EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
2.7.1.136 | ATP + tylosin |
60% activity with respect to oleandomycin for strain CU1, 4% activity with respect to oleandomycin for strain BM 2506 |
Escherichia coli |
ADP + tylosin 2'-phosphate |
- |
? |
2.7.1.136 | ATP + tylosin |
- |
Streptomyces coelicolor UC 5240 |
ADP + tylosin 2'-phosphate |
- |
? |
2.7.1.136 | ATP + tylosin |
- |
uncultured bacterium |
ADP + tylosin 2'-O-phosphate |
- |
? |
2.7.1.136 | ATP + tylosin |
15-membered ring macrolide |
Escherichia coli |
ADP + tylosin 2'-O-phosphate |
- |
? |
2.7.1.136 | ATP + tylosin |
recombinant expression of the pRSB111 plasmid in Pseudomonas sp. strain B13 |
uncultured bacterium |
ADP + tylosin 2'-O-phosphate |
- |
? |
2.7.1.136 | more |
substrate specificities of wild-type and mutant enzymes, structure-function considerations |
Escherichia coli |
? |
- |
? |
2.7.1.136 | more |
under physiological conditions, enzyme exclusively uses ATP, no substrate: GTP |
Escherichia coli |
? |
- |
? |
2.7.1.136 | more |
structure-based substrate specificity, macrolide binding analysis, overview. Although erythromycin, clarithromycin, oleandomycin, and azithromycin differ in the size of the lactone ring and varying substitutions, the 14- and 15-membered ring substrates bind to the two MPH enzymes in a similar location, adopt similar conformations, and interact with the enzymes in a similar manner. MPH(2')-I cannot modify 16-membered macrolides, in contrast to MPH(2')-II |
Escherichia coli |
? |
- |
- |
2.7.1.136 | more |
structure-based substrate specificity, macrolide binding analysis, overview. Although erythromycin, clarithromycin, oleandomycin, and azithromycin differ in the size of the lactone ring and varying substitutions, the 14- and 15-membered ring substrates bind to the two MPH enzymes in a similar location, adopt similar conformations, and interact with the enzymes in a similar manner. Unlike MPH(2')-I, MPH(2')-II can efficiently modify 16-membered macrolides. The 16-membered rings are more ovoid in shape compared with the rounded shape of the 14- and 15-membered macrolides. The interactions between MPH(2')-II and the 16-membered macrolides, spiramycin and josamycin, are similar to those of the 14- and 15-membered macrolides, involving many of the same amino acid side chains |
Escherichia coli |
? |
- |
- |
2.7.1.136 | more |
substrate specificities of wild-type and mutant enzymes, structure-function considerations |
Escherichia coli CU1 |
? |
- |
? |