1.2.1.39: phenylacetaldehyde dehydrogenase

This is an abbreviated version!
For detailed information about phenylacetaldehyde dehydrogenase, go to the full flat file.

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

     1 Oxidoreductases

         1.2 Acting on the aldehyde or oxo group of donors

             1.2.1 With NAD⁺ or NADP⁺ as acceptor

                1.2.1.39 phenylacetaldehyde dehydrogenase

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Results	in table
1086	AA Sequence
1	CAS Registry Number
9	Cloned(Commentary)
31	Cofactor
1	Crystallization (Commentary)
11	General Information
1	General Stability
30	Inhibitors
2	kcat/KM [mM/s]
2	Ki Value [mM]
27	KM Value [mM]
2	Localization
13	Metals/Ions
10	Molecular Weight [Da]
35	Natural Substrates/ Products (Substrates)
49	Organism
13	Pathway
4	PDB ID
5	pH Optimum
1	pH Range
2	pH Stability
9	Purification (Commentary)
3	Reaction
4	Reaction Type
32	Reference
1	Source Tissue
7	Specific Activity [micromol/min/mg]
5	Storage Stability
114	Substrates and Products (Substrate)
12	Subunits
43	Synonyms
1	Systematic Name
3	Temperature Optimum [°C]
2	Temperature Stability [°C]
11	Turnover Number [1/s]

Metals Ions

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Metals Ions on EC 1.2.1.39 - phenylacetaldehyde dehydrogenase

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METALS and IONS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

Ca2+

Brevibacterium sp.

-

1 mM stimulates by 53%

690567

Cs+

Achromobacter eurydice

-

monovalent cation required. K+ , Rb+ , Na+, Li+, NH4+ and Cs+ activate in this order

390292

K+

Achromobacter eurydice

-

monovalent cation required. K+ , Rb+ , Na+, Li+, NH4+ and Cs+ activate in this order

390292

Li+

Achromobacter eurydice

-

monovalent cation required. K+ , Rb+ , Na+, Li+, NH4+ and Cs+ activate in this order

390292

Mg2+

2 entries

Mn2+

2 entries

Na+

Achromobacter eurydice

-

monovalent cation required. K+ , Rb+ , Na+, Li+, NH4+ and Cs+ activate in this order

390292

NH4+

Achromobacter eurydice

-

monovalent cation required. K+ , Rb+ , Na+, Li+, NH4+ and Cs+ activate in this order

390292

Rb+

Achromobacter eurydice

-

monovalent cation required. K+ , Rb+ , Na+, Li+, NH4+ and Cs+ activate in this order

390292

additional information

2 entries

Mg2+

Brevibacterium sp.

-

1 mM stimulates by 42%

690567

Mg2+

Pseudomonas putida

V4GH04

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

741787

Mn2+

Brevibacterium sp.

-

1 mM stimulates by 17%

690567

Mn2+

Pseudomonas putida

V4GH04

inhibits and activates

741787

additional information

Achromobacter eurydice

-

divalent cations (Mg2+, Ca2+) are inactive

390292

additional information

Brevibacterium sp.

-

is not stimulated by 10 mM KCl

690567