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Information on EC 1.2.1.7 - benzaldehyde dehydrogenase (NADP+)
for references in articles please use BRENDA:EC1.2.1.7
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EC Tree 1 Oxidoreductases
1.2 Acting on the aldehyde or oxo group of donors
1.2.1 With NAD+ or NADP+ as acceptor
1.2.1.7 benzaldehyde dehydrogenase (NADP+)
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
showSynonyms
ppbadh, 4-hydroxy benzaldehyde dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
NADP-linked benzaldehyde dehydrogenase
-
-
-
-
PpBADH
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
benzaldehyde + NADP+ + H2O = benzoate + NADPH + 2 H+
inducible by mandelic acid
-
benzaldehyde + NADP+ + H2O = benzoate + NADPH + 2 H+
inducible by xenobiotics, like DDT and TCDD
-
benzaldehyde + NADP+ + H2O = benzoate + NADPH + 2 H+
inducible by xenobiotics, like DDT and TCDD
-
benzaldehyde + NADP+ + H2O = benzoate + NADPH + 2 H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
-
-
-
-
oxidation
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
MetaCyc
2,5-xylenol and 3,5-xylenol degradation, m-cresol degradation, mandelate degradation I
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SYSTEMATIC NAME
IUBMB Comments
benzaldehyde:NADP+ oxidoreductase
-
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CAS REGISTRY NUMBER
COMMENTARY
9028-89-1
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,4-dihydroxybenzaldehyde + NAD+ + H2O
2,4-dihydroxybenzoate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
3,4-dihydroxybenzaldehyde + NAD+ + H2O
3,4-dihydroxybenzoate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
3-hydroxy-4-methoxybenzaldehyde + NAD+ + H2O
3-hydroxy-4-methoxybenzoate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
3-hydroxybenzaldehyde + NAD+ + H2O
3-hydroxybenzoate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
3-methoxybenzaldehyde + NAD+ + H2O
3-methoxybenzoate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
4-chlorobenzaldehyde + H2O + NADP+
4-chlorobenzoate + NADPH + 2 H+
Substrates: -
Products: -
Products: -
?
4-hydroxy-3-methoxybenzaldehyde + NAD+ + H2O
4-hydroxy-3-methoxybenzoate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
4-hydroxybenzaldehyde + NAD+ + H2O
4-hydroxybenzoate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
4-methoxybenzaldehyde + H2O + NADP+
4-methoxybenzoate + NADPH + 2 H+
Substrates: -
Products: -
Products: -
?
4-nitrobenzaldehyde + H2O + NADP+
4-nitrobenzoate + NADPH + 2 H+
Substrates: -
Products: -
Products: -
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
isovanillin + NADP+ + H2O
3-hydroxy-4-methoxybenzoate + NADPH
-
Substrates: -
Products: -
Products: -
?
salicylaldehyde + NADP+ + H2O
salicylic acid + NADPH
-
Substrates: -
Products: -
Products: -
?
4-hydroxybenzaldehyde + NADP+ + H2O
4-hydroxybenzoate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
4-hydroxybenzaldehyde + NADP+ + H2O
4-hydroxybenzoate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
benzaldehyde + H2O + NADP+
benzoate + NADPH + 2 H+
Substrates: -
Products: -
Products: -
?
benzaldehyde + H2O + NADP+
benzoate + NADPH + 2 H+
Substrates: -
Products: -
Products: -
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
Substrates: -
Products: -
Products: -
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
Substrates: -
Products: -
Products: -
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
Substrates: Pseudomonas enzyme on plasmid also active with NAD+, see also EC 1.2.1.28
Products: -
Products: -
ir
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
Substrates: metabolic pathway of mandelic acid
Products: -
Products: -
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
Substrates: metabolic pathway of phenylglycine
Products: -
Products: -
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
Substrates: -
Products: -
Products: -
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
Substrates: metabolic pathway of phenylglycine
Products: -
Products: -
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
Substrates: Pseudomonas enzyme on plasmid also active with NAD+, see also EC 1.2.1.28
Products: -
Products: -
ir
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-hydroxybenzaldehyde + NADP+ + H2O
4-hydroxybenzoate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
4-hydroxybenzaldehyde + NADP+ + H2O
4-hydroxybenzoate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
benzaldehyde + H2O + NADP+
benzoate + NADPH + 2 H+
Substrates: -
Products: -
Products: -
?
benzaldehyde + H2O + NADP+
benzoate + NADPH + 2 H+
Substrates: -
Products: -
Products: -
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
Substrates: -
Products: -
Products: -
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
Substrates: -
Products: -
Products: -
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
Substrates: Pseudomonas enzyme on plasmid also active with NAD+, see also EC 1.2.1.28
Products: -
Products: -
ir
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
Substrates: metabolic pathway of mandelic acid
Products: -
Products: -
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
Substrates: metabolic pathway of phenylglycine
Products: -
Products: -
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
Substrates: metabolic pathway of phenylglycine
Products: -
Products: -
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
Substrates: Pseudomonas enzyme on plasmid also active with NAD+, see also EC 1.2.1.28
Products: -
Products: -
ir
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
Rb+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
9.3
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
early eosinophilic focus, basophilic adenoma and hepatocellular carcinom
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
additional information
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
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). AL3B1_HUMAN
468
0
51840
Swiss-Prot
other Location (Reliability: 4)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E215D
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
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
additional information
-
random mutagenesis of plasmid encoded benzaldehyde dehydrogenase gene xylC, expression in Escherichia coli
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
EXTERNAL LINKS (specific for EC-Number 1.2.1.7)
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