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Literature summary for 1.14.99.67 extracted from
- CmlI N-oxygenase catalyzes the final three steps in chloramphenicol biosynthesis without dissociation of intermediates (2017), Biochemistry, 56, 4940-4950 .
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Streptomyces venezuelae | F2RB83 | - |
- |
| Streptomyces venezuelae DSM 40230 | F2RB83 | - |
- |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | diferrous CmlI can react with NH2-chloramphenicol species and O2 in either order to form a peroxo-NH2-chloramphenicol intermediate. Peroxo-NH2-chloramphenicol undergoes rapid oxygen transfer to form a diferric CmlI complex with the aryl-hydroxylamine [NH(OH)-chloramphenicol] pathway intermediate. Diferric CmlI-NH(OH)-chloramphenicol undergoes a rapid internal redox reaction to form a differous CmlI-nitroso-chloramphenicol complex. O2 binding results in formation of peroxo-NO-chloramphenicol that converts to differic CmlI-chloramphenicol by enzyme-mediated oxygen atom transfer. There is little dissociation of pathway intermediates as the reaction progresses | Streptomyces venezuelae |
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Release 2023.1 (January 2023)
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