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Information on EC 1.2.1.28 - benzaldehyde dehydrogenase (NAD+)
for references in articles please use BRENDA:EC1.2.1.28
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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
1.2.1.28 benzaldehyde dehydrogenase (NAD+)
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
showSynonyms
baldh, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
benzaldehyde dehydrogenase
benzaldehyde dehydrogenase (NAD)
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BZDH
mdlD
NAD(P)-dependent benzaldehyde dehydrogenase
PpBADH
additional information
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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
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reduction
oxidation
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reduction
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PATHWAY SOURCE
PATHWAYS
BRENDA
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), D-phenylglycine degradation, 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
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-bromobenzaldehyde + NAD+ + H2O
2-bromobenzoate + NADH
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Substrates: -
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2-fluorobenzaldehyde + NAD+ + H2O
2-fluorobenzoate + NADH + H+
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Substrates: 41% of activity with benzaldehyde
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2-methoxybenzaldehyde + NAD+ + H2O
2-methoxybenzoate + NADH + H+
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Substrates: -
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2-methylbenzaldehyde + NAD+ + H2O
2-methylbenzoate + NADH + 2 H+
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Substrates: -
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2-methylbenzaldehyde + NAD+ + H2O
2-methylbenzoate + NADH + H+
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Substrates: -
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2-naphthaldehyde + NAD+ + H2O
2-naphthoate + NADH + H+
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Substrates: -
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2-naphthaldehyde + NAD+ + H2O
naphthalene-2-carboxylic acid + NADH + 2 H+
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Substrates: -
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3,4-dihydroxybenzaldehyde + NAD+ + H2O
3,4-dihydroxybenzoate + NADH + H+
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Substrates: -
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3-chlorobenzaldehyde + NAD+ + H2O
3-chlorobenzoate + NADH + 2 H+
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Substrates: -
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3-chlorobenzaldehyde + NAD+ + H2O
3-chlorobenzoate + NADH + H+
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Substrates: -
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3-methoxy-4-hydroxybenzaldehyde + NAD+ + H2O
3-methoxy-4-hydroxybenzoate + NADH + H+
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Substrates: -
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3-methoxybenzaldehyde + NAD+ + H2O
3-methoxybenzoate + NADH + H+
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Substrates: -
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3-methylbenzaldehyde + NAD+ + H2O
3-methylbenzoate + NADH + 2 H+
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Substrates: -
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3-methylbenzaldehyde + NAD+ + H2O
3-methylbenzoate + NADH + H+
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Substrates: -
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4-chlorobenzaldehyde + NAD+ + H2O
4-chlorobenzoate + NADH
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Substrates: -
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4-chlorobenzaldehyde + NAD+ + H2O
4-chlorobenzoate + NADH + 2 H+
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Substrates: -
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4-chlorobenzaldehyde + NAD+ + H2O
4-chlorobenzoate + NADH + H+
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Substrates: -
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4-ethylbenzaldehyde + NAD+ + H2O
4-ethylbenzoate + NADH
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Substrates: -
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4-hydroxybenzaldehyde + NAD+ + H2O
4-hydroxybenzoate + NADH + 2 H+
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Substrates: 14.7% realtive activity as compared to benzaldehyde
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4-methoxy-3-hydroxybenzaldehyde + NAD+ + H2O
4-methoxy-3-hydroxybenzoate + NADH + H+
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Substrates: -
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4-methylbenzaldehyde + NAD+ + H2O
4-methylbenzoate + NADH + 2 H+
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Substrates: -
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4-methylbenzaldehyde + NAD+ + H2O
4-methylbenzoate + NADH + H+
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Substrates: -
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acetaldehyde + NAD+ + H2O
acetate + NADH + 2 H+
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Substrates: 25.8% realtive activity as compared to benzaldehyde
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acetaldehyde + NAD+ + H2O
acetate + NADH + H+
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Substrates: -
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benzaldehyde + FAD + H2O
benzoate + FADH2
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Substrates: the preferred cofactor is NAD+ followed by NADP+ (82%), FAD (40%) and FMN (34%)
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benzaldehyde + FMN + H2O
benzoate + FMNH2
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Substrates: the preferred cofactor is NAD+ followed by NADP+ (82%), FAD (40%) and FMN (34%)
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benzaldehyde + NADP+ + H2O
benzoate + NADPH
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Substrates: best substrate
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benzaldehyde + NADP+ + H2O
benzoate + NADPH + 2 H+
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Substrates: the preferred cofactor is NAD+ followed by NADP+ (82%), FAD (40%) and FMN (34%)
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cinnamaldehyde + NAD+ + H2O
cinnamate + NADH + H+
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Substrates: benzaldehyde dehydrogenase II
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formaldehyde + NAD+ + H2O
formate + NADH + H+
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Substrates: -
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furan-2-carboxyaldehyde + NAD+ + H2O
furan-2-formiate + NADH
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Substrates: benzaldehyde dehydrogenase II
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m-anisaldehyde + NAD+ + H2O
m-anisate + NADH + H+
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Substrates: -
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phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
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Substrates: -
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propionaldehyde + NAD+ + H2O
propionate + NADH + 2 H+
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Substrates: 10% realtive activity as compared to benzaldehyde
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propionaldehyde + NAD+ + H2O
propionate + NADH + H+
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Substrates: -
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pyridin-3-carboxyaldehyde + NAD+ + H2O
pyridin-3-formiate + NADH
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Substrates: benzaldehyde dehydrogenase II
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salicylaldehyde + NAD+ + H2O
salicylate + NADH + H+
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Substrates: -
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thiophen-2-carboxaldehyde + NAD+ + H2O
thiophen-2-formiate + NADH
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Substrates: -
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thiophen-2-carboxyaldehyde + NAD+ + H2O
thiophen-2-formiate + NADH
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Substrates: benzaldehyde dehydrogenase II
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trans-cinnamaldehyde + NAD+ + H2O
trans-cinnamate + NADH + H+
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Substrates: -
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2-chlorobenzaldehyde + NAD+ + H2O
2-chlorobenzoate + NADH + H+
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Substrates: low activity
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2-chlorobenzaldehyde + NAD+ + H2O
2-chlorobenzoate + NADH + H+
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Substrates: low activity
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2-hydroxybenzaldehyde + NAD+ + H2O
2-hydroxybenzoate + NADH + 2 H+
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Substrates: -
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2-hydroxybenzaldehyde + NAD+ + H2O
2-hydroxybenzoate + NADH + 2 H+
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Substrates: -
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2-hydroxybenzaldehyde + NAD+ + H2O
2-hydroxybenzoate + NADH + 2 H+
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Substrates: 2% realtive activity as compared to benzaldehyde
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2-hydroxybenzaldehyde + NAD+ + H2O
2-hydroxybenzoate + NADH + H+
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Substrates: benzaldehyde dehydrogenase II
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2-hydroxybenzaldehyde + NAD+ + H2O
2-hydroxybenzoate + NADH + H+
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Substrates: 39% of activity with benzaldehyde
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2-hydroxybenzaldehyde + NAD+ + H2O
2-hydroxybenzoate + NADH + H+
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Substrates: 16% of activity with benzaldehyde
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2-hydroxybenzaldehyde + NAD+ + H2O
2-hydroxybenzoate + NADH + H+
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Substrates: 16% of the activity with benzaldehyde
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2-hydroxybenzaldehyde + NAD+ + H2O
2-hydroxybenzoate + NADH + H+
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Substrates: -
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2-hydroxybenzaldehyde + NAD+ + H2O
2-hydroxybenzoate + NADH + H+
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Substrates: -
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2-hydroxybenzaldehyde + NAD+ + H2O
2-hydroxybenzoate + NADH + H+
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Substrates: -
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2-methylbenzaldehyde + NAD+ + H2O
2-methylbenzoate + NADH
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Substrates: 13% of activity with benzaldehyde
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2-methylbenzaldehyde + NAD+ + H2O
2-methylbenzoate + NADH
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Substrates: -
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2-methylbenzaldehyde + NAD+ + H2O
2-methylbenzoate + NADH
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Substrates: -
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2-methylbenzaldehyde + NAD+ + H2O
2-methylbenzoate + NADH
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Substrates: low activity
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3-chlorobenzaldehyde + NAD+ + H2O
3-chlorobenzoate + NADH
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Substrates: -
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3-chlorobenzaldehyde + NAD+ + H2O
3-chlorobenzoate + NADH
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Substrates: -
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3-chlorobenzaldehyde + NAD+ + H2O
3-chlorobenzoate + NADH
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Substrates: low activity
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3-chlorobenzaldehyde + NAD+ + H2O
3-chlorobenzoate + NADH
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Substrates: low activity
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3-fluorobenzaldehyde + NAD+ + H2O
3-fluorobenzoate + NADH + H+
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Substrates: benzaldehyde dehydrogenase II
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3-fluorobenzaldehyde + NAD+ + H2O
3-fluorobenzoate + NADH + H+
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Substrates: 98% of activity with benzaldehyde
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3-fluorobenzaldehyde + NAD+ + H2O
3-fluorobenzoate + NADH + H+
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Substrates: -
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3-hydroxybenzaldehyde + NAD+ + H2O
3-hydroxybenzoate + NADH + 2 H+
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Substrates: -
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3-hydroxybenzaldehyde + NAD+ + H2O
3-hydroxybenzoate + NADH + 2 H+
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Substrates: 1.5% realtive activity as compared to benzaldehyde
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3-hydroxybenzaldehyde + NAD+ + H2O
3-hydroxybenzoate + NADH + H+
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Substrates: benzaldehyde dehydrogenase II
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3-hydroxybenzaldehyde + NAD+ + H2O
3-hydroxybenzoate + NADH + H+
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Substrates: 222% of activity with benzaldehyde
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3-hydroxybenzaldehyde + NAD+ + H2O
3-hydroxybenzoate + NADH + H+
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Substrates: -
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3-hydroxybenzaldehyde + NAD+ + H2O
3-hydroxybenzoate + NADH + H+
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Substrates: 38% of activity with benzaldehyde
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3-hydroxybenzaldehyde + NAD+ + H2O
3-hydroxybenzoate + NADH + H+
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Substrates: 38% of the activity with benzaldehyde
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3-hydroxybenzaldehyde + NAD+ + H2O
3-hydroxybenzoate + NADH + H+
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Substrates: -
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3-methoxybenzaldehyde + NAD+ + H2O
3-methoxybenzoate + NADH
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Substrates: 235% of activity with benzaldehyde
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3-methoxybenzaldehyde + NAD+ + H2O
3-methoxybenzoate + NADH
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Substrates: benzaldehyde dehydrogenase II
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3-methoxybenzaldehyde + NAD+ + H2O
3-methoxybenzoate + NADH
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Substrates: -
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3-methoxybenzaldehyde + NAD+ + H2O
3-methoxybenzoate + NADH + 2 H+
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Substrates: -
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3-methoxybenzaldehyde + NAD+ + H2O
3-methoxybenzoate + NADH + 2 H+
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Substrates: -
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3-methylbenzaldehyde + NAD+ + H2O
3-methylbenzoate + NADH
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Substrates: 119% of activity with benzaldehyde
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3-methylbenzaldehyde + NAD+ + H2O
3-methylbenzoate + NADH
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Substrates: -
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3-methylbenzaldehyde + NAD+ + H2O
3-methylbenzoate + NADH
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Substrates: -
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3-methylbenzaldehyde + NAD+ + H2O
3-methylbenzoate + NADH
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Substrates: -
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3-methylbenzaldehyde + NAD+ + H2O
3-methylbenzoate + NADH
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Substrates: -
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3-nitrobenzaldehyde + NAD+ + H2O
3-nitrobenzoate + NADH
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Substrates: -
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3-nitrobenzaldehyde + NAD+ + H2O
3-nitrobenzoate + NADH
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Substrates: -
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4-carboxybenzaldehyde + NAD+ + H2O
4-carboxybenzoate + NADH
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Substrates: 1650% of activity with benzaldehyde
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4-carboxybenzaldehyde + NAD+ + H2O
4-carboxybenzoate + NADH
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Substrates: 1650% of activity with benzaldehyde
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4-chlorobenzaldehyde + H2O + NADP+
4-chlorobenzoate + NADPH + 2 H+
Substrates: -
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4-chlorobenzaldehyde + H2O + NADP+
4-chlorobenzoate + NADPH + 2 H+
Substrates: -
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4-fluorobenzaldehyde + NAD+ + H2O
4-fluorobenzoate + NADH + H+
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Substrates: benzaldehyde dehydrogenase II
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4-fluorobenzaldehyde + NAD+ + H2O
4-fluorobenzoate + NADH + H+
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Substrates: 210% of activity with benzaldehyde
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4-hydroxybenzaldehyde + NAD+ + H2O
4-hydroxybenzoate + NADH + H+
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Substrates: -
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4-hydroxybenzaldehyde + NAD+ + H2O
4-hydroxybenzoate + NADH + H+
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Substrates: benzaldehyde dehydrogenase II
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4-hydroxybenzaldehyde + NAD+ + H2O
4-hydroxybenzoate + NADH + H+
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Substrates: 24% of activity with benzaldehyde
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4-hydroxybenzaldehyde + NAD+ + H2O
4-hydroxybenzoate + NADH + H+
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Substrates: 24% of the activity with benzaldehyde
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4-methoxybenzaldehyde + H2O + NADP+
4-methoxybenzoate + NADPH + 2 H+
Substrates: -
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4-methoxybenzaldehyde + H2O + NADP+
4-methoxybenzoate + NADPH + 2 H+
Substrates: -
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4-methoxybenzaldehyde + NAD+ + H2O
4-methoxybenzoate + NADH + 2 H+
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Substrates: -
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4-methoxybenzaldehyde + NAD+ + H2O
4-methoxybenzoate + NADH + 2 H+
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Substrates: -
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4-methoxybenzaldehyde + NAD+ + H2O
4-methoxybenzoate + NADH + H+
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Substrates: benzaldehyde dehydrogenase II
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4-methoxybenzaldehyde + NAD+ + H2O
4-methoxybenzoate + NADH + H+
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Substrates: -
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4-methoxybenzaldehyde + NAD+ + H2O
4-methoxybenzoate + NADH + H+
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Substrates: 90% of activity with benzaldehyde
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4-methoxybenzaldehyde + NAD+ + H2O
4-methoxybenzoate + NADH + H+
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Substrates: -
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4-methoxybenzaldehyde + NAD+ + H2O
4-methoxybenzoate + NADH + H+
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Substrates: 90% of activity with benzaldehyde
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4-methylbenzaldehyde + NAD+ + H2O
4-methylbenzoate + NADH
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Substrates: 240% of activity with benzaldehyde
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4-methylbenzaldehyde + NAD+ + H2O
4-methylbenzoate + NADH
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Substrates: -
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4-methylbenzaldehyde + NAD+ + H2O
4-methylbenzoate + NADH
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Substrates: -
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4-nitrobenzaldehyde + H2O + NADP+
4-nitrobenzoate + NADPH + 2 H+
Substrates: -
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4-nitrobenzaldehyde + H2O + NADP+
4-nitrobenzoate + NADPH + 2 H+
Substrates: -
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benzaldehyde + H2O + NAD+
benzoate + NADH + 2 H+
Substrates: -
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benzaldehyde + H2O + NAD+
benzoate + NADH + 2 H+
Substrates: -
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benzaldehyde + H2O + NAD+
benzoate + NADH + 2 H+
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Substrates: -
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benzaldehyde + H2O + NAD+
benzoate + NADH + 2 H+
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Substrates: -
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benzaldehyde + NAD+ + H2O
benzoate + NADH + 2 H+
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Substrates: -
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benzaldehyde + NAD+ + H2O
benzoate + NADH + 2 H+
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Substrates: -
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benzaldehyde + NAD+ + H2O
benzoate + NADH + 2 H+
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Substrates: the enzyme is involved in biphenyl phytoalexin biosynthesis. Pyrus pyrifolia cell cultures respond to yeast extract treatment by accumulating benzoate-derived biphenyl phytoalexins, namely, noraucuparin and aucuparin
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benzaldehyde + NAD+ + H2O
benzoate + NADH + 2 H+
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Substrates: the preferred cofactor is NAD+ followed by NADP+ (82%), FAD (40%) and FMN (34%)
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benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
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Substrates: -
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benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
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Substrates: -
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benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
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Substrates: benzaldehyde dehydrogenase II exhibits esterase activity with 4-nitrophenyl acetate
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benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
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Substrates: benzaldehyde dehydrogenase I exhibits esterase activity, approx. 2% of dehydrogenase activity
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benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
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Substrates: also active with NADP+, see also EC 1.2.1.7
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benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
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Substrates: -
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benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
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Substrates: -
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benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
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Substrates: -
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benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
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Substrates: -
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benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
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Substrates: -
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benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
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Substrates: -
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benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
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Substrates: -
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benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
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Substrates: last step in the biosynthesis of benzoic acid from cinnamic acid, a precursor of xanthones
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benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
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Substrates: best substrate
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benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
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Substrates: -
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benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
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Substrates: -
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benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
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Substrates: -
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benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
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Substrates: also active with NADP+, see also EC 1.2.1.7
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benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
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Substrates: -
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benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
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Substrates: -
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benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
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Substrates: -
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benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
Substrates: -
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benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
Substrates: -
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benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
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Substrates: -
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benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
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Substrates: also active with NADP+, see also EC 1.2.1.7
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ir
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
hexan-1-al + NAD+ + H2O
hexanoate + NADH
-
Substrates: -
Products: -
Products: -
?
hexan-1-al + NAD+ + H2O
hexanoate + NADH
-
Substrates: benzaldehyde dehydrogenase II
Products: -
Products: -
?
octan-1-al + NAD+ + H2O
octanoate + NADH
-
Substrates: -
Products: -
Products: -
?
octan-1-al + NAD+ + H2O
octanoate + NADH
-
Substrates: benzaldehyde dehydrogenase II
Products: -
Products: -
?
perillaldehyde + NAD+ + H2O
perillic acid + NADH
-
Substrates: -
Products: -
Products: -
?
perillaldehyde + NAD+ + H2O
perillic acid + NADH
-
Substrates: benzaldehyde dehydrogenase II
Products: -
Products: -
?
pyridine 4-carboxyaldehyde + NAD+ + H2O
pyridine 4-formiate + NADH
-
Substrates: benzaldehyde dehydrogenase II
Products: -
Products: -
?
pyridine 4-carboxyaldehyde + NAD+ + H2O
pyridine 4-formiate + NADH
-
Substrates: 1380% of activity with benzaldehyde
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme fails to show activity with NADP+ or NADPH and is inactive with 2-methoxybenzaldehyde, 4-hydroxybenzaldehyde, 2-chlorobenzaldehyde, and 1-naphthaldehyde
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: -
?
additional information
?
-
-
Substrates: metabolite identification by gas chromatography mass spectrometry (GC-MS)
Products: -
Products: -
?
additional information
?
-
-
Substrates: metabolite identification by gas chromatography mass spectrometry (GC-MS)
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
benzaldehyde + NAD+ + H2O
benzoate + NADH + 2 H+
-
Substrates: the enzyme is involved in biphenyl phytoalexin biosynthesis. Pyrus pyrifolia cell cultures respond to yeast extract treatment by accumulating benzoate-derived biphenyl phytoalexins, namely, noraucuparin and aucuparin
Products: -
Products: -
?
benzaldehyde + H2O + NAD+
benzoate + NADH + 2 H+
Substrates: -
Products: -
Products: -
?
benzaldehyde + H2O + NAD+
benzoate + NADH + 2 H+
Substrates: -
Products: -
Products: -
?
benzaldehyde + H2O + NAD+
benzoate + NADH + 2 H+
-
Substrates: -
Products: -
Products: -
?
benzaldehyde + H2O + NAD+
benzoate + NADH + 2 H+
-
Substrates: -
Products: -
Products: -
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
Substrates: -
Products: -
Products: -
ir
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
Substrates: last step in the biosynthesis of benzoic acid from cinnamic acid, a precursor of xanthones
Products: -
Products: -
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
Substrates: -
Products: -
Products: -
ir
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
the preferred cofactor is NAD+ followed by NADP+ (82%), FAD (40%) and FMN (34%)
FMN
-
the preferred cofactor is NAD+ followed by NADP+ (82%), FAD (40%) and FMN (34%)
NAD+
-
-
NAD+
-
the preferred cofactor is NAD+ followed by NADP+ (82%), FAD (40%) and FMN (34%)
NADP+
-
the preferred cofactor is NAD+ followed by NADP+ (82%), FAD (40%) and FMN (34%)
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+
Mg2+
additional information
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
K+
-
or NH4+ or Rb+ required for maximal activity, maximum activity occurs at approx. 70 mM K+
additional information
-
external addition of Cu2+, Fe3+, Ca2+, Mg2+, Mn2+, and Zn2+ up to 2.5 mM in the assay mixture do not affect activity
additional information
-
metal chelators at 10 mM like EDTA and EGTA do not affect activity
additional information
-
BZDH shows the presence of 5.1 mol of magnesium per mole of the enzyme
additional information
-
external addition of Cu2+, Fe3+, Ca2+, Mg2+, Mn2+, or Zn2+ (up to 2.5 mM) does not affect the enzymatic activity
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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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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Carcinogenesis
Immunohistochemical detection of tumour-associated aldehyde dehydrogenase in formalin-fixed rat and mouse normal liver and hepatomas.
Carcinoma, Hepatocellular
Immunohistochemical detection of tumour-associated aldehyde dehydrogenase in formalin-fixed rat and mouse normal liver and hepatomas.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0093
4-nitrobenzaldehyde
pH 8.5, 30°C, recombinant wild-type enzyme, with NAD+
0.497
2-Hydroxybenzaldehyde
-
apparent Km-value, pH 9.6, temperature not specified in the publication
0.497
2-Hydroxybenzaldehyde
-
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
0.377
2-Methylbenzaldehyde
-
in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
0.0038
2-naphthaldehyde
-
apparent Km-value, pH 9.6, temperature not specified in the publication
0.0038
2-naphthaldehyde
-
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
0.0028
3-Chlorobenzaldehyde
-
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
0.0028
3-Hydroxybenzaldehyde
-
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
0.129
3-Methoxybenzaldehyde
-
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
0.0018
3-methylbenzaldehyde
-
in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
0.0012
4-Chlorobenzaldehyde
pH 8.5, 30°C, recombinant wild-type enzyme, with NAD+
0.003
4-Chlorobenzaldehyde
-
apparent Km-value, pH 9.6, temperature not specified in the publication
0.003
4-Chlorobenzaldehyde
-
in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
0.002
4-methoxybenzaldehyde
pH 8.5, 30°C, recombinant wild-type enzyme, with NAD+
0.0035
4-methoxybenzaldehyde
-
apparent Km-value, pH 9.6, temperature not specified in the publication
0.0035
4-methoxybenzaldehyde
-
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
0.02
4-methylbenzaldehyde
-
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
0.0014
benzaldehyde
-
in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
0.0044
benzaldehyde
pH 8.5, 30°C, recombinant wild-type enzyme, with NAD+
0.0066
benzaldehyde
pH 8.5, 30°C, recombinant mutant E337D, with NAD+
0.02
benzaldehyde
pH 8.5, 30°C, recombinant mutant E337Q, with NAD+
0.02
benzaldehyde
pH 8.5, 30°C, recombinant mutant E337L, with NAD+
0.028
benzaldehyde
pH 8.5, 30°C, recombinant mutant E215D, with NAD+
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
95
4-nitrobenzaldehyde
pH 8.5, 30°C, recombinant wild-type enzyme, with NAD+
33
2-Hydroxybenzaldehyde
-
apparent Kcat-value, pH 9.6, temperature not specified in the publication
33
2-Hydroxybenzaldehyde
-
in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
39
2-Methylbenzaldehyde
-
apparent Kcat-value, pH 9.6, temperature not specified in the publication
39
2-Methylbenzaldehyde
-
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
56
2-naphthaldehyde
-
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
16
3-Chlorobenzaldehyde
-
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
24
3-Hydroxybenzaldehyde
-
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
885
3-Methoxybenzaldehyde
-
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
23
3-methylbenzaldehyde
-
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
67
4-Chlorobenzaldehyde
-
in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
135
4-Chlorobenzaldehyde
pH 8.5, 30°C, recombinant wild-type enzyme, with NAD+
101
4-methoxybenzaldehyde
-
apparent Kcat-value, pH 9.6, temperature not specified in the publication
101
4-methoxybenzaldehyde
-
in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
116
4-methoxybenzaldehyde
pH 8.5, 30°C, recombinant wild-type enzyme, with NAD+
120
4-methylbenzaldehyde
-
apparent Kcat-value, pH 9.6, temperature not specified in the publication
120
4-methylbenzaldehyde
-
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
14
benzaldehyde
-
in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
156
benzaldehyde
pH 8.5, 30°C, recombinant wild-type enzyme, with NAD+
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
10215
4-nitrobenzaldehyde
pH 8.5, 30°C, recombinant wild-type enzyme, with NAD+
60
2-Hydroxybenzaldehyde
-
apparent Kcat/Km-value, pH 9.6, temperature not specified in the publication
60
2-Hydroxybenzaldehyde
-
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
110
2-Methylbenzaldehyde
-
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
14700
2-naphthaldehyde
-
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
5700
3-Chlorobenzaldehyde
-
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
9000
3-Hydroxybenzaldehyde
-
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
6800
3-Methoxybenzaldehyde
-
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
13000
3-methylbenzaldehyde
-
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
22000
4-Chlorobenzaldehyde
-
in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
112500
4-Chlorobenzaldehyde
pH 8.5, 30°C, recombinant wild-type enzyme, with NAD+
29000
4-methoxybenzaldehyde
-
apparent Kcat/Km-value, pH 9.6, temperature not specified in the publication
29000
4-methoxybenzaldehyde
-
in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
58000
4-methoxybenzaldehyde
pH 8.5, 30°C, recombinant wild-type enzyme, with NAD+
6000
4-methylbenzaldehyde
-
apparent Kcat/Km-value, pH 9.6, temperature not specified in the publication
6000
4-methylbenzaldehyde
-
in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
53.6
benzaldehyde
pH 8.5, 30°C, recombinant mutant E215D, with NAD+
6818.2
benzaldehyde
pH 8.5, 30°C, recombinant mutant E337D, with NAD+
10000
benzaldehyde
-
apparent Kcat/Km-value, pH 9.6, temperature not specified in the publication
10000
benzaldehyde
-
in glycine-KOH buffer (100 mM, pH 9.6), temperature not specified in the publication
35454
benzaldehyde
pH 8.5, 30°C, recombinant wild-type enzyme, with NAD+
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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
0.006
benzaldehyde
-
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
0.005
-
enzyme activity in extracts of cells grown on either D-phenylglycine, L-phenylglycine, or succinate
additional information
-
substrate formaldehyde, relative activity 22%, benzaldehyde 100%
additional information
-
substrate acetaldehyde, relative activity 309%, benzaldehyde 100%
additional information
-
substrate propionaldehyde, relative activity 165%, benzaldehyde 100%
additional information
-
substrate hexanal, relative activity 50%, benzaldehyde 100%
additional information
-
substrate phenylacetaldehyde, relative activity 62%, benzaldehyde 100%
additional information
-
substrate trans-cinnamaldehyde, relative activity 47%, benzaldehyde 100%
additional information
-
substrate salicylaldehyde, relative activity 9%, benzaldehyde 100%
additional information
-
substrate 3-hydroxybenzaldehyde, relative activity 11%, benzaldehyde 100%
additional information
-
substrate m-anisaldehyde, relative activity 25%, benzaldehyde 100%
additional information
-
substrate p-anisaldehyde, relative activity 31%, benzaldehyde 100%
additional information
-
purified recombinant enzyme shows highest activity of 9.4 U/ml
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
9.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
40
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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
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
physiological function
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
-
the wide substrate specificity of the enzyme enables the strain to detoxify methylnaphthalenes to naphthoic acids efficiently
metabolism
-
the enzyme is involved in biphenyl phytoalexin biosynthesis. Pyrus pyrifolia cell cultures respond to yeast extract treatment by accumulating benzoate-derived biphenyl phytoalexins, namely, noraucuparin and aucuparin
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
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metabolism
-
the wide substrate specificity of the enzyme enables the strain to detoxify methylnaphthalenes to naphthoic acids efficiently
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physiological function
-
enzyme BZDH has the ability to degrade benzaldehyde to less toxic compounds. The BZDH is a critical enzyme for the degradation of aromatic hydrocarbons in Rhodococcus sp. The BZDH from Rhodococcus ruber strain UKMP-5M shows similar function with other aldehyde dehydrogenases
physiological function
-
enzyme BZDH has the ability to degrade benzaldehyde to less toxic compounds. The BZDH is a critical enzyme for the degradation of aromatic hydrocarbons in Rhodococcus sp. The BZDH from Rhodococcus ruber strain UKMP-5M shows similar function with other aldehyde dehydrogenases
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additional information
two conserved glutamates, at positions 215 and 337, might 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, might 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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Show AA Sequence and Transmembrane Helices (133 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
117000
141000 - 219000
-
dehydrogenase I, gel filtration with different gels
51654
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4 * 51654, dehydrogenase II, deduced from nucleotide sequence, electrospray MS
117000
-
native molecular mass of BZDH, determined by Sephacryl S-300-HR gel filtration chromatography
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
tetramer
tetramer
-
4 * 51654, dehydrogenase II, deduced from nucleotide sequence, electrospray MS
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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
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
-
E337Q
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
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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
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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
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-20°C, 24 h, significant loss in enzyme activity (70 %) upon storage of cell-free extract
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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
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recombinant enzyme 14fold from Escherichia coli strain BL21(DE3) by anion exchange chromatography
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recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and 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
gene mdlD, recombinant epression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene xylC, recombinant expression in Escherichia coli strain BL21(DE3) in inclusion bodies. Using higher concentration of lysozyme in lysis buffer, high speed, and long-term centrifugation reduces the protein aggregation
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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
Saini, S.S.; Teotia, D.; Gaid, M.; Thakur, A.; Beerhues, L.; Sircar, D.
Benzaldehyde dehydrogenase-driven phytoalexin biosynthesis in elicitor-treated Pyrus pyrifolia cell cultures
J. Plant Physiol.
215
154-162
2017
Pyrus pyrifolia
brenda
Tavakoli, A.; Hamzah, A.
Partial purification and characterization of the recombinant benzaldehyde dehydrogenase from Rhodococcus ruber UKMP-5M
Iran. J. Biotechnol.
15
67-73
2017
Rhodococcus ruber, Rhodococcus ruber UKMP-5M
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 ATCC 12633 (Q84DC3)
brenda
EXTERNAL LINKS (specific for EC-Number 1.2.1.28)
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