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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Metals Ions
Metals Ions on EC 1.2.1.39 - phenylacetaldehyde dehydrogenase
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Cs+
Achromobacter eurydice
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monovalent cation required. K+ , Rb+ , Na+, Li+, NH4+ and Cs+ activate in this order
K+
Achromobacter eurydice
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monovalent cation required. K+ , Rb+ , Na+, Li+, NH4+ and Cs+ activate in this order
Li+
Achromobacter eurydice
-
monovalent cation required. K+ , Rb+ , Na+, Li+, NH4+ and Cs+ activate in this order
Mg2+
Mn2+
Na+
Achromobacter eurydice
-
monovalent cation required. K+ , Rb+ , Na+, Li+, NH4+ and Cs+ activate in this order
NH4+
Achromobacter eurydice
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monovalent cation required. K+ , Rb+ , Na+, Li+, NH4+ and Cs+ activate in this order
Rb+
Achromobacter eurydice
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monovalent cation required. K+ , Rb+ , Na+, Li+, NH4+ and Cs+ activate in this order
additional information
Mg2+
the enzyme includes both an activating and inhibitory metal binding site in the catalytic mechanism of NPADH. The activating divalent metal binding site may be best described as the direct interaction of the metal ion with the pyrophosphate linkage joining the nicotinamide mononucleotide and adenosine mononucleotide components of the pyridine nucleotide structure. A second mononuclear metal binding site, occupied by Mg2+ is detected in this structure. The Mg2+ in this site assumes a roughly octahedral geometry and is coordinated by the backbone carbonyl oxygens of Val40, Asp109, Glu196, and Val345, as well as a monodentate interaction with a carboxylate oxygen of Asp109. The sixth ligand is a crystallographically resolved water molecule