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EC Tree
Word Map
1.2.1.7
tumefaciens
virb10
walker
brucella
atpases
pylori
avirulent
helicobacter
traffic
nucleotide-binding
merodiploid
transdominant
abortus
nucleoprotein
nonpolar
brucellosis
nonfunctional
halves
hexameric
tumor-inducing
energize
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
ppbadh, 4-hydroxy benzaldehyde dehydrogenase,
more
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4-hydroxy benzaldehyde dehydrogenase
-
-
4-hydroxybenzaldehyde dehydrogenase
-
-
NAD(P)-dependent benzaldehyde dehydrogenase
NADP-linked benzaldehyde dehydrogenase
-
-
-
-
mdlD
-
NAD(P)-dependent benzaldehyde dehydrogenase
-
NAD(P)-dependent benzaldehyde dehydrogenase
-
-
PpBADH
-
additional information
see also EC 1.2.1.28
additional information
see also EC 1.2.1.28
-
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benzaldehyde + NADP+ + H2O = benzoate + NADPH + H+
benzaldehyde + NADP+ + H2O = benzoate + NADPH + H+
inducible by mandelic acid
-
benzaldehyde + NADP+ + H2O = benzoate + NADPH + H+
inducible by xenobiotics, like DDT and TCDD
-
benzaldehyde + NADP+ + H2O = benzoate + NADPH + H+
inducible by xenobiotics, like DDT and TCDD
-
benzaldehyde + NADP+ + H2O = benzoate + NADPH + H+
-
-
-
-
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oxidation
-
-
-
-
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benzaldehyde:NADP+ oxidoreductase
-
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2,4-dihydroxybenzaldehyde + NAD+ + H2O
2,4-dihydroxybenzoate + NADH + H+
-
-
-
-
?
3,4-dihydroxybenzaldehyde + NAD+ + H2O
3,4-dihydroxybenzoate + NADH + H+
-
-
-
-
?
3-hydroxy-4-methoxybenzaldehyde + NAD+ + H2O
3-hydroxy-4-methoxybenzoate + NADH + H+
-
-
-
-
?
3-hydroxybenzaldehyde + NAD+ + H2O
3-hydroxybenzoate + NADH + H+
-
-
-
-
?
3-methoxybenzaldehyde + NAD+ + H2O
3-methoxybenzoate + NADH + H+
-
-
-
-
?
4-chlorobenzaldehyde + H2O + NADP+
4-chlorobenzoate + NADPH + 2 H+
4-hydroxy-3-methoxybenzaldehyde + NAD+ + H2O
4-hydroxy-3-methoxybenzoate + NADH + H+
-
-
-
-
?
4-hydroxybenzaldehyde + NAD+ + H2O
4-hydroxybenzoate + NADH + H+
-
-
-
-
?
4-hydroxybenzaldehyde + NADP+ + H2O
4-hydroxybenzoate + NADPH + H+
4-methoxybenzaldehyde + H2O + NADP+
4-methoxybenzoate + NADPH + 2 H+
4-nitrobenzaldehyde + H2O + NADP+
4-nitrobenzoate + NADPH + 2 H+
benzaldehyde + H2O + NADP+
benzoate + NADPH + 2 H+
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
-
-
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
isovanillin + NADP+ + H2O
3-hydroxy-4-methoxybenzoate + NADPH
-
-
-
-
?
salicylaldehyde + NADP+ + H2O
salicylic acid + NADPH
-
-
-
-
?
additional information
?
-
4-chlorobenzaldehyde + H2O + NADP+
4-chlorobenzoate + NADPH + 2 H+
-
-
-
?
4-chlorobenzaldehyde + H2O + NADP+
4-chlorobenzoate + NADPH + 2 H+
-
-
-
?
4-hydroxybenzaldehyde + NADP+ + H2O
4-hydroxybenzoate + NADPH + H+
-
-
-
?
4-hydroxybenzaldehyde + NADP+ + H2O
4-hydroxybenzoate + NADPH + H+
-
-
-
?
4-methoxybenzaldehyde + H2O + NADP+
4-methoxybenzoate + NADPH + 2 H+
-
-
-
?
4-methoxybenzaldehyde + H2O + NADP+
4-methoxybenzoate + NADPH + 2 H+
-
-
-
?
4-nitrobenzaldehyde + H2O + NADP+
4-nitrobenzoate + NADPH + 2 H+
-
-
-
?
4-nitrobenzaldehyde + H2O + NADP+
4-nitrobenzoate + NADPH + 2 H+
-
-
-
?
benzaldehyde + H2O + NADP+
benzoate + NADPH + 2 H+
-
-
-
?
benzaldehyde + H2O + NADP+
benzoate + NADPH + 2 H+
-
-
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
-
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
-
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
-
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
-
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
-
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
-
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
-
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
-
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
Pseudomonas enzyme on plasmid also active with NAD+, see also EC 1.2.1.28
-
ir
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
metabolic pathway of mandelic acid
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
metabolic pathway of phenylglycine
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
-
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
metabolic pathway of phenylglycine
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
Pseudomonas enzyme on plasmid also active with NAD+, see also EC 1.2.1.28
-
ir
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
-
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
-
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
-
-
?
additional information
?
-
specificity data for PpBADH shows that long chain aliphatics containing 5-8 carbons have about twice the relative rate of reactivity than benzaldehyde. As the chain length decreases, the activity declines quickly, with less than 0.1% activity being observed with acetaldehyde. Structure-function analysis
-
-
-
additional information
?
-
-
specificity data for PpBADH shows that long chain aliphatics containing 5-8 carbons have about twice the relative rate of reactivity than benzaldehyde. As the chain length decreases, the activity declines quickly, with less than 0.1% activity being observed with acetaldehyde. Structure-function analysis
-
-
-
additional information
?
-
specificity data for PpBADH shows that long chain aliphatics containing 5-8 carbons have about twice the relative rate of reactivity than benzaldehyde. As the chain length decreases, the activity declines quickly, with less than 0.1% activity being observed with acetaldehyde. Structure-function analysis
-
-
-
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4-hydroxybenzaldehyde + NADP+ + H2O
4-hydroxybenzoate + NADPH + H+
benzaldehyde + H2O + NADP+
benzoate + NADPH + 2 H+
benzaldehyde + NADP+ + H2O
benzoate + NADPH
4-hydroxybenzaldehyde + NADP+ + H2O
4-hydroxybenzoate + NADPH + H+
-
-
-
?
4-hydroxybenzaldehyde + NADP+ + H2O
4-hydroxybenzoate + NADPH + H+
-
-
-
?
benzaldehyde + H2O + NADP+
benzoate + NADPH + 2 H+
-
-
-
?
benzaldehyde + H2O + NADP+
benzoate + NADPH + 2 H+
-
-
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
-
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
-
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
-
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
-
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
-
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
-
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
Pseudomonas enzyme on plasmid also active with NAD+, see also EC 1.2.1.28
-
ir
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
metabolic pathway of mandelic acid
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
metabolic pathway of phenylglycine
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
metabolic pathway of phenylglycine
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
Pseudomonas enzyme on plasmid also active with NAD+, see also EC 1.2.1.28
-
ir
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
-
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
-
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
-
-
?
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NAD+
-
-
NAD+
-
enzyme on Pseudomonas plasmid
NADP+
-
-
additional information
PpBADH is able to utilize both NAD+ and NADP+, selective mechanism, overview
-
additional information
-
PpBADH is able to utilize both NAD+ and NADP+, selective mechanism, overview
-
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K+
-
or NH4+ or Rb+ required for maximal activity
K+
-
or NH4+ or Rb+ required for maximal activity
Rb+
-
or K+ or NH4+ required for maximal activity
Rb+
-
or K+ or NH4+ required for maximal activity
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p-hydroxymercuribenzoate
-
-
Disulfiram
-
-
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K+
-
125 mM KCl, 1.5 fold increase in activity
Na+
-
125 mM NaCl, 1.5 fold increase in activity
NH4+
-
or K+ or Rb+ required for maximal activity
NH4+
-
or K+ or Rb+ required for maximal activity
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0.037
3,4-Dihydroxybenzaldehyde
-
apparent KM
0.044
4-hydroxy-3-methoxybenzaldehyde
-
apparent KM
0.006
4-hydroxybenzaldehyde
-
apparent KM
0.0002 - 0.1
benzaldehyde
0.0002
benzaldehyde
-
-
0.029
benzaldehyde
-
apparent KM
0.037
NADP+
-
-
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25
3,4-Dihydroxybenzaldehyde
-
apparent Kcat
18
4-hydroxy-3-methoxybenzaldehyde
-
apparent Kcat
4
4-hydroxybenzaldehyde
-
apparent Kcat
4.6
benzaldehyde
-
apparent Kcat
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0.0086
-
4-hydroxybenzaldehyde and also benzaldehyde
0.034
-
cells grown on benzoate
0.065
-
cells grown on benzyl alcohol
0.091
-
cells grown on toluene
0.132
-
cells grown on benzaldehyde
0.28
-
cells grown on D-phenylglycine
0.3
-
cells grown on L-phenylglycine
22
-
IMAC eluted 4-hydroxy benzaldehyde dehydrogenase, total activity 35 Units, protein concentration 0.27 mg/ml
3.2
-
clarified lysate, total activity 37 U, protein concentration 5.77 mg/ml
additional information
-
-
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8.5
-
-
9.3
-
-
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6.9 - 10.7
-
the activities measured at pH 6.85 and 10.7 are approximately 30% of the activity measured at pH 9.3
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21 - 45
-
21°C 100%, 37°C 90%, 45°C 75% activity
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5.6
-
determined by isoelectric focusing electrophoresis
5.8
-
predicted from the amino acid sequence
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-
-
-
brenda
flounder
-
-
brenda
-
-
-
brenda
-
UniProt
brenda
MT53
-
-
brenda
-
-
-
brenda
-
-
-
brenda
strain K172, formerly Pseudomonas strain K172
-
-
brenda
-
-
-
brenda
-
UniProt
brenda
MT53
-
-
brenda
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-
-
brenda
-
early eosinophilic focus, basophilic adenoma and hepatocellular carcinom
brenda
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evolution
benzaldehyde dehydrogenase from Pseudomonas putida (PpBADH) belongs to the Class 3 aldehyde dehydrogenase (ALDH) family. The Class 3 ALDHs are unusual in that they are generally dimeric (rather than tetrameric), relatively non-specific and utilize both NAD+ and NADP+. The pattern of cofactor binding for the rat Class 3 ALDH differs from that of PpBADH and other ALDHs
evolution
-
benzaldehyde dehydrogenase from Pseudomonas putida (PpBADH) belongs to the Class 3 aldehyde dehydrogenase (ALDH) family. The Class 3 ALDHs are unusual in that they are generally dimeric (rather than tetrameric), relatively non-specific and utilize both NAD+ and NADP+. The pattern of cofactor binding for the rat Class 3 ALDH differs from that of PpBADH and other ALDHs
-
metabolism
benzaldehyde dehydrogenase (PpBADH) is the terminal enzyme in the mandelamide/mandelate pathway of Pseudomonas putida strain ATCC 12633, it catalyzes the conversion of benzaldehyde to benzoic acid with the concomitant reduction of NAD+ (EC 1.2.1.28) or NADP+ (EC 1.2.1.7) to NADH or NADPH, respectively. Benzoic acid subsequently enters the beta-oxoadipate pathway and the citric acid cycle
metabolism
-
benzaldehyde dehydrogenase (PpBADH) is the terminal enzyme in the mandelamide/mandelate pathway of Pseudomonas putida strain ATCC 12633, it catalyzes the conversion of benzaldehyde to benzoic acid with the concomitant reduction of NAD+ (EC 1.2.1.28) or NADP+ (EC 1.2.1.7) to NADH or NADPH, respectively. Benzoic acid subsequently enters the beta-oxoadipate pathway and the citric acid cycle
-
additional information
two conserved glutamates, at positions 215 and 337, act as the general base necessary to hydrolyze the thioacyl intermediate, structure-activity relationship, mechanism, overview. Glu215 is the likely candidate for PpBADH, a result more typical of the Class 1 and 2 ALDH families. Hydride transfer is not rate limiting, lending further credence to the suggestion that PpBADH is more similar to the Class 1 and 2 ALDHs than it is to other Class 3 ALDHs. Structure comparisons
additional information
-
two conserved glutamates, at positions 215 and 337, act as the general base necessary to hydrolyze the thioacyl intermediate, structure-activity relationship, mechanism, overview. Glu215 is the likely candidate for PpBADH, a result more typical of the Class 1 and 2 ALDH families. Hydride transfer is not rate limiting, lending further credence to the suggestion that PpBADH is more similar to the Class 1 and 2 ALDHs than it is to other Class 3 ALDHs. Structure comparisons
additional information
-
two conserved glutamates, at positions 215 and 337, act as the general base necessary to hydrolyze the thioacyl intermediate, structure-activity relationship, mechanism, overview. Glu215 is the likely candidate for PpBADH, a result more typical of the Class 1 and 2 ALDH families. Hydride transfer is not rate limiting, lending further credence to the suggestion that PpBADH is more similar to the Class 1 and 2 ALDHs than it is to other Class 3 ALDHs. Structure comparisons
-
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MDLD_PSEPU
436
0
47435
Swiss-Prot
-
AL3B1_BOVIN
468
0
51800
Swiss-Prot
other Location (Reliability: 4 )
AL3B1_HUMAN
468
0
51840
Swiss-Prot
Mitochondrion (Reliability: 4 )
AL3B1_MOUSE
468
0
52292
Swiss-Prot
other Location (Reliability: 2 )
AL3B1_RAT
468
0
52147
Swiss-Prot
other Location (Reliability: 3 )
A0A1J5S9M2_9ZZZZ
459
0
51315
TrEMBL
other Location (Reliability: 2 )
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116000
-
determined by gel filtration
200000
-
sucrose density gradient centrifugation
55000
-
determined by SDS-PAGE
56300
-
4 * 56300, SDS-PAGE
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?
-
? x 57000, sequence determination
tetramer
-
4 * 56300, SDS-PAGE
tetramer
-
4 * 56300, SDS-PAGE
-
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purified recombinant enzyme in complex with NADP+ and NADP+/benzoate, sitting drop vapour diffusion method, mixing of 10 mg/ml protein in 100 mM HEPES, 100 mM KCl, 2 mM DTT, 2 mM NADP+, pH 7.5, and 1 mM benzoate (for the complex cyrstals), with crystallization solution containing 2.0 M ammonium sulfate and 5% v/v isopropanol, 5-7 days, X-ray diffraction structure determination and analysis at 2.28 A resolution
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E215D
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
E215L
site-directed mutagenesis, inactive mutant
E215Q
site-directed mutagenesis, inactive mutant
E337D
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
E337L
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
E337Q
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
E215D
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
-
E215L
-
site-directed mutagenesis, inactive mutant
-
E215Q
-
site-directed mutagenesis, inactive mutant
-
E337D
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
-
E337Q
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
-
additional information
-
random mutagenesis of plasmid encoded benzaldehyde dehydrogenase gene xylC, expression in Escherichia coli
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50
-
inactivation after 5 min
additional information
-
heat-labile
additional information
-
heat-labile
additional information
-
heat-labile
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-17°C, pH 7.2, 10 mM dithiothreitol, several months
-
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on a His-Trap FF IMAC column
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
-
-
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expression in Escherichia coli K12 derivatives
-
gene mdlD, recombinant epression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
into the vector pET-Duet1 for expression in Escherichia coli BL21DE3 cells
-
restriction mapping of native plasmids, subcloning of the operon in Escherichia coli and Pseudomonas sp.
-
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Van den Tweel, W.J.J.; Smits, J.P.; de Bont, J.A.M.
Microbial metabolism of D- and L-phenylglycine by Pseudomonas putida LW-4
Arch. Microbiol.
144
169-174
1986
Pseudomonas putida
-
brenda
Tsou, A.Y.; Ransom, S.C.; Gerlt, J.A.; Buechter, D.D.; Babbitt, P.C.; Kenyon, G.L.
Mandelate pathway of Pseudomonas putida: sequence relationships involving mandelate racemase, (S)-mandelate dehydrogenase, and benzoylformate decarboxylase and expression of benzoylformate decarboxylase in Escherichia coli
Biochemistry
29
9856-9862
1990
Pseudomonas putida
brenda
Altenschmidt, U.; Fuchs, G.
Anaerobic degradation of toluene in denitrifying Pseudomonas sp.: indication for toluene methylhydroxylation and benzoyl-CoA as central aromatic intermediate
Arch. Microbiol.
156
152-158
1991
Pseudomonas sp.
brenda
Chalmers, R.M.; Scott, A.J.; Fewson, C.A.
Purification of the benzyl alcohol dehydrogenase and benzaldehyde dehydrogenase encoded by the TOL plasmid pWW53 of Pseudomonas putida MT53 and their preliminary comparison with benzyl alcohol dehydrogenase and benzaldehyde dehydrogenases I and II from Acinetobacter calcoaceticus
J. Gen. Microbiol.
136
637-643
1990
Pseudomonas putida, Pseudomonas putida MT53
-
brenda
Harayama, S.; Rekik, M.; Wubbolts, M.; Rose, K.; Leppik, R.A.; Timmis, K.N.
Characterization of five genes in the upper-pathway operon of TOL plasmid pWW0 from Pseudomonas putida and identification of the gene products
J. Bacteriol.
171
5048-5055
1989
Pseudomonas putida
brenda
Shaw, L.E.; Williams, P.A.
Physical and functional mapping of two cointegrate plasmids derived from RP4 and TOL plasmid pDK1
J. Gen. Microbiol.
134
2463-2474
1988
Pseudomonas putida
brenda
Keil, H.; Saint, C.M.; Williams, P.A.
Gene organization of the first catabolic operon of TOL plasmid pWW53: production of indigo by the xylA gene product
J. Bacteriol.
169
764-770
1987
Pseudomonas putida
brenda
Bhat, S.G.; Vaidyanathan, C.S.
Involvement of 4-hydroxymandelic acid in the degradation of mandelic acid by Pseudomonas convexa
J. Bacteriol.
127
1108-1118
1976
Pseudomonas putida
brenda
Stachow, C.S.; Stevenson, I.L.; Day, D.
Purification and properties of nicotinamide adenine dinucleotide phosphate-specific benzaldehyde dehydrogenase from Pseudomonas
J. Biol. Chem.
242
5294-5300
1967
Pseudomonas fluorescens
brenda
Kohler, A.; Broeg, K.; Bahns, S.
Localization of a tumor-associated phenotype of benzaldehyde dehydrogenase in liver carcinogenesis of flounder by quantitative histochemistry
Mar. Environ. Res.
46
185-189
1998
Platichthys flesus, Rattus norvegicus
-
brenda
Biergert, T.; Fuchs, G.
Anaerobic oxidation of toluene (analogues) to benzoate (analogues) by whole cells and by cell extracts of a denitrifying Thauera sp.
Arch. Microbiol.
163
407-417
1995
Thauera sp.
-
brenda
Gosling, A.; Zachariou, M.; Straffon, M.
Purification and characterisation of a 4-hydroxy benzaldehyde dehydrogenase cloned from Acinetobacter baylyi
Enzyme Microb. Technol.
43
417-422
2008
Acinetobacter baylyi
-
brenda
Zahniser, M.P.D.; Prasad, S.; Kneen, M.M.; Kreinbring, C.A.; Petsko, G.A.; Ringe, D.; McLeish, M.J.
Structure and mechanism of benzaldehyde dehydrogenase from Pseudomonas putida ATCC 12633, a member of the Class 3 aldehyde dehydrogenase superfamily
Protein Eng. Des. Sel.
30
271-278
2017
Pseudomonas putida (Q84DC3), Pseudomonas putida, Pseudomonas putida ATCC 12633 (Q84DC3)
brenda
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