Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Nitrosomonas europaea | enzyme AMO-Ne in whole cells produces 1- and 2-alcohols from C4-C8n-alkanes, the regioselectivity is dependent on the length of the carbon chain. 2-Alcohols produced from C4-C7n-alkanes are predominantly either the R- or S-enantiomers, while 2-octanol produced from n-octane is racemic. AMO-Ne can discriminate between the prochiral hydrogens at the C-2 position, with the degree of discrimination varying according to the n-alkane, and AMO-Ne shows a distinct ability to discriminate between the orientation of n-butane and n-pentane in the catalytic site, as compared to the particulate methane monooxygenase (pMMO, EC 1.14.18.3) of Methylococcus capsulatus (Bath) and that of Methylosinus trichosporium OB3b | ? | - |
? | |
additional information | Nitrosomonas europaea ATCC 19718 | enzyme AMO-Ne in whole cells produces 1- and 2-alcohols from C4-C8n-alkanes, the regioselectivity is dependent on the length of the carbon chain. 2-Alcohols produced from C4-C7n-alkanes are predominantly either the R- or S-enantiomers, while 2-octanol produced from n-octane is racemic. AMO-Ne can discriminate between the prochiral hydrogens at the C-2 position, with the degree of discrimination varying according to the n-alkane, and AMO-Ne shows a distinct ability to discriminate between the orientation of n-butane and n-pentane in the catalytic site, as compared to the particulate methane monooxygenase (pMMO, EC 1.14.18.3) of Methylococcus capsulatus (Bath) and that of Methylosinus trichosporium OB3b | ? | - |
? | |
NH3 + a reduced acceptor + O2 | Nitrosomonas europaea | - |
NH2OH + an acceptor + H2O | - |
? | |
NH3 + a reduced acceptor + O2 | Nitrosomonas europaea ATCC 19718 | - |
NH2OH + an acceptor + H2O | - |
? |
Organic Solvent | Comment | Organism |
---|---|---|
additional information | alcohol productions in C5-C8 n-alkane oxidtions by enzyme AMO-Ne, overview | Nitrosomonas europaea |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Nitrosomonas europaea | Q04507 AND Q04508 | subunits a and b | - |
Nitrosomonas europaea ATCC 19718 | Q04507 AND Q04508 | subunits a and b | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | enzyme AMO-Ne in whole cells produces 1- and 2-alcohols from C4-C8n-alkanes, the regioselectivity is dependent on the length of the carbon chain. 2-Alcohols produced from C4-C7n-alkanes are predominantly either the R- or S-enantiomers, while 2-octanol produced from n-octane is racemic. AMO-Ne can discriminate between the prochiral hydrogens at the C-2 position, with the degree of discrimination varying according to the n-alkane, and AMO-Ne shows a distinct ability to discriminate between the orientation of n-butane and n-pentane in the catalytic site, as compared to the particulate methane monooxygenase (pMMO, EC 1.14.18.3) of Methylococcus capsulatus (Bath) and that of Methylosinus trichosporium OB3b | Nitrosomonas europaea | ? | - |
? | |
additional information | analysis of selectivity of ammonia monooxygenase from Nitrosomonas europaea (AMO-Ne) for the oxidation of C4-C8n-alkanes to the corresponding alcohol isomers, ability of enzyme AMO-Ne to recognize the n-alkane orientation within the catalytic site, overview | Nitrosomonas europaea | ? | - |
? | |
additional information | enzyme AMO-Ne in whole cells produces 1- and 2-alcohols from C4-C8n-alkanes, the regioselectivity is dependent on the length of the carbon chain. 2-Alcohols produced from C4-C7n-alkanes are predominantly either the R- or S-enantiomers, while 2-octanol produced from n-octane is racemic. AMO-Ne can discriminate between the prochiral hydrogens at the C-2 position, with the degree of discrimination varying according to the n-alkane, and AMO-Ne shows a distinct ability to discriminate between the orientation of n-butane and n-pentane in the catalytic site, as compared to the particulate methane monooxygenase (pMMO, EC 1.14.18.3) of Methylococcus capsulatus (Bath) and that of Methylosinus trichosporium OB3b | Nitrosomonas europaea ATCC 19718 | ? | - |
? | |
additional information | analysis of selectivity of ammonia monooxygenase from Nitrosomonas europaea (AMO-Ne) for the oxidation of C4-C8n-alkanes to the corresponding alcohol isomers, ability of enzyme AMO-Ne to recognize the n-alkane orientation within the catalytic site, overview | Nitrosomonas europaea ATCC 19718 | ? | - |
? | |
NH3 + a reduced acceptor + O2 | - |
Nitrosomonas europaea | NH2OH + an acceptor + H2O | - |
? | |
NH3 + a reduced acceptor + O2 | - |
Nitrosomonas europaea ATCC 19718 | NH2OH + an acceptor + H2O | - |
? | |
NH3 + duroquinol + O2 | - |
Nitrosomonas europaea | NH2OH + duroquinone + H2O | - |
? | |
NH3 + duroquinol + O2 | - |
Nitrosomonas europaea ATCC 19718 | NH2OH + duroquinone + H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
AMO | - |
Nitrosomonas europaea |
AMO-Ne | - |
Nitrosomonas europaea |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Nitrosomonas europaea |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Nitrosomonas europaea |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
duroquinol | artificial | Nitrosomonas europaea |