1.2.1.39: phenylacetaldehyde dehydrogenase
This is an abbreviated version!
For detailed information about phenylacetaldehyde dehydrogenase, go to the full flat file.
Word Map on EC 1.2.1.39
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1.2.1.39
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phenylacetic
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monooxygenase
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phenylpyruvate
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2-phenylethylamine
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nad+-dependent
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2-phenylethanol
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denitrifying
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aromaticum
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agrochemical
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tungstate
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aromatoleum
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tyrosol
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4-hydroxyphenylacetaldehyde
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tungsten-dependent
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dinucleotide-dependent
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betaproteobacterium
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phenylacetyl-coa
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phenylethanols
- 1.2.1.39
-
phenylacetic
- monooxygenase
- phenylpyruvate
- 2-phenylethylamine
-
nad+-dependent
- 2-phenylethanol
-
denitrifying
- aromaticum
-
agrochemical
- tungstate
-
aromatoleum
- tyrosol
- 4-hydroxyphenylacetaldehyde
-
tungsten-dependent
-
dinucleotide-dependent
-
betaproteobacterium
- phenylacetyl-coa
- phenylethanols
Reaction
Synonyms
dehydrogenase, phenylacetaldehyde, ebA4954, feaB, NAD(P)+-dependent phenylacetaldehyde dehydrogenase, NPADH, PAAL dehydrogenase, PAD, PadA, PADH, PDH, PeaE, PeaE protein, phenylacetaldehyde dehydrogenase, styD
ECTree
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Specific Activity
Specific Activity on EC 1.2.1.39 - phenylacetaldehyde dehydrogenase
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0.102
purified native enzyme, with cofactor NADP+, pH 8.5, 28°C
additional information
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Analysis of phenylacetaldehyde dehydrogenase activity in cell-free extracts reveals that although enzymatic activity decreases in the peaE knocked-out mutant (20% with respect to the control), good phenylacetaldehyde dehydrogenase activity is present. Another aldehyde dehydrogenase(s) exist(s) that could replace the role played by PeaE
additional information
Analysis of phenylacetaldehyde dehydrogenase activity in cell-free extracts reveals that although enzymatic activity decreases in the peaE knocked-out mutant (20% with respect to the control), good phenylacetaldehyde dehydrogenase activity is present. Another aldehyde dehydrogenase(s) exist(s) that could replace the role played by PeaE