Information on EC 1.14.13.1 - salicylate 1-monooxygenase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.14.13.1
-
RECOMMENDED NAME
GeneOntology No.
salicylate 1-monooxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
salicylate + NADH + 2 H+ + O2 = catechol + NAD+ + H2O + CO2
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
oxidative decarboxylation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
chlorosalicylate degradation
-
-
methylsalicylate degradation
-
-
salicylate degradation I
-
-
phenol degradation
-
-
Dioxin degradation
-
-
Polycyclic aromatic hydrocarbon degradation
-
-
Naphthalene degradation
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
SYSTEMATIC NAME
IUBMB Comments
salicylate,NADH:oxygen oxidoreductase (1-hydroxylating, decarboxylating)
A flavoprotein (FAD).
CAS REGISTRY NUMBER
COMMENTARY hide
9059-28-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
phenanthrene-degrading
-
-
Manually annotated by BRENDA team
phenanthrene-degrading
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
strain BI
-
-
Manually annotated by BRENDA team
strain BI
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain BS202-P1, grown on phenanthrene
-
-
Manually annotated by BRENDA team
strain ND6
-
-
Manually annotated by BRENDA team
strain ND6
-
-
Manually annotated by BRENDA team
strain AN10
-
-
Manually annotated by BRENDA team
strain AN10
-
-
Manually annotated by BRENDA team
Sphingobium sp.
strain P2
-
-
Manually annotated by BRENDA team
strain P2
-
-
Manually annotated by BRENDA team
strain CHY-1
-
-
Manually annotated by BRENDA team
strain CHY-1
-
-
Manually annotated by BRENDA team
-
Q4P3T3
UniProt
Manually annotated by BRENDA team
-
Q4P3T3
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-hydroxy-2-naphthoate + NADH + 2 H+ + O2
?
show the reaction diagram
1-hydroxy-2-naphthoate + NADH + O2
1,2-dihydroxynaphthalene + CO2 + H2O + NAD+
show the reaction diagram
-
-
-
-
?
2,3-dihydroxybenzoate + NADH + O2
pyrogallol + CO2 + H2O + NAD+
show the reaction diagram
2,4,6,8,10,12-hexanitro-2,4,6,8,10,12-hexaazaisowurzitane + NADH
NO2- + N2O + formate + NH4+
show the reaction diagram
-
the enzyme catalyzes two oxygen-sensitive single-electron transfer steps necessary to release two nitrite ions from 2,4,6,8,10,12-hexanitro-2,4,6,8,10,12-hexaazaisowurzitane and this is followed by the secondary decomposition of this energetic chemical
N2O is abiotically produced from NO2-NH2
-
?
2,4-dihydroxybenzoate + NAD(P)H + O2
benzene-1,2,4-triol + CO2 + H2O + NAD(P)+
show the reaction diagram
-
-
-
?
2,4-dihydroxybenzoate + NADH + 2 H+ + O2
1,2,4-trihydroxybenzene + NAD+ + H2O + CO2
show the reaction diagram
2,5-dihydroxybenzoate + NADH + O2
benzene-1,2,5-triol + CO2 + H2O + NAD+
show the reaction diagram
2,6-dihydroxybenzoate + NADH + 2 H+ + O2
1,2,3-trihydroxybenzene + NAD+ + H2O + CO2
show the reaction diagram
2,6-dihydroxybenzoate + NADH + O2
pyrogallol + CO2 + H2O + NAD+
show the reaction diagram
2-hydroxy-1-naphthoate + NADH + 2 H+ + O2
?
show the reaction diagram
3,5-dinitrosalicylate + NADH + O2
? + NAD+ + H2O + CO2
show the reaction diagram
3-chlorosalicylate + NADH + H+ + O2
3-chlorocatechol + NAD+ + H2O
show the reaction diagram
3-methylsalicylate + NADH + 2 H+ + O2
3-methylcatechol + NAD+ + H2O + CO2
show the reaction diagram
-
76% of the activity with salicylate
-
-
?
3-methylsalicylate + NADH + H+ + O2
3-methylcatechol + NAD+ + H2O
show the reaction diagram
3-methylsalicylate + NADH + O2
1,2-dihydroxy-3-methylbenzene + CO2 + NAD+ + H2O
show the reaction diagram
3-methylsalicylate + NADH + O2
1,2-dihydroxy-3-methylbenzene + NAD+ + H2O + CO2
show the reaction diagram
4-(3-benzothiazol-2-yl-4-cyano-2-oxo-2H-chromen-7-yloxymethyl)-2-hydroxy-benzoic acid + O2 + NADH + 2 H+
?
show the reaction diagram
-
i.e. SHLF, two-step synthesis of a long-wavelength latent fluorogenic substrate SHLF. In the presence of NADH and under aerobic conditions, SHL catalyzes the decarboxylative hydroxylation of SHLF followed by a quinonemethide-type rearrangement reaction concomitant with the ejection of a fluorescence coumarin 2, which is spontaneous and irreversible at physiological temperatures in aqueous media. The fluorescence signal generated by this process is specific and, in the near red spectral region with an emission maximum at 595 nm, is suppressed by salicylic acid
-
-
?
4-aminosalicylate + NADH + O2
4-aminocatechol + CO2 + NAD+ + H2O
show the reaction diagram
4-chlorosalicylate + NADH + H+ + O2
4-chlorocatechol + NAD+ + H2O
show the reaction diagram
4-chlorosalicylate + NADH + O2
1,2-dihydroxy-4-chlorobenzene + CO2 + NAD+ + H2O
show the reaction diagram
4-chlorosalicylate + NADH + O2
4-chlorocatechol + NAD+ + H2O + CO2
show the reaction diagram
4-methylsalicylate + NADH + 2 H+ + O2
4-methylcatechol + NAD+ + H2O + CO2
show the reaction diagram
4-methylsalicylate + NADH + O2
1,2-dihydroxy-4-methylbenzene + CO2 + NAD+ + H2O
show the reaction diagram
5-aminosalicylate + NADH + O2
5-aminocatechol + CO2 + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
5-chlorosalicylate + NADH + 2 H+ + O2
4-chlorocatechol + NAD+ + H2O + CO2
show the reaction diagram
-
46% of the activity with salicylate
-
-
?
5-chlorosalicylate + NADH + H+ + O2
5-chlorocatechol + NAD+ + H2O
show the reaction diagram
5-chlorosalicylate + NADH + O2
1,2-dihydroxy-5-chlorobenzene + CO2 + NAD+ + H2O
show the reaction diagram
5-chlorosalicylate + NADH + O2
1,2-dihydroxy-5-chlorobenzene + NAD+ + H2O + CO2
show the reaction diagram
5-fluorosalicylate + NADH + O2
1,2-dihydroxy-5-fluorobenzene + CO2 + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
5-methoxysalicylate + NADH + O2
1,2-dihydroxy-5-methoxybenzene + CO2 + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
5-methylsalicylate + NADH + 2 H+ + O2
4-methylcatechol + NAD+ + H2O + CO2
show the reaction diagram
-
68.5% of the activity with salicylate
-
-
?
5-methylsalicylate + NADH + 2 H+ + O2
5-methylcatechol + NAD+ + H2O + CO2
show the reaction diagram
5-methylsalicylate + NADH + O2
1,2-dihydroxy-5-methoxybenzene + NAD+ + H2O + CO2
show the reaction diagram
5-methylsalicylate + NADH + O2
1,2-dihydroxy-5-methylbenzene + CO2 + NAD+ + H2O
show the reaction diagram
5-nitrosalicylate + NADH + 2 H+ + O2
4-nitrocatechol + NAD+ + H2O + CO2
show the reaction diagram
-
32% of the activity with salicylate
-
-
?
anthranilate + NADH + 2 H+ + O2
2-aminophenol + NAD+ + H2O + CO2
show the reaction diagram
-
67% of the activity with salicylate
-
-
?
aspirin + NADH + O2
? + NAD+ + H2O + CO2
show the reaction diagram
-
-
-
-
?
gentisate + NADH + 2 H+ + O2
?
show the reaction diagram
-
99% of the activity with salicylate
-
-
?
m-hydroxybenzoate + NADH + O2
1,3-dihydroxybenzene + CO2 + NAD+ + H2O
show the reaction diagram
-
6% of the reaction with salicylate
-
-
?
o-iodophenol + NADH + O2
catechol + iodide + NAD+
show the reaction diagram
-
-
-
-
?
o-nitrophenol + NADH + O2
catechol + nitrite + NAD+
show the reaction diagram
p-aminosalicylate + NADH + O2
1,2-dihydroxy-4-aminobenzene + NAD+ + CO2 + H2O
show the reaction diagram
salicylaldehyde + NADH + O2
catechol + formate + NAD+
show the reaction diagram
-
mechanism
-
-
?
salicylate + NADH + 2 H+ + O2
catechol + NAD+ + H2O + CO2
show the reaction diagram
-
-
-
-
?
salicylate + NADH + H+ + O2
catechol + NAD+ + H2O
show the reaction diagram
salicylate + NADH + O2
catechol + NAD+ + H2O + CO2
show the reaction diagram
salicylate + NADH + O2
catechol + NAD+ + O2
show the reaction diagram
Sphingobium sp.
-
-
-
-
?
salicylate + O2 + NADH + 2 H+
catechol + CO2 + H2O + NAD+
show the reaction diagram
salicylate + O2 + NADPH + 2 H+
catechol + CO2 + H2O + NADP+
show the reaction diagram
sulfosalicylate + NADH + O2
? + NAD+ + H2O + CO2
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
4-methylsalicylate + NADH + 2 H+ + O2
4-methylcatechol + NAD+ + H2O + CO2
show the reaction diagram
5-methylsalicylate + NADH + 2 H+ + O2
5-methylcatechol + NAD+ + H2O + CO2
show the reaction diagram
salicylate + O2 + NADH + 2 H+
catechol + CO2 + H2O + NAD+
show the reaction diagram
salicylate + O2 + NADPH + 2 H+
catechol + CO2 + H2O + NADP+
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
-
three-component Fe-S protein complex: the oxygenase component, designated PhnII, exhibits an alpha3beta3 heterohexameric structure and contains one Rieske-type [2Fe-2S] cluster and one mononuclear iron per alpha subunit
additional information
-
no metal ion requirement
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
-
-
1-hydroxy-2-naphthoate
-
strong competitive inhibition of salicylate hydroxylation
ascorbic acid
-
slight
Benzoate
-
competitive inhibitor
Na2MoO4
-
slight
O2
-
inhibits biotransformation of 2,4,6,8,10,12-hexanitro-2,4,6,8,10,12-hexaazaisowurzitane
p-chloromercuribenzoate
-
-
Trinitrobenzenesulfonic acid
-
irreversible inactivation, modification of a lysine residue results in loss of NADH-dehydrogenase activity suggesting its role in the NADH-binding site of the enzyme
additional information
-
chemical modification of one arginine residue with glyoxal causes the enzyme to act as dehydrogenase, but not as oxygenase
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
flavin 1,N6-ethenoadenine dinucleotide
-
weaker binding to the apoenzyme than FAD
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.004
1-hydroxy-2-naphthoate
-
-
0.028
2,3-Dihydroxybenzoate
0.143
2,4-Dihydroxybenzoate
-
cosubstrate NADH
0.065
2,5-Dihydroxybenzoate
0.011
2,6-Dihydroxybenzoate
0.0038
3-chlorosalicylate
-
pH not specified in the publication, 25C
0.0127
3-methylsalicylate
-
pH not specified in the publication, 25C
0.0042
4-(3-benzothiazol-2-yl-4-cyano-2-oxo-2H-chromen-7-yloxymethyl)-2-hydroxy-benzoic acid
-
pH 8.0, 37C
0.0028
4-chlorosalicylate
-
pH not specified in the publication, 25C
0.0158
4-methylsalicylate
-
pH not specified in the publication, 25C
0.0006
5-chlorosalicylate
-
pH not specified in the publication, 25C
0.0024
5-Methylsalicylate
-
pH not specified in the publication, 25C
0.028
anthranilate
-
30C, pH 7.0
0.0026 - 0.23
NADH
0.1
NADPH
0.034
o-Nitrophenol
0.13 - 0.196
O2
0.015
p-Aminosalicylate
0.087
Salicylaldehyde
-
-
0.0005 - 0.0096
salicylate
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.3
3-chlorosalicylate
Pseudomonas reinekei
-
pH not specified in the publication, 25C
2.2
3-methylsalicylate
Pseudomonas reinekei
-
pH not specified in the publication, 25C
0.00075
4-(3-benzothiazol-2-yl-4-cyano-2-oxo-2H-chromen-7-yloxymethyl)-2-hydroxy-benzoic acid
Pseudomonas sp.
-
pH 8.0, 37C
2.9
4-chlorosalicylate
Pseudomonas reinekei
-
pH not specified in the publication, 25C
6.4
4-methylsalicylate
Pseudomonas reinekei
-
pH not specified in the publication, 25C
1.6
5-chlorosalicylate
Pseudomonas reinekei
-
pH not specified in the publication, 25C
7.8
5-Methylsalicylate
Pseudomonas reinekei
-
pH not specified in the publication, 25C
5.4
NADH
Pseudomonas reinekei
-
pH not specified in the publication, 25C
4.6
salicylate
Pseudomonas reinekei
-
pH not specified in the publication, 25C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
340
3-chlorosalicylate
Pseudomonas reinekei
-
pH not specified in the publication, 25C
14712
170
3-methylsalicylate
Pseudomonas reinekei
-
pH not specified in the publication, 25C
8609
1000
4-chlorosalicylate
Pseudomonas reinekei
-
pH not specified in the publication, 25C
9055
410
4-methylsalicylate
Pseudomonas reinekei
-
pH not specified in the publication, 25C
11584
2700
5-chlorosalicylate
Pseudomonas reinekei
-
pH not specified in the publication, 25C
6458
3300
5-Methylsalicylate
Pseudomonas reinekei
-
pH not specified in the publication, 25C
6463
340
NADH
Pseudomonas reinekei
-
pH not specified in the publication, 25C
8
480
salicylate
Pseudomonas reinekei
-
pH not specified in the publication, 25C
617
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00068
1-hydroxy-2-naphthoate
-
30C, pH 7.0
3.1
Benzoate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000256
-
biotransformation of 2,4,6,8,10,12-hexanitro-2,4,6,8,10,12-hexaazaisowurzitane
0.0017
-
salicylate-grown cells, pH 7.5, 30C
0.0127
-
phenanthrene-grown cells, pH 7.5, 30C
0.58
-
reaction with salicylate
1.27
-
enzyme form NahG, using 3,5-dinitrosalicylate as substrate, at 20C
1.53
-
enzyme form NahU, using sulfosalicylate as substrate, at 20C
3.17
-
enzyme form NahG, using salicylate as substrate, at 20C
3.63
-
enzyme form NahG, using 5-chlorosalicylate as substrate, at 20C
3.91
-
enzyme form NahG, using 5-methylsalicylate as substrate, at 20C
4.04
-
enzyme form NahG, using 3-methylsalicylate as substrate, at 20C
4.12
-
enzyme form NahG, using aspirin as substrate, at 20C
4.24
-
enzyme form NahG, using sulfosalicylate as substrate, at 20C
5.25
-
enzyme form NahU, using 5-chlorosalicylate as substrate, at 20C
10.59
-
enzyme form NahU, using 3-methylsalicylate as substrate, at 20C
18.79
-
enzyme form NahU, using 5-methylsalicylate as substrate, at 20C
23.44
-
enzyme form NahU, using salicylate as substrate, at 20C
25.64
-
enzyme form NahU, using aspirin as substrate, at 20C
85
-
purified enzyme from 4-methylsalicylate-grown cells, pH not specified in the publication, 25C, substrate salicylate
90
-
purified enzyme from 5-methylsalicylate-grown cells, pH not specified in the publication, 25C, substrate salicylate
190
-
purified enzyme from 5-chlorosalicylate-grown cells, pH not specified in the publication, 25C, substrate 5-chlorosalicylate
240
-
purified enzyme from 5-chlorosalicylate-grown cells, pH not specified in the publication, 25C, substrate 4-chlorosalicylate
460
-
purified enzyme from 5-chlorosalicylate-grown cells, pH not specified in the publication, 25C, substrate salicylate
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8.5
-
-
7.5
-
assay at
7.5 - 8
-
-
7.8
-
substrate salicylaldehyde
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
-
65% of maximal activity at pH 6, 96% of maximal activity at pH 8
6 - 10
-
about 50% of activity maximum at pH 6 and 10
6.5 - 8.5
-
about 75% of activity maximum at pH 6.5 and 8.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
-
assay at
25 - 27
-
assay at
37
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 50
-
62% of maximal activity at 20C, 70% of maximal activity at 50C, no activity at 55C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Rhodococcus jostii (strain RHA1)
Rhodococcus jostii (strain RHA1)
Rhodococcus jostii (strain RHA1)
Rhodococcus jostii (strain RHA1)
Rhodococcus jostii (strain RHA1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43000 - 48700
-
gel filtration, sedimentation equilibrium, calculation of MW per flavin
43000
-
SDS-PAGE
43400 - 45300
-
gel filtration, SDS-PAGE
47000
-
SDS-PAGE
57000
-
SDS-PAGE
57200
-
calculation from diffusion and sedimentation data
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 43000-48700, sedimentation equilibrium
monomer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
apoenzyme is crystallized by dialysis method, using ammonium sulfate as the precipitant
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
-
highest stability
389999
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
apoenzyme unstable above
38
-
2 h, 10% loss of activity in the presence of FAD; 30 min, complete inactivation in absence of FAD
60
-
5 min, cell-free extract, in presence of 1-hydroxy-2-naphthoic acid, inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dithiothreitol, 0.5 mM, stabilizes
-
glycerol, 10%, stabilizes
-
loses its activity after ammonium sulfate fractionation and dialysis, and its full activity is restored by the addition of a heat-stable factor of rat liver
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 20 mM KH2PO4 buffer pH 7.5
-
-20C, stable for a few weeks
-
4C, 0.5 mM dithiothreitol, 10% loss of activity after 1 week
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
affinity chromatography
-
cells grown on 1-hydroxy-2-naphthoate
-
native enzyme from 5-chlorosalicylate-grown cells by anion exchange chromatography and gel filtration
-
Ni-NTA His Bind resin column chromatography
-
oxygenase component PhnII
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
biotransformation experiments with resting cells of Escherichia coli JM109 harboring recombinant ahd genes reveal that AhdA2cA1c, AhdA1dA2d, and AhdA1eA2e can function as a salicylate 1-hydroxylase
Sphingobium sp.
-
expressed in Escherichia coli strain BL21(DE3)
-
expression in Arabidopsis thalaina, with chloroplast targeting sequence
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expression in Escherichia coli
-
gene salA, DNA and amino acid sequence determination and analysis, phylogenetic analysis
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transgenic Populus tremula x Populus alba hybrid expressing the nahG transgene. Expression of nahG decreases quinic acid conjugates and increased catechol glucoside, while exerting little effect on levels of salicylic acid and catechol, the substrate and product, respectively, of the nahG enzyme
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
5-chlorosalicylate induces the enzyme
gene Shy1 is transcriptionally induced during the biotrophic stages of development but not required for virulence during seedling infection. The trigger for Shy1 transcriptional induction is salicylic acid
in mixed Pseudomonas reinekei MT1 with Achromobacter xylosoxidans MT3 cultures, analyzed by 2-D electrophoresis
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K163E
-
site directed mutagenesis, Lys163 is involved in the NADH-binding site
K163G
-
site directed mutagenesis, Lys163 is involved in the NADH-binding site
K163R
-
site directed mutagenesis, Lys163 is involved in the NADH-binding site
additional information
-
construction of transgenic plants, using wild-type Columbia(0) plants and sid2 mutant plants, overexpressing the bacterial NahG, germination of NahG transgenic plants is influenced to a lesser degree by high salinity. Catechol accumulates in the transgenic plants and acts as an antioxidant that compromises the inhibitory effects of high salinity. Salicylic acid promotes seed germination under high salinity by modulating antioxidant activity in transgenic Arabidopsis thaliana, detailed overview
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
diagnostics
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usage of the enzyme in a fluorescence assay that detects 3-hydroxybutyrate and cholesterol in the nanomolar range and is more sensitive than the current SHL-dehydrogenase amperometric sensors, making it applicable to the construction of a fiber-optic fluorescence biosensor for clinical diagnostic uses
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