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Information on EC 1.2.1.28 - benzaldehyde dehydrogenase (NAD+)
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1.2.1.28 benzaldehyde dehydrogenase (NAD+)Specify your search results
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
baldh, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
benzaldehyde dehydrogenase
benzaldehyde dehydrogenase (NAD)
-
-
-
-
BZDH
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
benzaldehyde + NAD+ + H2O = benzoate + NADH + 2 H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
oxidation
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
MetaCyc
1,3-dimethylbenzene degradation to 3-methylbenzoate, 1,4-dimethylbenzene degradation to 4-methylbenzoate, 3-chlorotoluene degradation II, benzoate biosynthesis II (CoA-independent, non-beta-oxidative), benzoate biosynthesis III (CoA-dependent, non-beta-oxidative), mandelate degradation I, salicin biosynthesis, salicortin biosynthesis, toluene degradation to benzoate
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SYSTEMATIC NAME
IUBMB Comments
benzaldehyde:NAD+ oxidoreductase
-
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CAS REGISTRY NUMBER
COMMENTARY
37250-93-4
-
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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-bromobenzaldehyde + NAD+ + H2O
2-bromobenzoate + NADH
-
-
-
?
2-fluorobenzaldehyde + NAD+ + H2O
2-fluorobenzoate + NADH + H+
-
41% of activity with benzaldehyde
-
?
2-hydroxybenzaldehyde + NAD+ + H2O
2-hydroxybenzoate + NADH + 2 H+
-
-
-
-
?
2-methoxybenzaldehyde + NAD+ + H2O
2-methoxybenzoate + NADH + H+
-
-
-
?
2-methylbenzaldehyde + NAD+ + H2O
2-methylbenzoate + NADH + 2 H+
-
-
-
-
?
2-naphthaldehyde + NAD+ + H2O
naphthalene-2-carboxylic acid + NADH + 2 H+
-
-
-
-
?
3,4-dihydroxybenzaldehyde + NAD+ + H2O
3,4-dihydroxybenzoate + NADH + H+
-
-
-
?
3-chlorobenzaldehyde + NAD+ + H2O
3-chlorobenzoate + NADH + 2 H+
-
-
-
-
?
3-hydroxybenzaldehyde + NAD+ + H2O
3-hydroxybenzoate + NADH + 2 H+
-
-
-
-
?
3-methoxy-4-hydroxybenzaldehyde + NAD+ + H2O
3-methoxy-4-hydroxybenzoate + NADH + H+
-
-
-
?
3-methoxybenzaldehyde + NAD+ + H2O
3-methoxybenzoate + NADH + 2 H+
-
-
-
-
?
3-methoxybenzaldehyde + NAD+ + H2O
3-methoxybenzoate + NADH + H+
-
-
-
-
?
3-methylbenzaldehyde + NAD+ + H2O
3-methylbenzoate + NADH + 2 H+
-
-
-
-
?
4-chlorobenzaldehyde + NAD+ + H2O
4-chlorobenzoate + NADH + 2 H+
-
-
-
-
?
4-methoxy-3-hydroxybenzaldehyde + NAD+ + H2O
4-methoxy-3-hydroxybenzoate + NADH + H+
-
-
-
?
4-methoxybenzaldehyde + NAD+ + H2O
4-methoxybenzoate + NADH + 2 H+
-
-
-
-
?
4-methylbenzaldehyde + NAD+ + H2O
4-methylbenzoate + NADH + 2 H+
-
-
-
-
?
cinnamaldehyde + NAD+ + H2O
cinnamate + NADH + H+
-
benzaldehyde dehydrogenase II
-
?
furan-2-carboxyaldehyde + NAD+ + H2O
furan-2-formiate + NADH
-
benzaldehyde dehydrogenase II
-
?
pyridin-3-carboxyaldehyde + NAD+ + H2O
pyridin-3-formiate + NADH
-
benzaldehyde dehydrogenase II
-
?
thiophen-2-carboxyaldehyde + NAD+ + H2O
thiophen-2-formiate + NADH
-
benzaldehyde dehydrogenase II
-
?
2-chlorobenzaldehyde + NAD+ + H2O
2-chlorobenzoate + NADH + H+
-
low activity
-
?
2-chlorobenzaldehyde + NAD+ + H2O
2-chlorobenzoate + NADH + H+
-
low activity
-
?
2-hydroxybenzaldehyde + NAD+ + H2O
2-hydroxybenzoate + NADH + H+
-
benzaldehyde dehydrogenase II
-
?
2-hydroxybenzaldehyde + NAD+ + H2O
2-hydroxybenzoate + NADH + H+
-
39% of activity with benzaldehyde
-
?
2-hydroxybenzaldehyde + NAD+ + H2O
2-hydroxybenzoate + NADH + H+
-
16% of activity with benzaldehyde
-
?
2-hydroxybenzaldehyde + NAD+ + H2O
2-hydroxybenzoate + NADH + H+
-
16% of the activity with benzaldehyde
-
-
?
2-hydroxybenzaldehyde + NAD+ + H2O
2-hydroxybenzoate + NADH + H+
-
-
-
-
?
2-hydroxybenzaldehyde + NAD+ + H2O
2-hydroxybenzoate + NADH + H+
-
-
-
-
?
2-hydroxybenzaldehyde + NAD+ + H2O
2-hydroxybenzoate + NADH + H+
-
-
-
?
2-hydroxybenzaldehyde + NAD+ + H2O
2-hydroxybenzoate + NADH + H+
-
-
-
?
2-methylbenzaldehyde + NAD+ + H2O
2-methylbenzoate + NADH
-
-
-
-
-
2-methylbenzaldehyde + NAD+ + H2O
2-methylbenzoate + NADH
-
13% of activity with benzaldehyde
-
?
2-methylbenzaldehyde + NAD+ + H2O
2-methylbenzoate + NADH
-
low activity
-
?
3-chlorobenzaldehyde + NAD+ + H2O
3-chlorobenzoate + NADH
-
-
-
?
3-chlorobenzaldehyde + NAD+ + H2O
3-chlorobenzoate + NADH
-
low activity
-
?
3-chlorobenzaldehyde + NAD+ + H2O
3-chlorobenzoate + NADH
-
low activity
-
?
3-fluorobenzaldehyde + NAD+ + H2O
3-fluorobenzoate + NADH + H+
-
benzaldehyde dehydrogenase II
-
-
3-fluorobenzaldehyde + NAD+ + H2O
3-fluorobenzoate + NADH + H+
-
98% of activity with benzaldehyde
-
?
3-fluorobenzaldehyde + NAD+ + H2O
3-fluorobenzoate + NADH + H+
-
-
-
?
3-hydroxybenzaldehyde + NAD+ + H2O
3-hydroxybenzoate + NADH + H+
-
benzaldehyde dehydrogenase II
-
?
3-hydroxybenzaldehyde + NAD+ + H2O
3-hydroxybenzoate + NADH + H+
-
222% of activity with benzaldehyde
-
?
3-hydroxybenzaldehyde + NAD+ + H2O
3-hydroxybenzoate + NADH + H+
-
38% of activity with benzaldehyde
-
?
3-hydroxybenzaldehyde + NAD+ + H2O
3-hydroxybenzoate + NADH + H+
-
38% of the activity with benzaldehyde
-
-
?
3-hydroxybenzaldehyde + NAD+ + H2O
3-hydroxybenzoate + NADH + H+
-
-
-
-
?
3-hydroxybenzaldehyde + NAD+ + H2O
3-hydroxybenzoate + NADH + H+
-
-
-
-
?
3-methoxybenzaldehyde + NAD+ + H2O
3-methoxybenzoate + NADH
-
benzaldehyde dehydrogenase II
-
-
-
3-methoxybenzaldehyde + NAD+ + H2O
3-methoxybenzoate + NADH
-
235% of activity with benzaldehyde
-
?
3-methoxybenzaldehyde + NAD+ + H2O
3-methoxybenzoate + NADH
-
-
-
?
3-methylbenzaldehyde + NAD+ + H2O
3-methylbenzoate + NADH
-
-
-
-
-
3-methylbenzaldehyde + NAD+ + H2O
3-methylbenzoate + NADH
-
119% of activity with benzaldehyde
-
?
3-methylbenzaldehyde + NAD+ + H2O
3-methylbenzoate + NADH
-
-
-
?
3-nitrobenzaldehyde + NAD+ + H2O
3-nitrobenzoate + NADH
-
-
-
?
4-carboxybenzaldehyde + NAD+ + H2O
4-carboxybenzoate + NADH
-
1650% of activity with benzaldehyde
-
?
4-carboxybenzaldehyde + NAD+ + H2O
4-carboxybenzoate + NADH
-
1650% of activity with benzaldehyde
-
?
4-fluorobenzaldehyde + NAD+ + H2O
4-fluorobenzoate + NADH + H+
-
benzaldehyde dehydrogenase II
-
-
4-fluorobenzaldehyde + NAD+ + H2O
4-fluorobenzoate + NADH + H+
-
210% of activity with benzaldehyde
-
?
4-hydroxybenzaldehyde + NAD+ + H2O
4-hydroxybenzoate + NADH + H+
-
-
-
?
4-hydroxybenzaldehyde + NAD+ + H2O
4-hydroxybenzoate + NADH + H+
-
benzaldehyde dehydrogenase II
-
-
4-hydroxybenzaldehyde + NAD+ + H2O
4-hydroxybenzoate + NADH + H+
-
24% of activity with benzaldehyde
-
?
4-hydroxybenzaldehyde + NAD+ + H2O
4-hydroxybenzoate + NADH + H+
-
24% of the activity with benzaldehyde
-
-
?
4-methoxybenzaldehyde + NAD+ + H2O
4-methoxybenzoate + NADH + H+
-
benzaldehyde dehydrogenase II
-
?
4-methoxybenzaldehyde + NAD+ + H2O
4-methoxybenzoate + NADH + H+
-
-
-
-
?
4-methoxybenzaldehyde + NAD+ + H2O
4-methoxybenzoate + NADH + H+
-
90% of activity with benzaldehyde
-
?
4-methylbenzaldehyde + NAD+ + H2O
4-methylbenzoate + NADH
-
-
-
-
-
4-methylbenzaldehyde + NAD+ + H2O
4-methylbenzoate + NADH
-
240% of activity with benzaldehyde
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
benzaldehyde dehydrogenase II exhibits esterase activity with 4-nitrophenyl acetate
-
-
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
benzaldehyde dehydrogenase II exhibits esterase activity with 4-nitrophenyl acetate
-
-
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
benzaldehyde dehydrogenase I exhibits esterase activity, approx. 2% of dehydrogenase activity
-
ir
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
also active with NADP+, see also EC 1.2.1.7
-
ir
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
also active with NADP+, see also EC 1.2.1.7
-
ir
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
-
-
-
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
last step in the biosynthesis of benzoic acid from cinnamic acid, a precursor of xanthones
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
also active with NADP+, see also EC 1.2.1.7
-
ir
hexan-1-al + NAD+ + H2O
hexanoate + NADH
-
benzaldehyde dehydrogenase II
-
-
octan-1-al + NAD+ + H2O
octanoate + NADH
-
benzaldehyde dehydrogenase II
-
?
perillaldehyde + NAD+ + H2O
perillic acid + NADH
-
benzaldehyde dehydrogenase II
-
?
pyridine 4-carboxyaldehyde + NAD+ + H2O
pyridine 4-formiate + NADH
-
benzaldehyde dehydrogenase II
-
?
pyridine 4-carboxyaldehyde + NAD+ + H2O
pyridine 4-formiate + NADH
-
1380% of activity with benzaldehyde
-
?
additional information
?
-
-
enzyme has a broad substrate specificity accepting mono- and di-aromatic aldehydes but not 2-methoxy derivatives or aliphatic primary aldehydes with 1-6 carbon atoms, no activity with NADP+ or NADPH, BZDH prefers benzaldehydes having substitution either at meta- or para-positions
-
-
?
additional information
?
-
-
the enzyme fails to show activity with NADP+ or NADPH and is inactive with 2-methoxybenzaldehyde, 4-hydroxybenzaldehyde, 2-chlorobenzaldehyde, and 1-naphthaldehyde
-
-
-
additional information
?
-
-
enzyme has a broad substrate specificity accepting mono- and di-aromatic aldehydes but not 2-methoxy derivatives or aliphatic primary aldehydes with 1-6 carbon atoms, no activity with NADP+ or NADPH, BZDH prefers benzaldehydes having substitution either at meta- or para-positions
-
-
?
additional information
?
-
-
the enzyme fails to show activity with NADP+ or NADPH and is inactive with 2-methoxybenzaldehyde, 4-hydroxybenzaldehyde, 2-chlorobenzaldehyde, and 1-naphthaldehyde
-
-
-
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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
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
-
-
-
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
last step in the biosynthesis of benzoic acid from cinnamic acid, a precursor of xanthones
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
additional information
-
BZDH shows the presence of 5.1 mol of magnesium per mole of the enzyme; external addition of Cu2+, Fe3+, Ca2+, Mg2+, Mn2+, and Zn2+ up to 2.5 mM in the assay mixture do not affect activity; external addition of Cu2+, Fe3+, Ca2+, Mg2+, Mn2+, or Zn2+ (up to 2.5 mM) does not affect the enzymatic activity; metal chelators at 10 mM like EDTA and EGTA do not affect activity
K+
-
or NH4+ or Rb+ required for maximal activity, maximum activity occurs at approx. 70 mM K+
K+
-
only dehydrogenase I of strain N.C.I.B. 8250 is activated by univalent cations; or NH4+ or Rb+ required for maximal activity, maximum activity occurs at approx. 70 mM K+
K+
-
or NH4+ or Rb+ required for maximal activity, maximum activity occurs at approx. 70 mM K+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
; inhibits BZDH by 60%, probably by chelation of tightly bound Mg2+ ions
2,2'-dipyridyl
-
40% residual activity at 1 mM; inhibits BZDH by 60%, probably by chelation of tightly bound Mg2+ ions
2-Bromobenzaldehyde
-
0.1 mM, 90% inhibition, benzaldehyde dehydrogenase II
2-Chlorobenzaldehyde
-
0.1 mM, 100% inhibition, benzaldehydedehydrogenase II
2-Fluorobenzaldehyde
-
0.1 mM, 100% inhibition, benzaldehydedehydrogenase II
4-Isopropylbenzaldehyde
-
0.01 mM, 87% inhibition, benzaldehyde dehydrogenase II
pentafluorobenzaldehyde
-
0.1 mM, 44% inhibition, benzaldehyde dehydrogenase II
additional information
-
metal chelators (10 mM) like EDTA and EGTA do not affect the activity
-
3-methylbenzaldehyde
-
0.1 mM, 75% inhibition, benzaldehyde dehydrogenase II
4-chloromercuribenzoate
-
0.005 mM, 50% inhibition after 270 min, benzaldehyde dehydrogenase II
4-chloromercuribenzoate
-
0.10 mM, 50% inhibition after less than 1 min, benzaldehyde dehydrogenase I
benzaldehyde
-
substrate inhibition at concentrations below 0.005 mM, benzaldehyde dehydrogenase I
benzaldehyde
-
inhibition at concentrations above 0.01 mM, benzaldehyde dehydrogenase II
benzaldehyde
-
substrate inhibition; substrate inhibition at higher concentration of benzaldehyde
iodoacetamide
-
1 mM, 50% inhibition after 210 min, benzaldehyde dehydrogenase II
iodoacetamide
-
10 mM, 50% inhibition after less than 1 min, benzaldehyde dehydrogenase I
iodoacetate
-
10 mM, 50% inhibition after 30 min, benzaldehyde dehydrogenase II
iodoacetate
-
10 mM, 50% inhibition after 11 min, benzaldehyde dehydrogenase I
N-ethylmaleimide
-
1 mM, 50% inhibition after 160 min, benzaldehyde dehydrogenase II
N-ethylmaleimide
-
10 mM, 50% inhibition after less than 1 min, benzaldehyde dehydrogenase I
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0038
2-naphthaldehyde
-
apparent Km-value, pH 9.6, temperature not specified in the publication; in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
0.003
4-Chlorobenzaldehyde
-
apparent Km-value, pH 9.6, temperature not specified in the publication; in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
0.497
2-Hydroxybenzaldehyde
-
apparent Km-value, pH 9.6, temperature not specified in the publication; in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
0.377
2-Methylbenzaldehyde
-
apparent Km-value, pH 9.6, temperature not specified in the publication; in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
0.0028
3-Chlorobenzaldehyde
-
apparent Km-value, pH 9.6, temperature not specified in the publication; in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
0.0028
3-Hydroxybenzaldehyde
-
apparent Km-value, pH 9.6, temperature not specified in the publication; in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
0.129
3-Methoxybenzaldehyde
-
apparent Km-value, pH 9.6, temperature not specified in the publication; in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
0.0018
3-methylbenzaldehyde
-
apparent Km-value, pH 9.6, temperature not specified in the publication; in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
0.0035
4-methoxybenzaldehyde
-
apparent Km-value, pH 9.6, temperature not specified in the publication; in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
0.02
4-methylbenzaldehyde
-
apparent Km-value, pH 9.6, temperature not specified in the publication; in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
0.0014
benzaldehyde
-
apparent Km-value, pH 9.6, temperature not specified in the publication; in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
0.115
NAD+
-
apparent Km-value at substrate saturation, pH 9.6, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
39
2-Methylbenzaldehyde
-
apparent Kcat-value, pH 9.6, temperature not specified in the publication; in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
56
2-naphthaldehyde
-
apparent Kcat-value, pH 9.6, temperature not specified in the publication; in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
16
3-Chlorobenzaldehyde
-
apparent Kcat-value, pH 9.6, temperature not specified in the publication; in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
23
3-methylbenzaldehyde
-
apparent Kcat-value, pH 9.6, temperature not specified in the publication; in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
67
4-Chlorobenzaldehyde
-
apparent Kcat-value, pH 9.6, temperature not specified in the publication; in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
120
4-methylbenzaldehyde
-
apparent Kcat-value, pH 9.6, temperature not specified in the publication; in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
33
2-Hydroxybenzaldehyde
-
apparent Kcat-value, pH 9.6, temperature not specified in the publication; in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
24
3-Hydroxybenzaldehyde
-
apparent Kcat-value, pH 9.6, temperature not specified in the publication; in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
885
3-Methoxybenzaldehyde
-
apparent Kcat-value, pH 9.6, temperature not specified in the publication; in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
101
4-methoxybenzaldehyde
-
apparent Kcat-value, pH 9.6, temperature not specified in the publication; in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
14
benzaldehyde
-
apparent Kcat-value, pH 9.6, temperature not specified in the publication; in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
60
2-Hydroxybenzaldehyde
-
apparent Kcat/Km-value, pH 9.6, temperature not specified in the publication; in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
110
2-Methylbenzaldehyde
-
apparent Kcat/Km-value, pH 9.6, temperature not specified in the publication; in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
14700
2-naphthaldehyde
-
apparent Kcat/Km-value, pH 9.6, temperature not specified in the publication; in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
5700
3-Chlorobenzaldehyde
-
apparent Kcat/Km-value, pH 9.6, temperature not specified in the publication; in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
9000
3-Hydroxybenzaldehyde
-
apparent Kcat/Km-value, pH 9.6, temperature not specified in the publication; in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
6800
3-Methoxybenzaldehyde
-
apparent Kcat/Km-value, pH 9.6, temperature not specified in the publication; in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
13000
3-methylbenzaldehyde
-
apparent Kcat/Km-value, pH 9.6, temperature not specified in the publication; in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
22000
4-Chlorobenzaldehyde
-
apparent Kcat/Km-value, pH 9.6, temperature not specified in the publication; in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
29000
4-methoxybenzaldehyde
-
apparent Kcat/Km-value, pH 9.6, temperature not specified in the publication; in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
6000
4-methylbenzaldehyde
-
apparent Kcat/Km-value, pH 9.6, temperature not specified in the publication; in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
10000
benzaldehyde
-
apparent Kcat/Km-value, pH 9.6, temperature not specified in the publication; in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.808
2-Hydroxybenzaldehyde
-
apparent Ki-value, pH 9.6, temperature not specified in the publication
0.521
2-Methylbenzaldehyde
-
apparent Ki-value, pH 9.6, temperature not specified in the publication
0.008
2-naphthaldehyde
-
apparent Ki-value, pH 9.6, temperature not specified in the publication
0.068
3-Chlorobenzaldehyde
-
apparent Ki-value, pH 9.6, temperature not specified in the publication
0.131
3-Hydroxybenzaldehyde
-
apparent Ki-value, pH 9.6, temperature not specified in the publication
0.0013
3-Methoxybenzaldehyde
-
apparent Ki-value, pH 9.6, temperature not specified in the publication
0.051
3-methylbenzaldehyde
-
apparent Ki-value, pH 9.6, temperature not specified in the publication
0.013
4-Chlorobenzaldehyde
-
apparent Ki-value, pH 9.6, temperature not specified in the publication
0.035
4-methoxybenzaldehyde
-
apparent Ki-value, pH 9.6, temperature not specified in the publication
0.003
4-methylbenzaldehyde
-
apparent Ki-value, pH 9.6, temperature not specified in the publication
0.006
benzaldehyde
-
apparent Ki-value, pH 9.6, temperature not specified in the publication; in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.002
-
benzaldehyde dehydrogenase II and class 1 mutant activity in cell extracts of wild-type grown without inducer
0.0022
-
maximum activity in 5-day-old cell cultures 17 h after treatment with chitosan, 25 mg/l
0.005
0.006
-
class 1 mutant enzyme activity in cell extracts of wild-type grown in the presence of 5 mM benzyl alcohol or 1 mM benzaldehyde
0.094
-
class 2 mutant enzyme activity in cell extracts of wild-type grown in the presence of 1 mM benzaldehyde
0.126
-
benzaldehyde dehydrogenase II activity in cell extracts of wild-type grown in the presence of 1 mM benzaldehyde
0.32
-
cell free extract, in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
0.324
-
benzaldehyde dehydrogenase II activity in cell extracts of wild-type grown in the presence of 5 mM benzyl alcohol
0.325
-
class 2 mutant enzyme activity in cell extracts of wild-type grown in the presence of 5 mM benzyl alcohol
64
-
after 200fold purification, in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
additional information
-
substrate 3-hydroxybenzaldehyde, relative activity 11%, benzaldehyde 100%; substrate acetaldehyde, relative activity 309%, benzaldehyde 100%; substrate formaldehyde, relative activity 22%, benzaldehyde 100%; substrate hexanal, relative activity 50%, benzaldehyde 100%; substrate m-anisaldehyde, relative activity 25%, benzaldehyde 100%; substrate p-anisaldehyde, relative activity 31%, benzaldehyde 100%; substrate phenylacetaldehyde, relative activity 62%, benzaldehyde 100%; substrate propionaldehyde, relative activity 165%, benzaldehyde 100%; substrate salicylaldehyde, relative activity 9%, benzaldehyde 100%; substrate trans-cinnamaldehyde, relative activity 47%, benzaldehyde 100%
0.005
-
enzyme activity in extracts of cells grown on either D-phenylglycine, L-phenylglycine, or succinate
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
benzaldehyde dehydrogenase I is induced by phenylglyoxal, benzaldehyde dehydrogenase II by benzaldehyde or benzyl alcohol
-
-
brenda
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
5-days-old, without or after treatment with methyl jasmonate for 6 h
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
-
the wide substrate specificity of the enzyme enables the strain to detoxify methylnaphthalenes to naphthoic acids efficiently
metabolism
-
the wide substrate specificity of the enzyme enables the strain to detoxify methylnaphthalenes to naphthoic acids efficiently
-
Show AA Sequence and Transmembrane Helices (332 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
51654
-
4 * 51654, dehydrogenase II, deduced from nucleotide sequence, electrospray MS
117000
-
gel filtration; native molecular mass of BZDH, determined by Sephacryl S-300-HR gel filtration chromatography
141000 - 219000
-
dehydrogenase I, gel filtration with different gels
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
tetramer
tetramer
-
4 * 55000, dehydrogenase II, SDS-PAGE; 4 * 56000, dehydrogenase I, SDS-PAGE
tetramer
-
4 * 51654, dehydrogenase II, deduced from nucleotide sequence, electrospray MS
tetramer
-
4 * 51941, deduced from nucleotide sequence; 4 * 52500, SDS-PAGE
tetramer
-
4 * 51941, deduced from nucleotide sequence; 4 * 52500, SDS-PAGE
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
37
-
half-lives: benzaldehyde dehydrogenase I, 520 min, benzaldehyde dehydrogenase II, 30 min, pH 9.18, half-life for benzaldehyde dehydrogenase II increases to 113 min at pH 8.5
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dithiothreitol stabilizes
the enzyme loses its activity irreversibly when dialyzed against 50 mM potassium phosphate, pH 6.5, 5% (v/v) glycerol, 2 mM dithiothreitol without benzyl alcohol for 5 h. Enzyme activity is unaffected by varying the concentration of benzyl alcohol
-
the presence of magnesium may be essential for the stability of the enzyme
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 100 mM potassium phosphate, pH 7.5, 2 mM dithiothreitol, 1 mM EDTA, 1 mM benzamidine, 1.2 mM phenylmethanesulfonylfluoride, 40% glycerol, 3 months, 10% loss of activity
-
purified enzyme preparations are found to be stable and stored either at 4 or -20°C, stable up to 6 months at -20°C
-
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, phenyl Sepharose column chromatography, DEAE Sephacel column chromatography, Blue agarose column chromatography, Q Sepharose column chromatography, and Sephacryl S-300-HR gel filtration; to apparent homogeneity by ammonium sulfate precipitation and DEAE Sephacel chromatography and resolved by Blue agarose matrix, where BZDH binds to the matrix, BZDH further purified by Sephacryl S-300-HR gel filtration chromatography
-
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
into the vector pET-28a+ for expression in Escherichia coli BL21 Rosetta cells, into the pEF1-LIS binary vector for transformation of petunia flowers with Agrobacterium tumefaciens, for subcellular localization experiments in Arabidopsis protoplasts GFP fusion proteins are constructed using the vector p326-SGFP
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
degradation
-
in cells of Acinetobacter sp. AG1 isolated from the River Elbe a combined action of benzylalcohol and benzaldehyde dehydrogenase induced after growth with benzylbenzoate does produce benzoate from benzylalcohol, which is a mechanism to quantitatively eliminate the anthropogenic marker compound benzylbenzoate under aerobic conditions
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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
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
Acinetobacter calcoaceticus, Pseudomonas putida
-
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
Abril, M.A.; Michan, C.; Timmis, K.N.; Ramos, J.L.
Regulator and enzyme specificities of the TOL plasmid-encoded upper pathway for degradation of aromatic hydrocarbons and expansion of the substrate range of the pathway [published erratum appears in J Bacteriol 1990 Jun;172(6):3534]
J. Bacteriol.
171
6782-6790
1989
Pseudomonas putida
brenda
MacKintosh, R.W.; Fewson, C.A.
Benzyl alcohol dehydrogenase and benzaldehyde dehydrogenase II from Acinetobacter calcoaceticus. Purification and preliminary characterization
Biochem. J.
250
743-751
1988
Acinetobacter calcoaceticus
brenda
MacKintosh, R.W.; Fewson, C.A.
Benzyl alcohol dehydrogenase and benzaldehyde dehydrogenase II from Acinetobacter calcoaceticus. Substrate specificities and inhibition studies
Biochem. J.
255
653-661
1988
Acinetobacter calcoaceticus
brenda
Inoue, J.; Shaw, J.P.; Rekik, M.; Harayama, S.
Overlapping substrate specificities of benzaldehyde dehydrogenase (the xylC gene product) and 2-hydroxymuconic semialdehyde dehydrogenase (the xylG gene product) encoded by TOL plasmid pWW0 of Pseudomonas putida
J. Bacteriol.
177
1196-1201
1995
Pseudomonas putida
brenda
Chalmers, R.M.; Fewson, C.A.
Purification and characterization of benzaldehyde dehydrogenase I from Acinetobacter calcoaceticus [published erratum appears in Biochem J 1990 Feb 1;265(6):931]
Biochem. J.
263
913-919
1989
Acinetobacter calcoaceticus
brenda
Chalmers, R.M.; Fewson, C.A.
Quantitative immunoblotting in the study of bacterial evolution
Biochem. Soc. Trans.
16
153-154
1988
Acinetobacter calcoaceticus
-
brenda
Van den Tweel, W.J.J.; de Bont, J.A.M.
Physical and functional mapping of two cointegrate plasmids derived from RP4 and TOL plasmid pDK1
J. Gen. Microbiol.
133
745-754
1987
Flavobacterium sp.
-
brenda
MacKintosh, R.W.; Fewson, C.A.
Benzyl alcohol dehydrogenase and benzaldehyde dehydrogenase II from Acinetobacter calcoaceticus
Biochem. Soc. Trans.
15
1048-1049
1987
Acinetobacter calcoaceticus
-
brenda
Livingstone, A.; Fewson, C.A.; Kennedy, S.I.T.; Zatman, L.J.
Two benzaldehyde dehydrogenases in bacterium N.C.I.B. 8250. Distinguishing properties and regulation
Biochem. J.
130
927-935
1972
Acinetobacter calcoaceticus, Acinetobacter calcoaceticus N.C.I.B. 8250
brenda
Fewson, C.A.; Kennedy, S.I.T.
Regulation of enzymes of the mandelate pathway in Bacterium NCIB 8250
Biochem. J.
106
31P
1968
Acinetobacter calcoaceticus
-
brenda
Gillooly, D.J.; Robertson, A.G.S.; Fewson, C.A.
Molecular characterization of benzyl alcohol dehydrogenase and benzaldehyde dehydrogenase II of Acinetobacter calcoaceticus
Biochem. J.
330
1375-1381
1998
Acinetobacter calcoaceticus
brenda
Kim, S.J.; Hwang, S.; Kim, Y.C.
DNA sequence of the phnN gene for benzaldehyde dehydrogenase from Pseudomonas sp. DJ77 and its substrate preference
J. Microbiol.
37
224-228
1999
Pseudomonas sp., Pseudomonas sp. DJ77
-
brenda
Abd El-Mawla, A.M.A.; Beerhues, L.
Benzoic acid biosynthesis in cell cultures of Hypericum androsaemum
Planta
214
727-733
2002
Hypericum androsaemum
brenda
van Sint Fiet, S.; van Beilen, J.B.; Witholt, B.
Selection of biocatalysts for chemical synthesis
Proc. Natl. Acad. Sci. USA
103
1693-1698
2006
Pseudomonas putida
brenda
Goettsching, A.; Schmidt, S.
Productive degradation of the biocide benzylbenzoate by Acinetobacter sp. strain AG1 isolated from the River Elbe
Res. Microbiol.
158
251-257
2007
Acinetobacter sp. AG1
brenda
Gaid, M.M.; Sircar, D.; Beuerle, T.; Mitra, A.; Beerhues, L.
Benzaldehyde dehydrogenase from chitosan-treated Sorbus aucuparia cell cultures
J. Plant Physiol.
166
1343-1349
2009
Sorbus aucuparia
brenda
Long, M.C.; Nagegowda, D.A.; Kaminaga, Y.; Ho, K.K.; Kish, C.M.; Schnepp, J.; Sherman, D.; Weiner, H.; Rhodes, D.; Dudareva, N.
Involvement of snapdragon benzaldehyde dehydrogenase in benzoic acid biosynthesis
Plant J.
59
256-265
2009
Antirrhinum majus
brenda
Shrivastava, R.; Basu, A.; Phale, P.S.
Purification and characterization of benzyl alcohol- and benzaldehyde-dehydrogenase from Pseudomonas putida CSV86
Arch. Microbiol.
193
553-563
2011
Pseudomonas putida, Pseudomonas putida CSV86
brenda
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