Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Shaw, J.; Harayama, S.
    Purification and characterisation of the NADH acceptor reductase component of xylene monooxygenase encoded by the TOL plasmid pWWO of Pseudomonas putida mt-2 (1992), Eur. J. Biochem., 209, 51-61 .
    View publication on PubMed

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.18.1.3 42000
-
gel filtration Pseudomonas putida

Organism

EC Number Organism UniProt Comment Textmining
1.14.15.26 Pseudomonas putida
-
-
-
1.18.1.3 Pseudomonas putida P21394 enzyme acts as reductase component of xylene monooxygenase, EC 1.18.1.3
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.18.1.3 electron-transfer component XylA Pseudomonas putida

Subunits

EC Number Subunits Comment Organism
1.18.1.3 ? x * 40000, SDS-PAGE Pseudomonas putida

Synonyms

EC Number Synonyms Comment Organism
1.14.15.26 xylM
-
Pseudomonas putida
1.18.1.3 XYLA
-
Pseudomonas putida

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.15.26 additional information electron-transfer component XylA, EC 1.18.1.3 contains 1 mol FAD per mol of enzyme. The electron flow is from NADH to FAD to[2Fe-2S] Pseudomonas putida
1.18.1.3 FAD 1 mol/mol enzyme. The electron flow is from NADH to FAD to [2Fe-2S] Pseudomonas putida
1.18.1.3 NADH electron-transfer component XylA. The electron flow is from NADH to FAD to [2Fe-2S] Pseudomonas putida
1.18.1.3 [2Fe-2S]-center protein contains 2 mol/mol of non-haem iron and 2 mol/mol of acid-labile sulfide. The electron flow is from NADH to FAD to [2Fe-2S] Pseudomonas putida