EC Number | Cloned (Comment) | Organism |
---|---|---|
1.4.3.26 | expression in Escherichia coli | Mycobacterium ulcerans |
1.4.3.26 | expression in Escherichia coli | Mycolicibacterium smegmatis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.4.3.26 | 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2 | Mycobacterium ulcerans | - |
5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O2 | - |
? | |
1.4.3.26 | 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2 | Mycolicibacterium smegmatis | - |
5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O2 | - |
? | |
1.4.3.26 | 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2 | Mycobacterium ulcerans Agy99 | - |
5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O2 | - |
? | |
1.4.3.26 | 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2 | Mycolicibacterium smegmatis ATCC 700084 | - |
5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O2 | - |
? | |
1.4.3.26 | 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2 + H2O | Mycobacterium ulcerans | - |
5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3 + H2O2 | - |
? | |
1.4.3.26 | 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2 + H2O | Mycolicibacterium smegmatis | - |
5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3 + H2O2 | - |
? | |
1.4.3.26 | 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2 + H2O | Mycobacterium ulcerans Agy99 | - |
5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3 + H2O2 | - |
? | |
1.4.3.26 | 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2 + H2O | Mycolicibacterium smegmatis ATCC 700084 | - |
5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3 + H2O2 | - |
? | |
1.4.3.26 | 5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O | Mycobacterium ulcerans | - |
5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3 | - |
? | |
1.4.3.26 | 5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O | Mycolicibacterium smegmatis | - |
5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3 | - |
? | |
1.4.3.26 | 5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O | Mycobacterium ulcerans Agy99 | - |
5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3 | - |
? | |
1.4.3.26 | 5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O | Mycolicibacterium smegmatis ATCC 700084 | - |
5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3 | - |
? | |
1.4.3.26 | additional information | Mycobacterium ulcerans | MftD catalyzes the oxidative deamination of 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethyl-2-pyrrolidinone, forming an 2-oxo moiety on the resulting premycofactocin molecule. The enzyme uses oxygen as an electron source to oxidize a C-N bond, followed by spontaneous exchange with water to form an 2-oxo moiety | ? | - |
- |
|
1.4.3.26 | additional information | Mycolicibacterium smegmatis | MftD catalyzes the oxidative deamination of 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethyl-2-pyrrolidinone, forming an 2-oxo moiety on the resulting premycofactocin molecule. The enzyme uses oxygen as an electron source to oxidize a C-N bond, followed by spontaneous exchange with water to form an 2-oxo moiety | ? | - |
- |
|
1.4.3.26 | additional information | Mycobacterium ulcerans Agy99 | MftD catalyzes the oxidative deamination of 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethyl-2-pyrrolidinone, forming an 2-oxo moiety on the resulting premycofactocin molecule. The enzyme uses oxygen as an electron source to oxidize a C-N bond, followed by spontaneous exchange with water to form an 2-oxo moiety | ? | - |
- |
|
1.4.3.26 | additional information | Mycolicibacterium smegmatis ATCC 700084 | MftD catalyzes the oxidative deamination of 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethyl-2-pyrrolidinone, forming an 2-oxo moiety on the resulting premycofactocin molecule. The enzyme uses oxygen as an electron source to oxidize a C-N bond, followed by spontaneous exchange with water to form an 2-oxo moiety | ? | - |
- |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.4.3.26 | Mycobacterium ulcerans | A0PM50 | - |
- |
1.4.3.26 | Mycobacterium ulcerans Agy99 | A0PM50 | - |
- |
1.4.3.26 | Mycolicibacterium smegmatis | A0QSB9 | - |
- |
1.4.3.26 | Mycolicibacterium smegmatis ATCC 700084 | A0QSB9 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.4.3.26 | 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2 | - |
Mycobacterium ulcerans | 5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O2 | - |
? | |
1.4.3.26 | 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2 | - |
Mycolicibacterium smegmatis | 5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O2 | - |
? | |
1.4.3.26 | 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2 | - |
Mycobacterium ulcerans Agy99 | 5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O2 | - |
? | |
1.4.3.26 | 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2 | - |
Mycolicibacterium smegmatis ATCC 700084 | 5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O2 | - |
? | |
1.4.3.26 | 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2 + H2O | - |
Mycobacterium ulcerans | 5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3 + H2O2 | - |
? | |
1.4.3.26 | 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2 + H2O | - |
Mycolicibacterium smegmatis | 5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3 + H2O2 | - |
? | |
1.4.3.26 | 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2 + H2O | - |
Mycobacterium ulcerans Agy99 | 5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3 + H2O2 | - |
? | |
1.4.3.26 | 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + O2 + H2O | - |
Mycolicibacterium smegmatis ATCC 700084 | 5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3 + H2O2 | - |
? | |
1.4.3.26 | 5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O | - |
Mycobacterium ulcerans | 5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3 | - |
? | |
1.4.3.26 | 5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O | - |
Mycolicibacterium smegmatis | 5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3 | - |
? | |
1.4.3.26 | 5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O | - |
Mycobacterium ulcerans Agy99 | 5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3 | - |
? | |
1.4.3.26 | 5-[(4-hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one + H2O | - |
Mycolicibacterium smegmatis ATCC 700084 | 5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidine-2,3-dione + NH3 | - |
? | |
1.4.3.26 | additional information | MftD catalyzes the oxidative deamination of 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethyl-2-pyrrolidinone, forming an 2-oxo moiety on the resulting premycofactocin molecule. The enzyme uses oxygen as an electron source to oxidize a C-N bond, followed by spontaneous exchange with water to form an 2-oxo moiety | Mycobacterium ulcerans | ? | - |
- |
|
1.4.3.26 | additional information | MftD catalyzes the oxidative deamination of 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethyl-2-pyrrolidinone, forming an 2-oxo moiety on the resulting premycofactocin molecule. The enzyme uses oxygen as an electron source to oxidize a C-N bond, followed by spontaneous exchange with water to form an 2-oxo moiety | Mycolicibacterium smegmatis | ? | - |
- |
|
1.4.3.26 | additional information | MftD catalyzes the oxidative deamination of 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethyl-2-pyrrolidinone , forming an 2-oxo moiety on the resulting premycofactocin molecule | Mycolicibacterium smegmatis | ? | - |
- |
|
1.4.3.26 | additional information | MftD catalyzes the oxidative deamination of 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethyl-2-pyrrolidinone, forming an 2-oxo moiety on the resulting premycofactocin molecule | Mycobacterium ulcerans | ? | - |
- |
|
1.4.3.26 | additional information | MftD catalyzes the oxidative deamination of 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethyl-2-pyrrolidinone, forming an 2-oxo moiety on the resulting premycofactocin molecule. The enzyme uses oxygen as an electron source to oxidize a C-N bond, followed by spontaneous exchange with water to form an 2-oxo moiety | Mycobacterium ulcerans Agy99 | ? | - |
- |
|
1.4.3.26 | additional information | MftD catalyzes the oxidative deamination of 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethyl-2-pyrrolidinone, forming an 2-oxo moiety on the resulting premycofactocin molecule | Mycobacterium ulcerans Agy99 | ? | - |
- |
|
1.4.3.26 | additional information | MftD catalyzes the oxidative deamination of 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethyl-2-pyrrolidinone, forming an 2-oxo moiety on the resulting premycofactocin molecule. The enzyme uses oxygen as an electron source to oxidize a C-N bond, followed by spontaneous exchange with water to form an 2-oxo moiety | Mycolicibacterium smegmatis ATCC 700084 | ? | - |
- |
|
1.4.3.26 | additional information | MftD catalyzes the oxidative deamination of 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethyl-2-pyrrolidinone , forming an 2-oxo moiety on the resulting premycofactocin molecule | Mycolicibacterium smegmatis ATCC 700084 | ? | - |
- |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.4.3.26 | IldD1 | - |
Mycobacterium ulcerans |
1.4.3.26 | mftD | - |
Mycobacterium ulcerans |
1.4.3.26 | mftD | - |
Mycolicibacterium smegmatis |
1.4.3.26 | msmeg 1424 | - |
Mycolicibacterium smegmatis |
1.4.3.26 | mul_0774 | - |
Mycobacterium ulcerans |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.4.3.26 | FMN | - |
Mycobacterium ulcerans | |
1.4.3.26 | FMN | - |
Mycolicibacterium smegmatis |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.4.3.26 | physiological function | premycofactocin is a biologically active redox cofactor that oxidizes NADH bound by Mycobycterium smegmatis carveol dehydrogenase and can be used by carveol dehydrogenase in the oxidation of carveol | Mycolicibacterium smegmatis |