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
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phenylacetic
- monooxygenase
- phenylpyruvate
- 2-phenylethylamine
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nad+-dependent
- 2-phenylethanol
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denitrifying
- aromaticum
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agrochemical
- tungstate
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aromatoleum
- tyrosol
- 4-hydroxyphenylacetaldehyde
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tungsten-dependent
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dinucleotide-dependent
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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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General Information
General Information on EC 1.2.1.39 - phenylacetaldehyde dehydrogenase
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malfunction
metabolism
physiological function
additional information
deletion of feaB gene results in increased desired aromatic compounds with decreased by-products. 2-Phenylethanol is not degraded by a feaB-deficient strain
malfunction
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disruption of the endogenous phenylacetaldehyde dehydrogenase gene shuts off 4-hydroxyphenylacetate production and improves the production of tyrosol as a sole product
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FeaB plays a major role in the formation of 4-hydroxyphenylacetate
metabolism
the enzyme catalyzes a step in the styrene catabolic pathway of Pseudomonas putida
metabolism
two distinct enzymes are involved in the oxidation of phenylacetaldehyde to phenylacetate, an aldehyde:ferredoxin oxidoreductase (AOR) and a phenylacetaldehyde dehydrogenase (PDH). PDH is the primary enzyme during anaerobic phenylalanine degradation, whereas AOR is not essential for the metabolic pathway and exhibits probably a function as a detoxifying enzyme if high aldehyde concentrations accumulate in the cytoplasm, which would lead to substrate inhibition of PDH
metabolism
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the enzyme catalyzes a step in the styrene catabolic pathway of Pseudomonas putida
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metabolism
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two distinct enzymes are involved in the oxidation of phenylacetaldehyde to phenylacetate, an aldehyde:ferredoxin oxidoreductase (AOR) and a phenylacetaldehyde dehydrogenase (PDH). PDH is the primary enzyme during anaerobic phenylalanine degradation, whereas AOR is not essential for the metabolic pathway and exhibits probably a function as a detoxifying enzyme if high aldehyde concentrations accumulate in the cytoplasm, which would lead to substrate inhibition of PDH
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phenylacetaldehyde dehydrogenase catalyzes the NAD+-dependent oxidation of phenylactealdehyde to phenylacetic acid in the styrene catabolic and detoxification pathway of Pseudomonas putida strain S12
physiological function
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phenylacetaldehyde dehydrogenase catalyzes the NAD+-dependent oxidation of phenylactealdehyde to phenylacetic acid in the styrene catabolic and detoxification pathway of Pseudomonas putida strain S12
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substrate channel and active site structure, overview. A majority of conserved residues in NPADH localize to the active site and NAD+-binding pocket. At the interface between the two pockets are the catalytic Cys 301 and Glu 267 residues, which serve as the general nucleophile and general base for the reaction, respectively
additional information
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substrate channel and active site structure, overview. A majority of conserved residues in NPADH localize to the active site and NAD+-binding pocket. At the interface between the two pockets are the catalytic Cys 301 and Glu 267 residues, which serve as the general nucleophile and general base for the reaction, respectively
additional information
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substrate channel and active site structure, overview. A majority of conserved residues in NPADH localize to the active site and NAD+-binding pocket. At the interface between the two pockets are the catalytic Cys 301 and Glu 267 residues, which serve as the general nucleophile and general base for the reaction, respectively
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