BRENDA - Enzyme Database
show all sequences of 1.2.1.29

Isolation and cloning of an aryl-aldehyde dehydrogenase gene from the white-rot fungus Pycnoporus cinnabarinus strain MUCL 39533

Ong, K.; Liew, S.; Mutalib, S.; Murad, A.; Bakar, F.; Malay. J. Microbiol. 11, 391-397 (2015)
No PubMed abstract available

Data extracted from this reference:

Application
Application
Commentary
Organism
synthesis
the enzyme can be used for production of bio-vanillin from vanillic acid
Trametes cinnabarina
Cloned(Commentary)
Commentary
Organism
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
Trametes cinnabarina
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
additional information
enzyme PcALDH contains a signal peptide
Trametes cinnabarina
-
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
vanillin + NAD+
Trametes cinnabarina
-
vanillinic acid + NADH + H+
-
-
r
vanillin + NAD+
Trametes cinnabarina MUCL 39533
-
vanillinic acid + NADH + H+
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Trametes cinnabarina
A0A0U2ETT9
-
-
Trametes cinnabarina MUCL 39533
A0A0U2ETT9
-
-
Reaction
Reaction
Commentary
Organism
an aromatic aldehyde + NAD+ + H2O = an aromatic acid + NADH + H+
ALDH catalysis involves acylation and deacylation
Trametes cinnabarina
Source Tissue
Source Tissue
Commentary
Organism
Textmining
mycelium
-
Trametes cinnabarina
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
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
743201
Trametes cinnabarina
?
-
-
-
-
additional information
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
743201
Trametes cinnabarina MUCL 39533
?
-
-
-
-
vanillin + NAD+
-
743201
Trametes cinnabarina
vanillinic acid + NADH + H+
-
-
-
r
vanillin + NAD+
-
743201
Trametes cinnabarina MUCL 39533
vanillinic acid + NADH + H+
-
-
-
r
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
-
Trametes cinnabarina
NADH
-
Trametes cinnabarina
Application (protein specific)
Application
Commentary
Organism
synthesis
the enzyme can be used for production of bio-vanillin from vanillic acid
Trametes cinnabarina
Cloned(Commentary) (protein specific)
Commentary
Organism
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
Trametes cinnabarina
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Trametes cinnabarina
NADH
-
Trametes cinnabarina
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
additional information
enzyme PcALDH contains a signal peptide
Trametes cinnabarina
-
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
vanillin + NAD+
Trametes cinnabarina
-
vanillinic acid + NADH + H+
-
-
r
vanillin + NAD+
Trametes cinnabarina MUCL 39533
-
vanillinic acid + NADH + H+
-
-
r
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
mycelium
-
Trametes cinnabarina
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
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
743201
Trametes cinnabarina
?
-
-
-
-
additional information
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
743201
Trametes cinnabarina MUCL 39533
?
-
-
-
-
vanillin + NAD+
-
743201
Trametes cinnabarina
vanillinic acid + NADH + H+
-
-
-
r
vanillin + NAD+
-
743201
Trametes cinnabarina MUCL 39533
vanillinic acid + NADH + H+
-
-
-
r
General Information
General Information
Commentary
Organism
evolution
in silico analysis of PcALDH indicate that enzyme PcALDH belongs to the ALDH superfamily and class 3 ALDHs
Trametes cinnabarina
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
Trametes cinnabarina
physiological function
reduction of vanillic acid to vanillin is catalysed by the key enzyme aryl-aldehyde dehydrogenase
Trametes cinnabarina
General Information (protein specific)
General Information
Commentary
Organism
evolution
in silico analysis of PcALDH indicate that enzyme PcALDH belongs to the ALDH superfamily and class 3 ALDHs
Trametes cinnabarina
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
Trametes cinnabarina
physiological function
reduction of vanillic acid to vanillin is catalysed by the key enzyme aryl-aldehyde dehydrogenase
Trametes cinnabarina
Other publictions for EC 1.2.1.29
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
743201
Ong
-
Isolation and cloning of an a ...
Trametes cinnabarina, Trametes cinnabarina MUCL 39533
Malay. J. Microbiol.
11
391-397
2015
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4
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3
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711095
Nakamura
Cloning and heterologous expre ...
Phanerochaete chrysosporium
Biochem. Biophys. Res. Commun.
394
470-475
2010
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13
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288178
Raison
The oxidation of gentisaldehyd ...
Oryctolagus cuniculus
Biochim. Biophys. Acta
118
285-298
1966
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