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Information on EC 2.7.1.136 - macrolide 2'-kinase
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2.7.1.136 macrolide 2'-kinaseIUBMB Comments
Erythromycin, spiramycin and some other macrolide antibiotics can also act as acceptors.
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Word Map
- 2.7.1.136
- erythromycin
- oleandomycin
-
erythromycin-resistant
-
phosphotransferases
- aminoglycoside
-
self-transferable
- purine
- roxithromycin
- triphosphate
- itp
- repressor
-
16-membered
- agarose
- 2'-phosphate
- iodine
- edta
-
macrolide-resistance
- aeruginosa
- analysis
The enzyme appears in viruses and cellular organisms
Synonyms
macrolide 2'-phosphotransferase, mph(2'), macrolide 2'-phosphotransferase ii, mph (2'), mph(2')-i, mph(2')-ii, macrolide 2'-phosphotransferase type ii, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
macrolide 2'-phosphotransferase
macrolide 2'-phosphotransferase II
Mph
-
-
-
-
MPH (2')
-
-
-
-
MPH(2')
mphA
phosphotransferase, macrolide 2'-
-
-
-
-
macrolide 2'-phosphotransferase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + oleandomycin = ADP + oleandomycin 2'-O-phosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
ATP:macrolide 2'-O-phosphotransferase
Erythromycin, spiramycin and some other macrolide antibiotics can also act as acceptors.
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CAS REGISTRY NUMBER
COMMENTARY
116036-69-2
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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 + rokitamycin
ADP + rokitamycin 2'-O-phosphate
-
15-membered ring macrolide
-
-
?
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 + 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
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
-
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
recombinant expression of the pRSB111 plasmid in Pseudomonas sp. strain B13
-
-
?
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
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
recombinant expression of the pRSB111 plasmid in Pseudomonas sp. strain B13
-
-
?
ATP + josamycin
?
-
75-95% activity with respect to oleandomycin for strain CU1, 96% activity with respect to oleandomycin for strain BM 2506
-
-
?
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 + 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
recombinant expression of the pRSB111 plasmid in Pseudomonas sp. strain B13
-
-
?
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 + 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
recombinant expression of the pRSB111 plasmid in Pseudomonas sp. strain B13
-
-
?
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
-
-
?
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
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-
-
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
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-
-
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
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
under physiological conditions, enzyme exclusively uses ATP, no substrate: GTP
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
additional information
additional information
-
potassium chloride enhances reactivity, it is added in the reaction mixture at 0.06 M
additional information
potassium chloride enhances reactivity, it is added in the reaction mixture at 0.06 M
additional information
potassium chloride enhances reactivity, it is added in the reaction mixture at 0.06 M
additional information
-
potassium chloride enhances reactivity, it is added in the reaction mixture at 0.06 M
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
1 mM p-chloromercuribenzoic acid or urea are no inhibitors, MphR(A) is a repressor protein that binds to the promoter of the mph(A) gene and negatively regulates the enzyme expression
-
additional information
-
1 mM p-chloromercuribenzoic acid or urea are no inhibitors, MphR(A) is a repressor protein that binds to the promoter of the mph(A) gene and negatively regulates the enzyme expression
-
additional information
1 mM p-chloromercuribenzoic acid or urea are no inhibitors, MphR(A) is a repressor protein that binds to the promoter of the mph(A) gene and negatively regulates the enzyme expression
-
additional information
-
1 mM p-chloromercuribenzoic acid or urea are no inhibitors, MphR(A) is a repressor protein that binds to the promoter of the mph(A) gene and negatively regulates the enzyme expression
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
erythromycin
crude cell extracts from cells treated with erythromycin show increased activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.04
-
purified recombinant wild-type enzyme, substrate roxithromycin or rokitamycin
0.05
-
purified recombinant wild-type enzyme, substrate josamycin or tylosin
0.06
-
purified recombinant wild-type enzyme, substrate troleandomycin, clarithromycin, azithromycin, or erythromycin
additional information
additional information
genetic map of the resistance plasmid pRSB105, functional antibiotic resistance regions of plasmid pRSB105 characterized, plasmid pRSB105 harbors the macrolide resistance gene mph, encoding a macrolide 2'-phosphotransferase, transcript analysis by RT-PCR, erythromycin resistance analyzed by determining values for minimum inhibitory concentration, mph gene shown to contribute to erythromycin resistance
additional information
accessory region on plasmid pRSB111 contains a new macrolide resistance operon, mph(E) gene encodes a macrolide phosphotransferase required for high-level macrolide resistance, resistance analyzed by determining values for minimum inhibitory concentration
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
macrolide 2'-phosphotransferase type I, high levels of activity with 14-member ring macrolides and extremely low levels with 16-member ring macrolides, accession code corresponds to nucleotide sequence for several proteins
UniProt
brenda
macrolide 2'-phosphotransferase type II, similar levels of activity with 14-member ring macrolides or 16-member ring macrolides, strain CU1 or BM 2506
-
-
brenda
macrolide resistance plasmid pRSB111, isolated from bacteria residing in the final effluents of a wastewater treatment plant
SwissProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
mph gene is located on nontransmissible plasmid DNA for Escherichia coli strain CU1
-
brenda
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