EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
1.3.3.16 | a [protein]-(1S,4R)-2-(C-substituted-aminomethyl)-4-acyl-2-thiazoline + O2 |
- |
Escherichia coli |
a [protein]-(S)-2-(C-substituted-aminomethyl)-4-acyl-1,3-thiazole + H2O2 |
- |
? |
1.3.3.16 | a [protein]-(S,S)-2-(C-substituted-aminomethyl)-4-acyl-2-oxazoline + O2 |
- |
Escherichia coli |
a [protein]-(S)-2-(C-substituted-aminomethyl)-4-acyl-1,3-oxazole + H2O2 |
- |
? |
1.3.3.16 | a [protein]-(S,S)-2-(C-substituted-aminomethyl)-4-acyl-5-methyl-2-oxazoline + O2 |
- |
Escherichia coli |
a [protein]-(S)-2-(C-substituted-aminomethyl)-4-acyl-5-methyl-1,3-oxazole + H2O2 |
- |
? |
1.3.3.16 | more |
enzyme oxidizes the 2-thiazoline in patellamide precursor peptides |
Prochloron didemni |
? |
- |
- |
1.3.3.16 | more |
proposed general mechanism for McbC: an activated Tyr202 abstracts a proton from the A carbon of an azoline substrate, which results in E2 elimination of the antiproton from the B carbon and hydride transfer to FMN. Instead of a proton being provided to FMN by a general base to yield FMNH2, the negative charge on N1 of FMN may be stabilized by a salt bridge with Arg233 |
Escherichia coli |
? |
- |
- |