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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Inhibitors
Inhibitors on EC 1.2.1.39 - phenylacetaldehyde dehydrogenase
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NADH
product inhibition, competitive binding of NAD+. For many aldehyde dehydrogenases, NADH binds competitively with NAD+ and forms a nonproductive dead-end complex during catalysis. In the absence of styrene monooxygenase reductase, which regenerates NAD+ from NADH in the first step of styrene catabolism, NPADH is inhibited by a ternary complex involving NADH, product, and phenylacetaldehyde, substrate
PMSF
inactivates NPADH, presumably by modifying the active site cysteine
Pyridine nucleotides
titrations of NPADH with NADþ and NADH are evaluated to estimate the binding affinities of the oxidized and reduced pyridine nucleotides under equilibrium conditions. Mg2+ is included in these studies
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the enzyme is highly specific for phenylacetaldehyde, has cooperative kinetics toward the substrate, and shows considerable substrate inhibition