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Information on EC 1.2.1.7 - benzaldehyde dehydrogenase (NADP+)
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1.2.1.7 benzaldehyde dehydrogenase (NADP+)Specify your search results
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
4-hydroxy benzaldehyde dehydrogenase, 4-hydroxybenzaldehyde dehydrogenase, NADP-linked benzaldehyde dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
NADP-linked benzaldehyde dehydrogenase
-
-
-
-
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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
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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
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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
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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-hydroxy-3-methoxybenzaldehyde + NAD+ + H2O
4-hydroxy-3-methoxybenzoate + NADH + H+
-
-
-
-
?
4-hydroxybenzaldehyde + NAD+ + H2O
4-hydroxybenzoate + NADH + H+
-
-
-
-
?
isovanillin + NADP+ + H2O
3-hydroxy-4-methoxybenzoate + NADPH
-
-
-
-
?
4-hydroxybenzaldehyde + NADP+ + H2O
4-hydroxybenzoate + NADPH + H+
-
-
-
?
4-hydroxybenzaldehyde + NADP+ + H2O
4-hydroxybenzoate + NADPH + H+
-
-
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
Pseudomonas enzyme on plasmid also active with NAD+, see also EC 1.2.1.28
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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
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-hydroxybenzaldehyde + NADP+ + H2O
4-hydroxybenzoate + NADPH + H+
-
-
-
?
4-hydroxybenzaldehyde + NADP+ + H2O
4-hydroxybenzoate + NADPH + H+
-
-
-
?
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
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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
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clarified lysate, total activity 37 U, protein concentration 5.77 mg/ml
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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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_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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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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
into the vector pET-Duet1 for expression in Escherichia coli BL21DE3 cells
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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
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