Information on EC 1.2.1.65 - salicylaldehyde dehydrogenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.2.1.65
-
RECOMMENDED NAME
GeneOntology No.
salicylaldehyde dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
salicylaldehyde + NAD+ + H2O = salicylate + NADH + 2 H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
naphthalene degradation (aerobic)
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Naphthalene degradation
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-
Metabolic pathways
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
salicylaldehyde:NAD+ oxidoreductase
Involved in the naphthalene degradation pathway in some bacteria.
CAS REGISTRY NUMBER
COMMENTARY hide
55354-34-2
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
network and phylogenetic analyses indicated that salicylaldehyde dehydrogenases (SALDs) and the homologues are present in bacteria and fungi, phylogenetic tree, distribution, and evolution of SALD, overview. Key residues in SALDs are analyzed by evolutionary methods and a molecular simulation analysis. The catalytic residue is most highly conserved, followed by the residues binding NAD+ and then the residues binding salicylaldehyde, molecular simulation analysis
malfunction
site-directed mutagenesis of selected residues binding NAD+ and/or SAL affects the enzyme's catalytic efficiency, but does not eliminate catalysis. Cys284 is positioned close to both NAD+ and SAL, implicating it as a potentially important residue
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-naphthaldehyde + NAD+ + H2O
1-naphthoate + NADH + 2 H+
show the reaction diagram
-
low activity
-
-
?
2-carboxybenzaldehyde + NAD+ + H2O
2-carboxybenzoate + NADH + 2 H+
show the reaction diagram
-
very low activity
-
-
?
2-chlorobenzaldehyde + NAD+ + H2O
2-chlorobenzoate + NADH + 2 H+
show the reaction diagram
-
low activity
-
-
?
2-methoxybenzaldehyde + NAD+ + H2O
2-methoxybenzoate + NADH + 2 H+
show the reaction diagram
-
low activity
-
-
?
2-naphthaldehyde + NAD+ + H2O
2-naphthoate + NADH + 2 H+
show the reaction diagram
-
moderate activity
-
-
?
2-nitrobenzaldehyde + NAD+ + H2O
2-nitrobenzoate + NADH + 2 H+
show the reaction diagram
-
low activity
-
-
?
3-carboxybenzaldehyde + NAD+ + H2O
3-carboxybenzoate + NADH + 2 H+
show the reaction diagram
-
very low activity
-
-
?
3-chlorobenzaldehyde + NAD+ + H2O
3-chlorobenzoate + NADH + 2 H+
show the reaction diagram
-
moderate activity
-
-
?
3-hydroxybenzaldehyde + NAD+ + H2O
3-hydroxybenzoate + NADH + 2 H+
show the reaction diagram
-
low to moderate activity
-
-
?
3-methoxybenzaldehyde + NAD+ + H2O
3-methoxybenzoate + NADH + 2 H+
show the reaction diagram
-
moderate activity
-
-
?
3-nitrobenzaldehyde + NAD+ + H2O
3-nitrobenzoate + NADH + 2 H+
show the reaction diagram
-
low activity
-
-
?
4-carboxybenzaldehyde + NAD+ + H2O
4-carboxybenzoate + NADH + 2 H+
show the reaction diagram
-
very low activity
-
-
?
4-chlorobenzaldehyde + NAD+ + H2O
4-chlorobenzoate + NADH + 2 H+
show the reaction diagram
-
high activity
-
-
?
4-hydroxybenzaldehyde + NAD+ + H2O
4-hydroxybenzoate + NADH + 2 H+
show the reaction diagram
-
low activity
-
-
?
4-methoxybenzaldehyde + NAD+ + H2O
4-methoxybenzoate + NADH + 2 H+
show the reaction diagram
-
low activity
-
-
?
4-nitrobenzaldehyde + NAD+ + H2O
4-nitrobenzoate + NADH + 2 H+
show the reaction diagram
-
moderate activity
-
-
?
5-chlorosalicylaldehyde + NAD+ + H2O
5-chlorosalicylate + NADH + H+
show the reaction diagram
acetaldehyde + NAD+ + H2O
acetate + NADH + 2 H+
show the reaction diagram
-
very low activity
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + 2 H+
show the reaction diagram
-
moderate to high activity
-
-
?
butyraldehyde + NAD+ + H2O
butyrate + NADH + 2 H+
show the reaction diagram
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low activity
-
-
?
caprylic aldehyde + NAD+ + H2O
caprylic acid + NADH + H+
show the reaction diagram
formaldehyde + NAD+ + H2O
formate + NADH + 2 H+
show the reaction diagram
-
very low activity
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH + H+
show the reaction diagram
glutaraldehyde + NAD+ + H2O
glutarate + NADH + 2 H+
show the reaction diagram
-
very low activity
-
-
?
glutaraldehyde + NAD+ + H2O
glutarate + NADH + H+
show the reaction diagram
glyoxal + NAD+ + H2O
glyoxylate + NADH + H+
show the reaction diagram
isovaleraldehyde + NAD+ + H2O
isovalerate + NADH + 2 H+
show the reaction diagram
-
very low activity
-
-
?
m-nitrobenzaldehyde + NAD+ + H2O
m-nitrobenzoate + NADH + H+
show the reaction diagram
-
-
-
?
o-methoxybenxaldehyde + NAD+ + H2O
o-methoxybenzoate + NADH + H+
show the reaction diagram
-
-
-
?
o-nitrobenzaldehyde + NAD+ + H2O
o-nitrobenzoate + NADH + H+
show the reaction diagram
-
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH + 2 H+
show the reaction diagram
-
very low activity
-
-
?
salicylaldehyde + NAD+ + H2O
salicylate + NADH
show the reaction diagram
salicylaldehyde + NAD+ + H2O
salicylate + NADH + 2 H+
show the reaction diagram
salicylaldehyde + NAD+ + H2O
salicylate + NADH + H+
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
salicylaldehyde + NAD+ + H2O
salicylate + NADH
show the reaction diagram
salicylaldehyde + NAD+ + H2O
salicylate + NADH + 2 H+
show the reaction diagram
additional information
?
-
-
involved in the degradation of acenaphthylene
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-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
enzyme SALDH shows poor activity with NADP+
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
the enzyme contains 1.8 mol/mol of enzyme
Cu2+
enhances NahV activity by 63% activity
K+
-
44% activating at 200 mM
Mg2+
-
the enzyme contains 0.3 mol/mol of enzyme
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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40% inhibition at 1 mM
2,2'-dipyridyl
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50% inhibition at 1 mM
2-naphthaldehyde
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substrate inhibition
3-Chlorobenzaldehyde
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substrate inhibition
3-Hydroxybenzaldehyde
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substrate inhibition
4-Chlorobenzaldehyde
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substrate inhibition
4-Nitrobenzaldehyde
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substrate inhibition
Al3+
inhibits NahF activity by 42%; inhibits NahV activity by 15%
Ba2+
inhibits NahF activity by 62%; inhibits NahV activity by 52%
benzaldehyde
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substrate inhibition
Ca2+
inhibits NahF activity by 63%; inhibits NahV activity by 35%
Cs+
inhibits NahF activity by 44%; inhibits NahV activity by 69%
Cu2+
inhibits NahF activity by 70%
EDTA
-
50% inhibition at 50 mM
EGTA
-
60% inhibition at 50 mM
Li+
inhibits NahF activity by 50%; inhibits NahV activity by 57%
Mg2+
inhibits NahF activity by 34%; inhibits NahV activity by 36%
Na+
-
inhibitory at higher concentration
NADP+
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7% inhibition at 5 mM with 5 mM NAD+
Ni2+
inhibits NahF activity by 60%; inhibits NahV activity by 70%
Salicylaldehyde
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0035
2-naphthaldehyde
-
pH 8.0, temperature not specified in the publication
0.0039
3-Chlorobenzaldehyde
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pH 8.0, temperature not specified in the publication
0.0021
3-Hydroxybenzaldehyde
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pH 8.0, temperature not specified in the publication
0.0064
4-Chlorobenzaldehyde
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pH 8.0, temperature not specified in the publication
0.011
4-Nitrobenzaldehyde
-
pH 8.0, temperature not specified in the publication
0.001
benzaldehyde
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pH 8.0, temperature not specified in the publication
0.00016 - 0.15
NAD+
0.0038 - 0.146
Salicylaldehyde
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
96
2-naphthaldehyde
-
pH 8.0, temperature not specified in the publication
65
3-Chlorobenzaldehyde
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pH 8.0, temperature not specified in the publication
18
3-Hydroxybenzaldehyde
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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
26.4
benzaldehyde
-
pH 8.0, temperature not specified in the publication
157.6 - 254.5
NAD+
82.2 - 153.5
Salicylaldehyde
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
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
26000
benzaldehyde
-
pH 8.0, temperature not specified in the publication
1492 - 5932
NAD+
5444 - 33370
Salicylaldehyde
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.136
2-naphthaldehyde
-
pH 8.0, temperature not specified in the publication
0.0075
3-Chlorobenzaldehyde
-
pH 8.0, temperature not specified in the publication
1.364
3-Hydroxybenzaldehyde
-
pH 8.0, temperature not specified in the publication
0.0773
4-Chlorobenzaldehyde
-
pH 8.0, temperature not specified in the publication
0.126
4-Nitrobenzaldehyde
-
pH 8.0, temperature not specified in the publication
0.306
benzaldehyde
-
pH 8.0, temperature not specified in the publication
0.185 - 0.4616
Salicylaldehyde
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.2
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in cell free extract of Stenotrophomonas sp. RMSK grown on 1-naphthoic acid
0.23
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in cell free extract of Stenotrophomonas sp. RMSK grown on acenaphthylene
0.89
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wild type naphthalene-succinate grown cells
1.33
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salicylate-induced enzyme synthesis
1.36
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salicylate-induced enzyme synthesis
1.8
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strain PpG7, salicylate-induced enzyme synthesis
15
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nahF mutant with naphthalene as the sole carbon and energy source, pH 7.4 and 25°C
36.3
-
purified native enzyme, pH 8.0, temperature not specified in the publication
67.81
-
nahV mutant with naphthalene as the sole carbon and energy source, pH 7.4 and 25°C
85.4
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wild-type ND6 with naphthalene as the sole carbon and energy source, pH 7.4 and 25°C
118
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mutant strain MC4, 2-aminobenzoate induced cells
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
high activity within this range
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 35
high activity within this range
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50000
1 * 50000, SDS-PAGE; 1 * 50000, SDS-PAGE
150000
-
gel filtration
160000
recombinant His-tagged enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotrimer
monomer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystals of recombinant 6xHis-NahF obtained at 291 K and diffracted to 2.42 A resolution
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
72.8% activity is retained for NahF after a 30 min exposure; NahV looses 88.8% activity after a 30 min exposure
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by Ni2+ affinity chromatography followed by gel filtration
-
cell free extracts are prepared
-
His-tagged NahF purified by Ni-NTA chromatography; His-tagged NahV purified by Ni-NTA chromatography
native enzyme 28fold from cellfree extract by anion exchange and hydrophobic interaction chromatography, followed by another step of anion exchange chromatography, and gel filtration
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recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli and Pseudomonas aeruginosa
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mutant strains, lacking induction of enzyme synthesis by naphthalene growth media
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nahF gene subcloned into the pET28a(TEV) vector and the recombinant protein with 6xHis tag at the N-terminaus overexpressed in Escherichia coli BL21 Arctic Express (DE3) cells
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nahF inserted into pET21b(+) and expressed in Escherichia coli BL21 (DE3); nahV inserted into pET21b(+) and expressed in Escherichia coli BL21 (DE3)
SALDH, DNA and amino acid sequence determination and analysis, the gene for SALDH is probably located on the chromosome in strains C4, C5 and C6, sequence comparisons and phylogenetic analysis
sequence comparisons and phylogenetic tree, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
a 10fold increase in nahV expression observed in the ND6-NahF mutant when cultured in the presence of naphthalene and a 30fold increase when cultured in the presence of salicylate; nahF expression levels in the ND6-NahV mutant elevated by 20fold compared to the levels observed in the wild-type strain cultured in the presence of naphthalene and a 5fold increase when cultured in the presence of salicylate
SALD from Alteromonas naphthalenivorans (SALDan) is specifically upregulated in response to naphthalene
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E175A
site-directed mutagenesis, the apparent Km value of the mutant enzyme to NAD+ is increased by about 2times and the kcat/Km toward the cofactor decreased by 4times. The Km value of the mutant toward salicylaldehyde also increases and the catalytic efficiency decreases by 6times compared to the wild-type enzyme
N149A
site-directed mutagenesis, the catalyic efficiency of the mutant is decreased compared to the wild-type enzyme
V153A
site-directed mutagenesis, the mutation has no significant effect on the kinetic parameters for either NAD+ or salicylaldehyde compared to the wild-type enzyme
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
environmental protection
-
the ability to degrade acenaphthylene and other aromatic compounds makes this strain ideal candidate for application in remediation at the contaminated sites
additional information