Activating Compound | Comment | Organism | Structure |
---|---|---|---|
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 | Comment | Organism | Structure |
---|---|---|---|
Iron | the enzyme is a non-heme diiron monooxygenase and contains a Rieske-type ferredoxin | Xanthobacter autotrophicus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Xanthobacter autotrophicus | O87082 | gene xamoA, oxygenase alpha subunit; gene xamoA | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
- |
Xanthobacter autotrophicus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(R)-styrene oxide + NADH + H+ + O2 | - |
Xanthobacter autotrophicus | ? | - |
? | |
(S)-styrene oxide + NADH + H+ + O2 | - |
Xanthobacter autotrophicus | ? | - |
? | |
2-cresol + NADH + H+ + O2 | - |
Xanthobacter autotrophicus | ? | - |
? | |
3-cresol + NADH + H+ + O2 | - |
Xanthobacter autotrophicus | ? | - |
? | |
4-cresol + NADH + H+ + O2 | - |
Xanthobacter autotrophicus | ? | - |
? | |
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 | ? | - |
? | |
toluene + NADH + H+ + O2 | - |
Xanthobacter autotrophicus | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
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 | Comment | Organism |
---|---|---|
More | AMOs are members of the non-heme diiron monooxygenase family of enzymes | Xanthobacter autotrophicus |
XAMO | - |
Xanthobacter autotrophicus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Xanthobacter autotrophicus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.2 | - |
assay at | Xanthobacter autotrophicus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
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 | |
NADH | - |
Xanthobacter autotrophicus |