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Information on EC 1.2.1.29 - aryl-aldehyde dehydrogenase for references in articles please use BRENDA:EC1.2.1.29
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EC Tree
IUBMB Comments Oxidizes a number of aromatic aldehydes, but not aliphatic aldehydes.
The enzyme appears in viruses and cellular organisms
Synonyms
aryl-aldehyde dehydrogenase, PcALDH, PcALDH1, PcALDH2,
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aryl-aldehyde dehydrogenase
aryl-aldehyde dehydrogenase
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aryl-aldehyde dehydrogenase
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PcALDH
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PcALDH1
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PcALDH2
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an aromatic aldehyde + NAD+ + H2O = an aromatic acid + NADH + H+
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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aryl-aldehyde:NAD+ oxidoreductase
Oxidizes a number of aromatic aldehydes, but not aliphatic aldehydes.
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3,4,5-trimethoxybenzaldehyde + NAD+ + H2O
3,4,5-trimethoxybenzoic acid + NADH + H+
3,4-dihydroxybenzaldehyde + NAD+ + H2O
3,4-dihydroxybenzoic acid + NADH + H+
3,4-dimethoxy-5-hydroxybenzaldehyde + NAD+ + H2O
3,4-dimethoxy-5-hydroxybenzoic acid + NADH + H+
3,4-dimethoxybenzaldehyde + NAD+ + H2O
3,4-dimethoxybenzoic 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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benzaldehyde + NAD+ + H2O
benzoic acid + NADH + H+
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gentisaldehyde + NAD+
gentisic acid + NADH
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vanillin + NAD+
vanillinic acid + NADH + H+
additional information
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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
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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aromatic aldehydes + NAD+ + H2O
corresponding aromatic acids + NADH
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vanillin + NAD+
vanillinic acid + NADH + H+
vanillin + NAD+
vanillinic acid + NADH + H+
A0A0U2ETT9
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r
vanillin + NAD+
vanillinic acid + NADH + H+
A0A0U2ETT9
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r
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additional information
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not inhibited by K+, Na+, NH4+ at 1 mM
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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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5.9
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PcALDH1, estimated from sequence
6.1
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PcALDH2, estimated from sequence
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brenda
white-rot basidiomycete
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brenda
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UniProt
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UniProt
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additional information
enzyme PcALDH contains a signal peptide
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brenda
additional information
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enzyme PcALDH contains a signal peptide
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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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A0A0U2ETT9_PYCCI
501
0
55042
TrEMBL
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53300
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PcALDH1, calculated from sequence
54400
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PcALDH2, calculated from sequence
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PcALDH1 and PcALDH2 recombinant protein purified with a His-tag affinity column
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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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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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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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Raison, J.K.; Henson, G.; Rienits, K.G.
The oxidation of gentisaldehyde by nicotinamide-adenine dinucleotide-specific, aromatic aldehyde dehydrogenase from rabbit liver
Biochim. Biophys. Acta
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285-298
1966
Oryctolagus cuniculus
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Nakamura, T.; Ichinose, H.; Wariishi, H.
Cloning and heterologous expression of two aryl-aldehyde dehydrogenases from the white-rot basidiomycete Phanerochaete chrysosporium
Biochem. Biophys. Res. Commun.
394
470-475
2010
Phanerochaete chrysosporium
brenda
Ong, K.; Liew, S.; Mutalib, S.; Murad, A.; Bakar, F.
Isolation and cloning of an aryl-aldehyde dehydrogenase gene from the white-rot fungus Pycnoporus cinnabarinus strain MUCL 39533
Malay. J. Microbiol.
11
391-397
2015
Trametes cinnabarina (A0A0U2ETT9), Trametes cinnabarina MUCL 39533 (A0A0U2ETT9)
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brenda
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