Information on EC 1.2.1.29 - aryl-aldehyde dehydrogenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.2.1.29
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RECOMMENDED NAME
GeneOntology No.
aryl-aldehyde dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
an aromatic aldehyde + NAD+ + H2O = an aromatic acid + NADH + H+
show the reaction diagram
oxidizes a number of aromatic aldehydes, but not aliphatic aldehydes
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
4-nitrotoluene degradation I
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Metabolic pathways
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Microbial metabolism in diverse environments
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p-cymene degradation to p-cumate
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Tyrosine metabolism
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Xylene degradation
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SYSTEMATIC NAME
IUBMB Comments
aryl-aldehyde:NAD+ oxidoreductase
Oxidizes a number of aromatic aldehydes, but not aliphatic aldehydes.
CAS REGISTRY NUMBER
COMMENTARY hide
37250-94-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
white-rot basidiomycete
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3,4,5-trimethoxybenzaldehyde + NAD+ + H2O
3,4,5-trimethoxybenzoic acid + NADH + H+
show the reaction diagram
3,4-dihydroxybenzaldehyde + NAD+ + H2O
3,4-dihydroxybenzoic acid + NADH + H+
show the reaction diagram
3,4-dimethoxy-5-hydroxybenzaldehyde + NAD+ + H2O
3,4-dimethoxy-5-hydroxybenzoic acid + NADH + H+
show the reaction diagram
3,4-dimethoxybenzaldehyde + NAD+ + H2O
3,4-dimethoxybenzoic acid + NADH + H+
show the reaction diagram
4-hydroxy-3,5-dimethoxybenzaldehyde + NAD+ + H2O
4-hydroxy-3,5-dimethoxybenzoic acid + NADH + H+
show the reaction diagram
4-hydroxy-3-methoxybenzaldehyde + NAD+ + H2O
4-hydroxy-3-methoxybenzoic acid + NADH + H+
show the reaction diagram
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4-hydroxy-3-methoxybenzaldehyde i.e. vanillin
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?
4-hydroxybenzaldehyde + NAD+ + H2O
4-hydroxybenzoic acid + NADH + H+
show the reaction diagram
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?
aromatic aldehydes + NAD+ + H2O
corresponding aromatic acids + NADH
show the reaction diagram
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benzaldehyde + NAD+ + H2O
benzoic acid + NADH + H+
show the reaction diagram
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?
gentisaldehyde + NAD+
gentisic acid + NADH
show the reaction diagram
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additional information
?
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the enzyme is capable of catalysing the oxidation of a number of aromatic aldehydes, but not aliphatic aldehydes
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
aromatic aldehydes + NAD+ + H2O
corresponding aromatic acids + NADH
show the reaction diagram
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
propionaldehyde
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additional information
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not inhibited by K+, Na+, NH4+ at 1 mM
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 11
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enzymatic reactions carried out at pH 4.0 show only 5–10% of the maximum activities observed at pH 10.0
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.9
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PcALDH1, estimated from sequence
6.1
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PcALDH2, estimated from sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
53300
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PcALDH1, calculated from sequence
54400
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PcALDH2, calculated from sequence
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
PcALDH1 and PcALDH2 recombinant protein purified with a His-tag affinity column
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
PcALDH1 and PcALDH2 expressed as C-terminal histidine-tagged proteins in Escherichia coli cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
up-regulation of PcALDH1 and PcALDH2 in response to exogenous addition of vanillin, which is an abundant key intermediate in the lignin biodegradation process, basidiomycetes presumably respond to vanillin by activating and optimizing ligninolytic processes