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: 22.214.171.124
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
The reaction is physiologically favored in the direction shown.
In Pathways: 2-aminophenol degradation
|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
©2014 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493