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Enzyme Nomenclature
Information on EC 1.2.1.29 - aryl-aldehyde dehydrogenase
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.2.1.29
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RECOMMENDED NAME
GeneOntology No.
aryl-aldehyde dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an aromatic aldehyde + NAD+ + H2O = an aromatic acid + NADH + H+
oxidizes a number of aromatic aldehydes, but not aliphatic aldehydes
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an aromatic aldehyde + NAD+ + H2O = an aromatic acid + NADH + H+
ALDH catalysis involves acylation and deacylation
an aromatic aldehyde + NAD+ + H2O = an aromatic acid + NADH + H+
ALDH catalysis involves acylation and deacylation
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
aryl-aldehyde:NAD+ oxidoreductase
Oxidizes a number of aromatic aldehydes, but not aliphatic aldehydes.
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CAS REGISTRY NUMBER
COMMENTARY
37250-94-5
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
evolution
in silico analysis of PcALDH indicate that enzyme PcALDH belongs to the ALDH superfamily and class 3 ALDHs
evolution
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in silico analysis of PcALDH indicate that enzyme PcALDH belongs to the ALDH superfamily and class 3 ALDHs
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metabolism
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results suggest that PcALDHs metabolize aryl-aldehyde compounds generated during fungal degradation of lignin and various aromatic xenobiotics
metabolism
in filamentous fungi, vanillin is formed in a two-stage process in which ferulic acid is converted to vanillic acid then reduced to vanillin
metabolism
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results suggest that PcALDHs metabolize aryl-aldehyde compounds generated during fungal degradation of lignin and various aromatic xenobiotics
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metabolism
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in filamentous fungi, vanillin is formed in a two-stage process in which ferulic acid is converted to vanillic acid then reduced to vanillin
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physiological function
reduction of vanillic acid to vanillin is catalysed by the key enzyme aryl-aldehyde dehydrogenase
physiological function
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reduction of vanillic acid to vanillin is catalysed by the key enzyme aryl-aldehyde dehydrogenase
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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
3,4-dimethoxy-5-hydroxybenzaldehyde + NAD+ + H2O
3,4-dimethoxy-5-hydroxybenzoic acid + NADH + H+
4-hydroxy-3,5-dimethoxybenzaldehyde + NAD+ + H2O
4-hydroxy-3,5-dimethoxybenzoic acid + NADH + H+
4-hydroxy-3-methoxybenzaldehyde + NAD+ + H2O
4-hydroxy-3-methoxybenzoic acid + NADH + H+
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4-hydroxy-3-methoxybenzaldehyde i.e. vanillin
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?
4-hydroxybenzaldehyde + NAD+ + H2O
4-hydroxybenzoic acid + NADH + H+
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?
aromatic aldehydes + NAD+ + H2O
corresponding aromatic acids + NADH
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3,4,5-trimethoxybenzaldehyde + NAD+ + H2O
3,4,5-trimethoxybenzoic acid + NADH + H+
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?
3,4,5-trimethoxybenzaldehyde + NAD+ + H2O
3,4,5-trimethoxybenzoic acid + NADH + H+
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?
3,4-dihydroxybenzaldehyde + NAD+ + H2O
3,4-dihydroxybenzoic acid + NADH + H+
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?
3,4-dihydroxybenzaldehyde + NAD+ + H2O
3,4-dihydroxybenzoic acid + NADH + H+
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?
3,4-dimethoxy-5-hydroxybenzaldehyde + NAD+ + H2O
3,4-dimethoxy-5-hydroxybenzoic acid + NADH + H+
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?
3,4-dimethoxy-5-hydroxybenzaldehyde + NAD+ + H2O
3,4-dimethoxy-5-hydroxybenzoic acid + NADH + H+
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?
3,4-dimethoxybenzaldehyde + NAD+ + H2O
3,4-dimethoxybenzoic acid + NADH + H+
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?
3,4-dimethoxybenzaldehyde + NAD+ + H2O
3,4-dimethoxybenzoic acid + NADH + H+
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?
4-hydroxy-3,5-dimethoxybenzaldehyde + NAD+ + H2O
4-hydroxy-3,5-dimethoxybenzoic acid + NADH + H+
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?
4-hydroxy-3,5-dimethoxybenzaldehyde + NAD+ + H2O
4-hydroxy-3,5-dimethoxybenzoic acid + NADH + H+
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?
vanillin + NAD+
vanillinic acid + NADH + H+
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r
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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additional information
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ALDH catalysis involves acylation and deacylation. During acylation, a cysteine nucleophile interacts with the carbonyl carbon of aldehyde forming a thiohemiacetal intermediate, followed by hydride transfer from a tetrahedral thiohemiacetal intermediate to the pyridine ring of NAD(P)+. Then, deacylation occurs involving hydrolysis of the resulting thioester intermediate. Glu268 and Cys296 of PcALDH are potential active site residues
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additional information
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ALDH catalysis involves acylation and deacylation. During acylation, a cysteine nucleophile interacts with the carbonyl carbon of aldehyde forming a thiohemiacetal intermediate, followed by hydride transfer from a tetrahedral thiohemiacetal intermediate to the pyridine ring of NAD(P)+. Then, deacylation occurs involving hydrolysis of the resulting thioester intermediate. Glu268 and Cys296 of PcALDH are potential active site residues
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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
aromatic aldehydes + NAD+ + H2O
corresponding aromatic acids + NADH
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vanillin + NAD+
vanillinic acid + NADH + H+
A0A0U2ETT9
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r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
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
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
additional information
enzyme PcALDH contains a signal peptide
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additional information
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enzyme PcALDH contains a signal peptide
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
gene PcALDH, cloning from RNA via RT-PCR, sequence comparisons and phylogenetic analysis, DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli strain JM109
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
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
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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
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
the enzyme can be used for production of bio-vanillin from vanillic acid
synthesis
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the enzyme can be used for production of bio-vanillin from vanillic acid
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LINKS TO OTHER DATABASES (specific for EC-Number 1.2.1.29)
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