Species: Pseudomonas sp. AP3
2-aminophenol 1,6-dioxygenase has been purified to homogeneity from Pseudomonas sp. AP3 [Takenaka97]. The enzyme is a homotetramer, composed of two types of subunits, and contains 1 mole of Fe2+ per mole tetramer. Substrate range was rather narrow, although the enzyme did accept several alternative substrates, such as 2-amino-5-methylphenol, with much lower activity.
Molecular Weight: 140.0 kD (experimental) [Takenaka97]
Enzymatic reaction of: 2-aminophenol 1,6-dioxygenase
EC Number: 188.8.131.522-aminophenol + oxygen → 2-aminomuconate 6-semialdehyde + H+
The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.
The reaction is physiologically favored in the direction shown.Alternative Substrates for 2-aminophenol: 2-amino-5-methylphenol [Takenaka97]
In Pathways: 2-aminophenol degradationMn2+ [Takenaka97], Cu2+ [Takenaka97], Fe3+ [Takenaka97], Ag+ [Takenaka97], Hg2+ [Takenaka97]Kinetic Parameters:
|Gene:||amnA||Accession Number: G-11248 (MetaCyc)|
Molecular Weight: 29.416 kD (from nucleotide sequence)
Molecular Weight: 32.0 kD (experimental) [Takenaka97]
|Gene:||amnB||Accession Number: G-11249 (MetaCyc)|
Molecular Weight: 34.441 kD (from nucleotide sequence)
Molecular Weight: 40.0 kD (experimental) [Takenaka97]
Takenaka97: Takenaka S, Murakami S, Shinke R, Hatakeyama K, Yukawa H, Aoki K (1997). "Novel genes encoding 2-aminophenol 1,6-dioxygenase from Pseudomonas species AP-3 growing on 2-aminophenol and catalytic properties of the purified enzyme." J Biol Chem 272(23);14727-32. PMID: 9169437
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