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Enzyme Nomenclature
Information on EC 1.2.1.28 - benzaldehyde dehydrogenase (NAD+)
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
1.2.1.28
-
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RECOMMENDED NAME
GeneOntology No.
benzaldehyde dehydrogenase (NAD+)
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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
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
benzaldehyde dehydrogenase I is induced by phenylglyoxal, benzaldehyde dehydrogenase II by benzaldehyde or benzyl alcohol
-
-
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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
-
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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-carboxybenzaldehyde + NAD+ + H2O
4-carboxybenzoate + NADH
-
1650% of activity with benzaldehyde
-
?
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
-
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
-
-
-
?
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 SUBSTRATES
NATURAL PRODUCTS
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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INHIBITORS
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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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
5-days-old, without or after treatment with methyl jasmonate for 6 h
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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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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SUBUNITS
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
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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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LINKS TO OTHER DATABASES (specific for EC-Number 1.2.1.28)
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