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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
-
-
?
5-chlorosalicylaldehyde + NAD+ + H2O
5-chlorosalicylate + NADH + H+
acetaldehyde + NAD+ + H2O
acetate + NADH + 2 H+
benzaldehyde + NAD+ + H2O
benzoate + NADH + 2 H+
butyraldehyde + NAD+ + H2O
butyrate + NADH + 2 H+
-
low activity
-
-
?
caprylic aldehyde + NAD+ + H2O
caprylic acid + NADH + H+
formaldehyde + NAD+ + H2O
formate + NADH + 2 H+
formaldehyde + NAD+ + H2O
formate + NADH + H+
glutaraldehyde + NAD+ + H2O
glutarate + NADH + 2 H+
-
very low activity
-
-
?
glutaraldehyde + NAD+ + H2O
glutarate + NADH + H+
glyoxal + NAD+ + H2O
glyoxylate + NADH + H+
-
-
-
?
isovaleraldehyde + NAD+ + H2O
isovalerate + NADH + 2 H+
-
very low activity
-
-
?
m-nitrobenzaldehyde + NAD+ + H2O
m-nitrobenzoate + NADH + H+
-
-
-
?
o-methoxybenzaldehyde + NAD+ + H2O
o-methoxybenzoate + NADH + H+
o-nitrobenzaldehyde + NAD+ + H2O
o-nitrobenzoate + NADH + H+
-
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH + 2 H+
-
very low activity
-
-
?
salicylaldehyde + NAD+ + H2O
salicylate + NADH
salicylaldehyde + NAD+ + H2O
salicylate + NADH + 2 H+
salicylaldehyde + NAD+ + H2O
salicylate + NADH + H+
additional information
?
-
5-chlorosalicylaldehyde + NAD+ + H2O
5-chlorosalicylate + NADH + H+
-
-
-
?
5-chlorosalicylaldehyde + NAD+ + H2O
5-chlorosalicylate + NADH + H+
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + 2 H+
-
very low activity
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + 2 H+
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + 2 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+
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH + 2 H+
-
very low activity
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH + 2 H+
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH + 2 H+
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH + H+
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH + H+
-
-
-
?
glutaraldehyde + NAD+ + H2O
glutarate + 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
-
-
-
?
salicylaldehyde + NAD+ + H2O
salicylate + NADH
-
-
-
?
salicylaldehyde + NAD+ + H2O
salicylate + NADH
-
-
-
?
salicylaldehyde + NAD+ + H2O
salicylate + NADH
-
-
-
?
salicylaldehyde + NAD+ + H2O
salicylate + NADH
-
-
-
?
salicylaldehyde + NAD+ + H2O
salicylate + NADH
-
-
-
?
salicylaldehyde + NAD+ + H2O
salicylate + NADH
-
-
-
?
salicylaldehyde + NAD+ + H2O
salicylate + NADH
-
-
-
?
salicylaldehyde + NAD+ + H2O
salicylate + NADH
-
-
-
?
salicylaldehyde + NAD+ + H2O
salicylate + NADH
-
-
-
?
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+
-
-
-
-
?
salicylaldehyde + NAD+ + H2O
salicylate + NADH + 2 H+
-
best substrate
-
-
?
salicylaldehyde + NAD+ + H2O
salicylate + NADH + 2 H+
-
-
-
?
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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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
0.001
benzaldehyde
-
pH 8.0, temperature not specified in the publication
0.0038 - 0.146
Salicylaldehyde
additional information
additional information
-
0.00016
NAD+
-
0.0395
NAD+
pH 7.5, 35°C, recombinant His-tagged enzyme
0.0449
NAD+
pH 7.5, 35°C, recombinant His-tagged mutant N149A
0.052
NAD+
-
pH 8.0, temperature not specified in the publication
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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96
2-naphthaldehyde
-
pH 8.0, temperature not specified in the publication
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
26.4
benzaldehyde
-
pH 8.0, temperature not specified in the publication
82.2 - 153.5
Salicylaldehyde
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
234.3
NAD+
pH 7.5, 35°C, recombinant His-tagged enzyme
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
93.6
Salicylaldehyde
-
pH 8.0, temperature not specified in the publication
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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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
5444 - 33370
Salicylaldehyde
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
5932
NAD+
pH 7.5, 35°C, recombinant His-tagged enzyme
5444
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged mutant E175A
10568
Salicylaldehyde
pH 7.5, 35°C, recombinant His-tagged mutant N149A
23000
Salicylaldehyde
-
pH 8.0, temperature not specified in the publication
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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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
-
mineralization of naphthalene, detoxification of salicylaldehyde
metabolism
-
NahF catalyzes the last reaction in the conversion of naphthalene to salicylate
metabolism
pathway for the degradation of carbaryl via gentisate, overview. Various enzymes are involved in the metabolic pathway, including salicylaldehyde dehydroganse
metabolism
the salicylaldehyde dehydrogenases is involved in the naphthalene degradation pathway
metabolism
-
mineralization of naphthalene, detoxification of salicylaldehyde
-
metabolism
-
NahF catalyzes the last reaction in the conversion of naphthalene to salicylate
-
physiological function
salicylaldehyde dehydrogenase is responsible for the oxidation of salicylaldehyde to salicylate using NAD+ as a cofactor in the naphthalene degradation pathway
physiological function
-
the enzyme catalyzes the oxidation of salicylaldehyde to salicylate in the carbaryl-degrading Pseudomonas sp. strain C6
additional information
substrate binding induces a conformational change
additional information
-
substrate binding induces a conformational change
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NAHF_PSEPU
483
0
51994
Swiss-Prot
-
NAHF_PSEU8
483
0
51994
Swiss-Prot
-
D8P271_RALSL
484
0
50259
TrEMBL
-
F6CVG5_MARPP
Marinomonas posidonica (strain CECT 7376 / NCIMB 14433 / IVIA-Po-181)
482
0
50655
TrEMBL
-
A0A7X5XC45_STRMQ
486
0
50000
TrEMBL
-
A0A653BBL3_PSEOL
483
0
51237
TrEMBL
-
A0A0E1UP46_BURPE
521
0
54046
TrEMBL
-
A0A235AIW9_9HYPH
481
0
50214
TrEMBL
-
A0A0E1VRJ5_BURPE
482
0
49506
TrEMBL
-
K0PNI2_9HYPH
481
0
50110
TrEMBL
-
A0A060IGS1_9HYPH
483
0
50404
TrEMBL
-
B1H5G1_BURPE
521
0
54032
TrEMBL
-
A0A0E1U6Q6_BURPE
521
0
54076
TrEMBL
-
A0A0E1SGM9_BURPE
521
0
54046
TrEMBL
-
C4KR91_BURPE
483
0
49638
TrEMBL
-
H0SPD9_BRAS3
Bradyrhizobium sp. (strain ORS 375)
482
0
50613
TrEMBL
-
A0A063BK68_9BURK
483
0
50280
TrEMBL
-
A0A1W6GT57_9HYPH
483
0
50063
TrEMBL
-
L0NKC0_9HYPH
483
0
50761
TrEMBL
-
I3QHK7_9PSED
159
1
16709
TrEMBL
-
F0MC22_PSEPM
483
0
51275
TrEMBL
-
F0MC22_PSEPM
Pseudarthrobacter phenanthrenivorans (strain DSM 18606 / JCM 16027 / LMG 23796 / Sphe3)
483
0
51275
TrEMBL
-
C5P1G2_COCP7
Coccidioides posadasii (strain C735)
476
0
50665
TrEMBL
other Location (Reliability: 1)
K0JV02_SACES
Saccharothrix espanaensis (strain ATCC 51144 / DSM 44229 / JCM 9112 / NBRC 15066 / NRRL 15764)
486
0
50234
TrEMBL
-
A0A7U4LA11_RHIET
483
0
50275
TrEMBL
-
W6RTF0_9HYPH
481
0
50112
TrEMBL
-
D8NG28_RALSL
484
0
50069
TrEMBL
-
F6F1R6_SPHCR
488
0
50949
TrEMBL
-
F0MC43_PSEPM
Pseudarthrobacter phenanthrenivorans (strain DSM 18606 / JCM 16027 / LMG 23796 / Sphe3)
483
0
51135
TrEMBL
-
A0A7U8D711_BURML
521
0
54046
TrEMBL
-
A0A084G6Z1_PSEDA
351
0
38334
TrEMBL
other Location (Reliability: 2)
B9BTE6_9BURK
493
0
50579
TrEMBL
-
A0A1W6PR30_9HYPH
487
0
50642
TrEMBL
-
B8MJT3_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
492
0
53125
TrEMBL
other Location (Reliability: 3)
A0A7U4Z8B4_9RHOB
478
0
52041
TrEMBL
-
A0A2C9ENP0_PSEPH
Pseudomonas protegens (strain DSM 19095 / LMG 27888 / CFBP 6595 / CHA0)
482
0
50122
TrEMBL
-
W6WB59_RHIS8
Rhizobium sp. (strain CF080)
476
0
49196
TrEMBL
-
K0Q4V3_9HYPH
483
0
50511
TrEMBL
-
H0TGD3_9BRAD
735
0
76973
TrEMBL
-
A0A8D9SBR7_BURPB
Burkholderia pseudomallei (strain 1106b)
521
0
54074
TrEMBL
-
A0A081REG5_SPHCR
488
0
50896
TrEMBL
-
F2JZR2_MARM1
Marinomonas mediterranea (strain ATCC 700492 / JCM 21426 / NBRC 103028 / MMB-1)
481
0
50578
TrEMBL
-
M5CBN5_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
436
0
47157
TrEMBL
Mitochondrion (Reliability: 3)
A0A238DM97_9BURK
99
0
10523
TrEMBL
-
F6CVH2_MARPP
Marinomonas posidonica (strain CECT 7376 / NCIMB 14433 / IVIA-Po-181)
501
0
53954
TrEMBL
-
A0A235AKD8_9HYPH
483
0
50142
TrEMBL
-
W6W9L9_RHIS8
Rhizobium sp. (strain CF080)
481
0
50416
TrEMBL
-
A0A1W6PQH8_9HYPH
481
0
50238
TrEMBL
-
F6AM48_DELSC
Delftia sp. (strain Cs1-4)
483
0
50365
TrEMBL
-
A8EA15_BURPE
457
0
46813
TrEMBL
-
A0A0B7FM59_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
508
0
54788
TrEMBL
other Location (Reliability: 2)
A3P443_BURP0
Burkholderia pseudomallei (strain 1106a)
521
0
54074
TrEMBL
-
G0F0C9_CUPNN
Cupriavidus necator (strain ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453 / N-1)
483
0
49617
TrEMBL
-
A0A1W6KYU1_9HYPH
487
0
50720
TrEMBL
-
A8EKQ9_BURPE
521
0
54046
TrEMBL
-
A0A0F4YRG3_TALEM
486
0
51632
TrEMBL
other Location (Reliability: 2)
A0A4Y1MT36_9PROT
486
0
50985
TrEMBL
-
W9TAK9_9PSED
483
0
52040
TrEMBL
-
F6AJ46_PSEF1
Pseudomonas fulva (strain 12-X)
482
0
50239
TrEMBL
-
A0A1W6GT45_9HYPH
481
0
50317
TrEMBL
-
A3RSM0_RALSU
Ralstonia solanacearum (strain UW551)
484
0
50251
TrEMBL
-
A0A158SPW2_9SPHN
465
0
48726
TrEMBL
-
A0A084G2D7_PSEDA
475
0
51033
TrEMBL
other Location (Reliability: 2)
A0A1B9VHZ4_9PROT
485
0
51082
TrEMBL
-
A0A0F8DIP4_CERFI
475
0
49625
TrEMBL
other Location (Reliability: 3)
B6AU72_9RHOB
478
0
51704
TrEMBL
-
B9B468_9BURK
483
0
49433
TrEMBL
-
A0A0M4CMN6_9CORY
483
0
51427
TrEMBL
-
A0A1W6KYP4_9HYPH
481
0
50362
TrEMBL
-
A0A0D5LYZ1_9GAMM
483
0
50436
TrEMBL
-
W6WAV3_RHIS8
Rhizobium sp. (strain CF080)
485
0
51319
TrEMBL
-
A0A084GE61_PSEDA
504
0
53529
TrEMBL
other Location (Reliability: 2)
A0A291LTT3_9NOCA
290
0
30477
TrEMBL
-
F5Z5S7_ALTNA
483
0
51666
TrEMBL
-
Q6XUJ4_PSEPU
483
0
51994
TrEMBL
-
Q6XUN9_PSEPU
483
0
50846
TrEMBL
-
Q1XGL7_PSEPU
483
0
52190
TrEMBL
-
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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
two genes code for salicylaldehyde dehydrogenase. NahF resides in the naphthalene degradation upper pathway operon as the meta-cleavage pathway gene, whereas NahV is situated outside of this operon. NahF-like genes occur in all naphthalene-degradation bacteria, whereas nahV-like genes are present in only some naphthalene-degrading bacteria
additional information
two genes code for salicylaldehyde dehydrogenase. NahF resides in the naphthalene degradation upper pathway operon as the meta-cleavage pathway gene, whereas NahV is situated outside of this operon. NahF-like genes occur in all naphthalene-degradation bacteria, whereas nahV-like genes are present in only some naphthalene-degrading bacteria
additional information
two genes code for salicylaldehyde dehydrogenase. NahF resides in the naphthalene degradation upper pathway operon as the meta-cleavage pathway gene, whereas NahV is situated outside of this operon. NahF-like genes occurr in all naphthalene-degradation bacteria, whereas nahV-like genes are present in only some naphthalene-degrading bacteria
additional information
two genes code for salicylaldehyde dehydrogenase. NahF resides in the naphthalene degradation upper pathway operon as the meta-cleavage pathway gene, whereas NahV is situated outside of this operon. NahF-like genes occurr in all naphthalene-degradation bacteria, whereas nahV-like genes are present in only some naphthalene-degrading bacteria
additional information
-
two genes code for salicylaldehyde dehydrogenase. NahF resides in the naphthalene degradation upper pathway operon as the meta-cleavage pathway gene, whereas NahV is situated outside of this operon. NahF-like genes occurr in all naphthalene-degradation bacteria, whereas nahV-like genes are present in only some naphthalene-degrading bacteria
-
additional information
-
two genes code for salicylaldehyde dehydrogenase. NahF resides in the naphthalene degradation upper pathway operon as the meta-cleavage pathway gene, whereas NahV is situated outside of this operon. NahF-like genes occur in all naphthalene-degradation bacteria, whereas nahV-like genes are present in only some naphthalene-degrading bacteria
-
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Manohar, S.; Karegoudar, T.B.
Degradation of naphthalene by a Pseudomonas strain NGK1
Indian J. Exp. Biol.
33
353-356
1995
Pseudomonas sp., Pseudomonas sp. NGK1
brenda
Eaton, R.W.; Chapman, P.J.
Bacterial metabolism of naphthalene: Construction and use of recombinant bacteria to study ring cleavage of 1,2-dihydroxynaphthalene and subsequent reactions
J. Bacteriol.
174
7542-7554
1992
Pseudomonas putida, Pseudomonas putida PpG1064
brenda
Connors, M.A.; Barnsley, E.A.
Metabolism of naphthalene by pseudomonads: Salicylaldehyde as the first possible inducer in the metabolic pathway
J. Bacteriol.
141
1052-1054
1980
Pseudomonas sp.
brenda
Austen, R.A.; Dunn, N.W.
Regulation of the plasmid-specified naphthalene catabolic pathway of Pseudomonas putida
J. Gen. Microbiol.
117
521-528
1980
Pseudomonas putida, Pseudomonas putida PpG7
-
brenda
Barnsley, E.A.
Role and regulation of the ortho and meta pathways of catechol metabolism in pseudomonads metabolising naphthalene and salicylate
J. Bacteriol.
125
404-408
1976
Pseudomonas sp., Pseudomonas putida, Pseudomonas putida PpG7
brenda
Barnsley, E.A.
The induction of the enzymes of naphthalene metabolism in pseudomonads by salicylate and 2-aminobenzoate
J. Gen. Microbiol.
88
193-196
1975
Pseudomonas sp., Pseudomonas putida, Pseudomonas putida PpG7
brenda
Shamsuzzaman, K.M.; Barnsley, E.A.
The regulation of naphthalene metabolism in pseudomonads
Biochem. Biophys. Res. Commun.
60
582-589
1974
Pseudomonas putida
brenda
Zhao, H.; Li, Y.; Chen, W.; Cai, B.
A novel salicylaldehyde dehydrogenase-NahV involved in catabolism of naphthalene from Pseudomonas putida ND6
Chin. Sci. Bull.
52
1942-1948
2007
Pseudomonas putida (Q6XUJ4), Pseudomonas putida (Q6XUN9), Pseudomonas putida ND6 (Q6XUJ4), Pseudomonas putida ND6 (Q6XUN9)
-
brenda
Nayak, A.S.; Veeranagouda, Y.; Lee, K.; Karegoudar, T.B.
Metabolism of acenaphthylene via 1,2-dihydroxynaphthalene and catechol by Stenotrophomonas sp. RMSK
Biodegradation
20
837-843
2009
Stenotrophomonas sp. RMSK
brenda
Coitinho, J.B.; Costa, D.M.; Guimaraes, S.L.; de Goes, A.M.; Nagem, R.A.
Expression, purification and preliminary crystallographic studies of NahF, a salicylaldehyde dehydrogenase from Pseudomonas putida G7 involved in naphthalene degradation
Acta Crystallogr. Sect. F
68
93-97
2012
Pseudomonas putida, Pseudomonas putida G7
brenda
Li, S.; Li, X.; Zhao, H.; Cai, B.
Physiological role of the novel salicylaldehyde dehydrogenase NahV in mineralization of naphthalene by Pseudomonas putida ND6
Microbiol. Res.
166
643-653
2011
Pseudomonas putida, Pseudomonas putida ND6
brenda
Singh, R.; Trivedi, V.D.; Phale, P.S.
Purification and characterization of NAD+-dependent salicylaldehyde dehydrogenase from carbaryl-degrading Pseudomonas sp. strain C6
Appl. Biochem. Biotechnol.
172
806-819
2014
Pseudomonas sp.
brenda
Singh, R.; Trivedi, V.D.; Phale, P.S.
Metabolic regulation and chromosomal localization of carbaryl degradation pathway in Pseudomonas sp. strains C4, C5 and C6
Arch. Microbiol.
195
521-535
2013
Pseudomonas sp. C6 (I3QHK7)
brenda
Jia, B.; Jia, X.; Hyun Kim, K.; Ji Pu, Z.; Kang, M.S.; Ok Jeon, C.
Evolutionary, computational, and biochemical studies of the salicylaldehyde dehydrogenases in the naphthalene degradation pathway
Sci. Rep.
7
43489
2017
Alteromonas naphthalenivorans (F5Z5S7), Alteromonas naphthalenivorans
brenda
Wang, Z.; Sun, Y.; Li, X.; Hu, H.; Zhang, C.
A novel acetaldehyde dehydrogenase with salicylaldehyde dehydrogenase activity from Rhodococcus ruber strain OA1
Curr. Microbiol.
74
1404-1410
2017
Rhodococcus ruber (A0A291LTT3), Rhodococcus ruber, Rhodococcus ruber OA1 (A0A291LTT3), Rhodococcus ruber OA1
brenda