Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + azithromycin
ADP + azithromycin 2'-O-phosphate
ATP + clarithromycin
ADP + clarithromycin 2'-O-phosphate
ATP + erythromycin
ADP + erythromycin 2'-O-phosphate
ATP + erythromycin
ADP + erythromycin-2'-O-phosphate
ATP + josamycin
ADP + josamycin 2'-O-phosphate
-
15-membered ring macrolide
-
-
?
ATP + kitasamycin
?
-
52% activity with respect to oleandomycin for strain CU1, 61% activity with respect to oleandomycin for strain BM 2506
-
-
?
ATP + kitasamycin
ADP + kitasamycin 2'-O-phosphate
-
15-membered ring macrolide
-
-
?
ATP + neomycin
ADP + ?
-
-
-
?
ATP + oleandomycin
ADP + oleandomycin 2'-O-phosphate
ATP + rokitamycin
ADP + rokitamycin 2'-O-phosphate
-
15-membered ring macrolide
-
-
?
ATP + roxithromycin
ADP + roxithromycin 2'-O-phosphate
ATP + spectinomycin
?
5% activity with respect to oleandomycin
-
-
?
ATP + spiramycin
ADP + spiramycin 2'-O-phosphate
ATP + telithromycin
ADP + telithromycin 2'-O-phosphate
ATP + triacetyloleandomycin
?
-
100% activity with respect to oleandomycin
-
-
?
ATP + triacetyloleandomycin + H2O
ADP + triacetyloleandomycin 2'-O-phosphate + acetate
-
as active as oleandomycin
-
-
?
ATP + troleandomycin
?
-
82% activity with respect to oleandomycin for strain CU1, 105% activity with respect to oleandomycin for strain BM 2506
-
-
?
ATP + troleandomycin + H2O
ADP + troleandomycin 2'-O-phosphate + acetate
-
14-membered ring macrolide
-
-
?
ATP + tylosin
ADP + tylosin 2'-O-phosphate
ATP + tylosin
ADP + tylosin 2'-phosphate
additional information
?
-
ATP + azithromycin
ADP + azithromycin 2'-O-phosphate
-
-
-
?
ATP + azithromycin
ADP + azithromycin 2'-O-phosphate
-
15-membered ring macrolide
-
-
?
ATP + azithromycin
ADP + azithromycin 2'-O-phosphate
the mph(A) gene conferrs resistance to azithromycin
-
-
?
ATP + azithromycin
ADP + azithromycin 2'-O-phosphate
-
15-membered ring macrolide
-
-
?
ATP + azithromycin
ADP + azithromycin 2'-O-phosphate
-
15% of the activity with oleandomycin
-
-
?
ATP + azithromycin
ADP + azithromycin 2'-O-phosphate
the mph(A) gene conferrs resistance to azithromycin
-
-
?
ATP + azithromycin
ADP + azithromycin 2'-O-phosphate
-
-
-
?
ATP + azithromycin
ADP + azithromycin 2'-O-phosphate
the mph(A) gene conferrs resistance to azithromycin
-
-
?
ATP + azithromycin
ADP + azithromycin 2'-O-phosphate
recombinant expression of the pRSB111 plasmid in Pseudomonas sp. strain B13
-
-
?
ATP + clarithromycin
?
-
46-55% activity with respect to oleandomycin for strain CU1, 17% activity with respect to oleandomycin for strain BM 2506
-
-
?
ATP + clarithromycin
?
-
77% activity with respect to oleandomycin
-
-
?
ATP + clarithromycin
ADP + clarithromycin 2'-O-phosphate
-
-
-
?
ATP + clarithromycin
ADP + clarithromycin 2'-O-phosphate
-
14-membered ring macrolide
-
-
?
ATP + clarithromycin
ADP + clarithromycin 2'-O-phosphate
-
14-membered ring macrolide
-
-
?
ATP + clarithromycin
ADP + clarithromycin 2'-O-phosphate
-
73% of the activity with oleandomycin
-
-
?
ATP + clarithromycin
ADP + clarithromycin 2'-O-phosphate
-
-
-
?
ATP + clarithromycin
ADP + clarithromycin 2'-O-phosphate
recombinant expression of the pRSB111 plasmid in Pseudomonas sp. strain B13
-
-
?
ATP + erythromycin
ADP + erythromycin 2'-O-phosphate
-
-
-
?
ATP + erythromycin
ADP + erythromycin 2'-O-phosphate
-
14-membered ring macrolide
-
-
?
ATP + erythromycin
ADP + erythromycin 2'-O-phosphate
erythromycin resistance analyzed in recombinant Escherichia coli harbouring plasmid pRSB105
-
-
?
ATP + erythromycin
ADP + erythromycin 2'-O-phosphate
-
88% of the activity with oleandomycin
-
-
?
ATP + erythromycin
ADP + erythromycin-2'-O-phosphate
-
-
-
?
ATP + erythromycin
ADP + erythromycin-2'-O-phosphate
87% activity with respect to oleandomycin
-
-
?
ATP + erythromycin
ADP + erythromycin-2'-O-phosphate
-
81% activity with respect to oleandomycin for strain CU1, 24% activity with respect to oleandomycin for strain BM 2506
-
-
?
ATP + erythromycin
ADP + erythromycin-2'-O-phosphate
-
88% activity with respect to oleandomycin
-
-
?
ATP + erythromycin
ADP + erythromycin-2'-O-phosphate
-
-
-
-
?
ATP + erythromycin
ADP + erythromycin-2'-O-phosphate
-
-
-
-
?
ATP + erythromycin
ADP + erythromycin-2'-O-phosphate
-
-
-
?
ATP + erythromycin
ADP + erythromycin-2'-O-phosphate
recombinant expression of the pRSB111 plasmid in Pseudomonas sp. strain B13
-
-
?
ATP + josamycin
?
1% activity with respect to oleandomycin
-
-
?
ATP + josamycin
?
-
75-95% activity with respect to oleandomycin for strain CU1, 96% activity with respect to oleandomycin for strain BM 2506
-
-
?
ATP + josamycin
?
-
2% activity with respect to oleandomycin
-
-
?
ATP + midecamycin
?
3% activity with respect to oleandomycin
-
-
?
ATP + midecamycin
?
-
2% activity with respect to oleandomycin
-
-
?
ATP + oleandomycin
ADP + oleandomycin 2'-O-phosphate
-
-
?
ATP + oleandomycin
ADP + oleandomycin 2'-O-phosphate
-
-
-
?
ATP + oleandomycin
ADP + oleandomycin 2'-O-phosphate
-
-
-
?
ATP + oleandomycin
ADP + oleandomycin 2'-O-phosphate
-
-
?
ATP + oleandomycin
ADP + oleandomycin 2'-O-phosphate
-
-
?
ATP + oleandomycin
ADP + oleandomycin 2'-O-phosphate
-
-
?
ATP + oleandomycin
ADP + oleandomycin 2'-O-phosphate
-
-
-
?
ATP + oleandomycin
ADP + oleandomycin 2'-O-phosphate
-
14-membered ring macrolide
-
-
?
ATP + oleandomycin
ADP + oleandomycin 2'-O-phosphate
-
14-membered ring macrolide
-
-
?
ATP + oleandomycin
ADP + oleandomycin 2'-O-phosphate
-
-
-
?
ATP + oleandomycin
ADP + oleandomycin 2'-O-phosphate
-
-
-
?
ATP + oleandomycin
ADP + oleandomycin 2'-O-phosphate
-
-
-
?
ATP + oleandomycin
ADP + oleandomycin 2'-O-phosphate
-
-
-
?
ATP + oleandomycin
ADP + oleandomycin 2'-O-phosphate
-
-
-
?
ATP + oleandomycin
ADP + oleandomycin 2'-O-phosphate
-
-
-
?
ATP + oleandomycin
ADP + oleandomycin 2'-O-phosphate
-
-
-
?
ATP + oleandomycin
ADP + oleandomycin 2'-O-phosphate
-
-
-
?
ATP + roxithromycin
?
-
42% activity with respect to oleandomycin for strain CU1, about 2% activity with respect to oleandomycin for strain BM 2506
-
-
?
ATP + roxithromycin
?
-
44% activity with respect to oleandomycin
-
-
?
ATP + roxithromycin
ADP + roxithromycin 2'-O-phosphate
-
14-membered ring macrolide
-
-
?
ATP + roxithromycin
ADP + roxithromycin 2'-O-phosphate
-
44% of the activity with oleandomycin
-
-
?
ATP + roxithromycin
ADP + roxithromycin 2'-O-phosphate
-
-
-
?
ATP + roxithromycin
ADP + roxithromycin 2'-O-phosphate
recombinant expression of the pRSB111 plasmid in Pseudomonas sp. strain B13
-
-
?
ATP + spiramycin
ADP + spiramycin 2'-O-phosphate
-
-
-
?
ATP + spiramycin
ADP + spiramycin 2'-O-phosphate
-
57-75% activity with respect to oleandomycin for strain CU1, 26% activity with respect to oleandomycin for strain BM 2506
-
-
?
ATP + spiramycin
ADP + spiramycin 2'-O-phosphate
-
15-membered ring macrolide
-
-
?
ATP + spiramycin
ADP + spiramycin 2'-O-phosphate
-
15-membered ring macrolide
-
-
?
ATP + spiramycin
ADP + spiramycin 2'-O-phosphate
-
2% activity with respect to oleandomycin
-
-
?
ATP + spiramycin
ADP + spiramycin 2'-O-phosphate
-
-
-
-
?
ATP + spiramycin
ADP + spiramycin 2'-O-phosphate
-
-
-
-
?
ATP + telithromycin
ADP + telithromycin 2'-O-phosphate
-
-
-
?
ATP + telithromycin
ADP + telithromycin 2'-O-phosphate
the mph(A) gene conferrs resistance to telithromycin
-
-
?
ATP + telithromycin
ADP + telithromycin 2'-O-phosphate
the mph(A) gene conferrs resistance to telithromycin
-
-
?
ATP + telithromycin
ADP + telithromycin 2'-O-phosphate
the mph(A) gene conferrs resistance to telithromycin
-
-
?
ATP + tylosin
ADP + tylosin 2'-O-phosphate
-
15-membered ring macrolide
-
-
?
ATP + tylosin
ADP + tylosin 2'-O-phosphate
-
-
-
?
ATP + tylosin
ADP + tylosin 2'-O-phosphate
recombinant expression of the pRSB111 plasmid in Pseudomonas sp. strain B13
-
-
?
ATP + tylosin
ADP + tylosin 2'-phosphate
-
-
-
?
ATP + tylosin
ADP + tylosin 2'-phosphate
-
60% activity with respect to oleandomycin for strain CU1, 4% activity with respect to oleandomycin for strain BM 2506
-
-
?
ATP + tylosin
ADP + tylosin 2'-phosphate
-
2% activity with respect to oleandomycin
-
-
?
ATP + tylosin
ADP + tylosin 2'-phosphate
-
-
-
-
?
ATP + tylosin
ADP + tylosin 2'-phosphate
-
-
-
?
ATP + tylosin
ADP + tylosin 2'-phosphate
-
-
-
-
?
ATP + tylosin
ADP + tylosin 2'-phosphate
-
-
-
?
additional information
?
-
-
substrate specificities of wild-type and mutant enzymes, structure-function considerations
-
-
?
additional information
?
-
under physiological conditions, enzyme exclusively uses ATP, no substrate: GTP
-
-
?
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
-
substrate specificities of wild-type and mutant enzymes, structure-function considerations
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
O'Hara, K.; Kanda,T.; Kono, M.
Structure of a phosphorylated derivative of oleandomycin, obtained by reaction of oleandomycin with an extract of an erythromycin-resistant strain of Escherichia coli
J. Antibiot.
41
823-827
1988
Escherichia coli (Q47396)
brenda
Marshall, V.P.; Coats, J.H.; Baczynskyj, L.; Cialdella, J.I.; Liggett, W.F.; McGee, J.E.
Purification of macrolide 2'-phosphotransferase from Streptomyces coelicolor Muller
J. Ind. Microbiol.
6
295-298
1990
Streptomyces coelicolor, Streptomyces coelicolor UC 5240
-
brenda
O'Hara, K.; Kanda,T.; Ohmiya, K.; Ebisu, T.; Kono, M.
Purification and characterization of macrolide 2'-phosphotransferase from a strain of Escherichia coli that is highly resistant to erythromycin
Antimicrob. Agents Chemother.
33
1354-1357
1989
Escherichia coli (Q47396), Escherichia coli
brenda
Wiley, P.F.; Baczynskyj, L.; Dolak, L.A.; Cialdella, J.I.; Marshall, V.P.
Enzymatic phosphorylation of macrolide antibiotics
J. Antibiot.
40
195-201
1987
Streptomyces coelicolor, Streptomyces coelicolor UC 5240
brenda
Marshall, V.P.; Cialdella, J.I.; Baczynskyj, L.; Liggett, W.F.; Johnson, R.A.
Microbial O-phosphorylation of macrolide antibiotics
J. Antibiot.
62
132-134
1989
Streptomyces coelicolor, Streptomyces coelicolor UC 5240
-
brenda
Taniguchi, K.; Nakamura, A.; Tsurubuchi, K.; O'Hara, K.; Sawai, T.
Identification of Escherichia coli clinical isolates producing macrolide 2'-phosphotransferase by a highly sensitive detection method
FEMS Microbiol. Lett.
167
191-195
1998
Escherichia coli, Escherichia coli (Q47396)
brenda
Noguchi, N.; Katayama, J.
Expression in Pseudomonas aeruginosa of an erythromycin-resistance determinant that encodes the mphA gene for macrolide 2'-phosphotransferase I from Escherichia coli
Biol. Pharm. Bull.
21
191-193
1998
Pseudomonas aeruginosa, Escherichia coli (Q47396), Escherichia coli
brenda
Taniguchi, K.; Nakamura, A.; Tsurubuchi, K.; Ishii, A.; O'Hara, K.; Sawai, T.
Appearance in Japan of highly macrolide-resistant Escherichia coli producing macrolide 2'-phosphotransferase II
Microbios
97
137-144
1999
Escherichia coli
brenda
Taniguchi, K.; Nakamura, A.; Tsurubuchi, K.; Ishii, A.; O'Hara, K.; Sawai, T.
Identification of functional amino acids in the macrolide 2'-phosphotransferase II
Antimicrob. Agents Chemother.
43
2063-2065
1999
Escherichia coli
brenda
Noguchi, N.; Takada, K.; Katayama, J.; Emura, A.; Sasatsu, M.
Regulation of transcription of the mph(A) gene for macrolide 2'-phosphotransferase I in Escherichia coli: characterization of the regulatory gene mphR(A)
J. Bacteriol.
182
5052-5058
2000
Escherichia coli (Q47396), Escherichia coli
brenda
Nakamura, A.; Miyakozawa, I.; Nakazawa, K.; O'Hara, K.; Sawai, T.
Detection and characterization of macrolide 2'-phosphotransferase from a Pseudomonas aeruginosa clinical isolate
Antimicrob. Agents Chemother.
44
3241-3242
2000
Pseudomonas aeruginosa
brenda
Taniguchi, K.; Nakamura, A.; Tsurubuchi, K.; O'Hara, K.; Sawai, T.
The role of histidine residues conserved in the putative ATP-binding region of macrolide 2'-phosphotransferase II
FEMS Microbiol. Lett.
232
123-126
2004
Escherichia coli, Escherichia coli CU1
brenda
Chesneau, O.; Tsvetkova, K.; Courvalin, P.
Resistance phenotypes conferred by macrolide phosphotransferases
FEMS Microbiol. Lett.
269
317-322
2007
uncultured bacterium (A0AEF2), uncultured bacterium (Q5W3B4), Escherichia coli (Q47396), Salmonella enterica subsp. enterica serovar Typhimurium (Q5QJG2)
brenda
Szczepanowski, R.; Krahn, I.; Bohn, N.; Puehler, A.; Schlueter, A.
Novel macrolide resistance module carried by the IncP-1beta resistance plasmid pRSB111, isolated from a wastewater treatment plant
Antimicrob. Agents Chemother.
51
673-678
2007
uncultured bacterium (Q5W3B4)
brenda
Schlueter, A.; Szczepanowski, R.; Kurz, N.; Schneiker, S.; Krahn, I.; Puehler, A.
Erythromycin resistance-conferring plasmid pRSB105, isolated from a sewage treatment plant, harbors a new macrolide resistance determinant, an integron-containing Tn402-like element, and a large region of unknown function
Appl. Environ. Microbiol.
73
1952-1960
2007
Escherichia coli (Q47396)
brenda
Shakya, T.; Wright, G.D.
Nucleotide selectivity of antibiotic kinases
Antimicrob. Agents Chemother.
54
1909-1913
2010
Escherichia coli (Q47396)
brenda
Fong, D.H.; Burk, D.L.; Blanchet, J.; Yan, A.Y.; Berghuis, A.M.
Structural basis for kinase-mediated macrolide antibiotic resistance
Structure
25
750-761.e5
2017
Escherichia coli (O32553), Escherichia coli (Q9EVJ6)
brenda