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

BRENDA support

Literature summary extracted from

  • Champreda, V.; Choi, Y.J.; Zhou, N.Y.; Leak, D.J.
    Alteration of the stereo- and regioselectivity of alkene monooxygenase based on coupling protein interactions (2006), Appl. Microbiol. Biotechnol., 71, 840-847.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.14.13.69 AamD the enzyme requires interaction with the small catalytic coupling/effector protein, substitution of AamD with IsoD, the coupling protein from the closely related isoprene monooxygenase, changes the regioselectivity of toluene hydroxylation and stereoselectivity of styrene epoxidation, although this is accompanied by a high level of uncoupling Xanthobacter autotrophicus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.13.69 Iron the enzyme is a non-heme diiron monooxygenase and contains a Rieske-type ferredoxin Xanthobacter autotrophicus

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.69 Xanthobacter autotrophicus O87082 gene xamoA, oxygenase alpha subunit; gene xamoA
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.14.13.69 additional information
-
-
 Xanthobacter autotrophicus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.69 (R)-styrene oxide + NADH + H+ + O2
-
 Xanthobacter autotrophicus ?
-
 ?
1.14.13.69 (S)-styrene oxide + NADH + H+ + O2
-
 Xanthobacter autotrophicus ?
-
 ?
1.14.13.69 2-cresol + NADH + H+ + O2
-
 Xanthobacter autotrophicus ?
-
 ?
1.14.13.69 3-cresol + NADH + H+ + O2
-
 Xanthobacter autotrophicus ?
-
 ?
1.14.13.69 4-cresol + NADH + H+ + O2
-
 Xanthobacter autotrophicus ?
-
 ?
1.14.13.69 additional information the enzyme catalyses the asymmetric epoxidation of a broad range of alkenes, stereo- and regioselectivity, residues Asn34 and Arg57 are involved, AMO requires a small catalytic coupling/effector protein, AamD, substitution of AamD with IsoD, the coupling protein from the closely related isoprene monooxygenase, changes the regioselectivity of toluene hydroxylation and stereoselectivity of styrene epoxidation, although this is accompanied by a high level of uncoupling, overview Xanthobacter autotrophicus ?
-
 ?
1.14.13.69 toluene + NADH + H+ + O2
-
 Xanthobacter autotrophicus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.14.13.69 More the enzyme contains NADH-oxidoreductase and a Rieske-type ferredoxin components and the binuclear non-haem iron active site, it requires a small catalytic coupling/effector protein, AamD Xanthobacter autotrophicus

Synonyms

EC Number Synonyms Comment Organism
1.14.13.69 More AMOs are members of the non-heme diiron monooxygenase family of enzymes Xanthobacter autotrophicus
1.14.13.69 XAMO
-
 Xanthobacter autotrophicus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.14.13.69 30
-
 assay at Xanthobacter autotrophicus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.13.69 7.2
-
 assay at Xanthobacter autotrophicus

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.69 additional information the enzyme contains a Rieske-type ferredoxin. AMO requires a small catalytic coupling/effector protein, AamD, the coupling protein cannot or very poorly be substituted by coupling proteins of AMOs of other species, e.g. IsoD from Rhodococcus sp. strain AD45, or PmoB from Mycobacterium sp. strain M156, substitution with IsoD changes the regioselectivity of toluene hydroxylation and stereoselectivity of styrene epoxidation, although this is accompanied by a high level of uncoupling, overview Xanthobacter autotrophicus
1.14.13.69 NADH
-
 Xanthobacter autotrophicus