH + 2 H+
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
amino acid residues Trp148, Phe226, Gly228, and Phe381 may bind NAD+, predicted binding mode based on modelling and molecular dynamic simulation. The adenine dinucleotide part of NAD+ is stabilized by Gly208, Glu209, Val212, Phe226, Gly228, Val232, Ile236, Glu379, and Phe381. The dinucleotide also forms a hydrogen bond with Lys172, Glu175, and Asn213. The nicotinamide of NAD+ interacts with Trp148 and Asn149 via hydrogen bond formation. Pro147, Leu251, and Gly252 contribute the binding by hydrophobic interactions. A conformational change occurred in the NAD+ binding site, which may facilitate NADH release
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Zn2+
additional information
additional information
-
external addition of Ca2+, Mg2+, Fe2+ and Fe3+ at 10 mM, either as sulfate or chloride salts, fail to show an increase in the enzyme activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Al3+
inhibits NahF activity by 42%; inhibits NahV activity by 15%
Ba2+
inhibits NahF activity by 62%; inhibits NahV activity by 52%
Ca2+
inhibits NahF activity by 63%; inhibits NahV activity by 35%
Cs+
inhibits NahF activity by 44%; inhibits NahV activity by 69%
Li+
inhibits NahF activity by 50%; inhibits NahV activity by 57%
Mg2+
inhibits NahF activity by 34%; inhibits NahV activity by 36%
Ni2+
inhibits NahF activity by 60%; inhibits NahV activity by 70%
Salicylaldehyde
-
substrate inhibition, 86% and 70% decrease in activity at 0.05 mM and 0.1 mM, respectively
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0035
2-naphthaldehyde
-
pH 8.0, temperature not specified in the publication
0.0039
3-Chlorobenzaldehyde
-
pH 8.0, temperature not specified in the publication
0.0021
3-Hydroxybenzaldehyde
-
pH 8.0, temperature not specified in the publication
0.0064
4-Chlorobenzaldehyde
-
pH 8.0, temperature not specified in the publication
0.011
4-nitrobenzaldehyde
-
pH 8.0, temperature not specified in the publication
0.0449
NAD+
pH 7.5, 35°C, recombinant His-tagged mutant N149A
0.0523
NAD+
pH 7.5, 35°C, recombinant His-tagged mutant N149A
0.1056
NAD+
pH 7.5, 35°C, recombinant His-tagged mutant E175A
0.0038
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged enzyme
0.0045
Salicylaldehyde
-
pH 8.0, temperature not specified in the publication
0.0046
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged mutant V153A
0.0095
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged mutant V153A
0.0151
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged mutant E175A
additional information
additional information
bisubstrate Michaelis-Menten kinetics
-
additional information
additional information
-
bisubstrate Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics for NAD+
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
65
3-Chlorobenzaldehyde
-
pH 8.0, temperature not specified in the publication
18
3-Hydroxybenzaldehyde
-
pH 8.0, temperature not specified in the publication
98
4-Chlorobenzaldehyde
-
pH 8.0, temperature not specified in the publication
59
4-nitrobenzaldehyde
-
pH 8.0, temperature not specified in the publication
157.6
NAD+
pH 7.5, 35°C, recombinant His-tagged mutant E175A
208.8
NAD+
pH 7.5, 35°C, recombinant His-tagged mutant N149A
254.5
NAD+
pH 7.5, 35°C, recombinant His-tagged mutant N149A
82.2
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged mutant E175A
100.4
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged mutant N149A
123.6
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged enzyme
153.5
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged mutant V153A
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
29000
2-naphthaldehyde
-
pH 8.0, temperature not specified in the publication
21500
3-Chlorobenzaldehyde
-
pH 8.0, temperature not specified in the publication
8800
3-Hydroxybenzaldehyde
-
pH 8.0, temperature not specified in the publication
12400
4-Chlorobenzaldehyde
-
pH 8.0, temperature not specified in the publication
6000
4-nitrobenzaldehyde
-
pH 8.0, temperature not specified in the publication
1492
NAD+
pH 7.5, 35°C, recombinant His-tagged mutant E175A
3992
NAD+
pH 7.5, 35°C, recombinant His-tagged mutant N149A
5668
NAD+
pH 7.5, 35°C, recombinant His-tagged mutant N149A
5444
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged mutant E175A
10568
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged mutant N149A
32526
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged enzyme
33370
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged mutant V153A
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.136
2-naphthaldehyde
-
pH 8.0, temperature not specified in the publication