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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
-
-
-
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
-
-
?
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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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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the macrolide phosphotransferase structures show that the enzymes are related to the aminoglycoside phosphotransferases, but are distinguished from them by the presence of a large interdomain linker that contributes to an expanded antibiotic binding pocket
physiological function
macrolide phosphotransferase enzymes can inactivate the macrolides, a class of antibiotic, characterized by a large macrocyclic lactone ring. Broad-spectrum resistance is conferred by the enzymes
additional information
additional information
the large interdomain linker contributes to an expanded antibiotic binding pocket. This pocket is largely hydrophobic, with a negatively charged patch located at a conserved aspartate residue. Comparison of the enzyme-macrolide complex structure with the structures of macrolides bound to their natural target, the 50S ribosome, overview. Nucleotides bind to MPH(2')-I in a cleft between the N-terminal lobe and the core subdomain of the C-terminal lobe, binding site structure analysis
additional information
the large interdomain linker contributes to an expanded antibiotic binding pocket. This pocket is largely hydrophobic, with a negatively charged patch located at a conserved aspartate residue. Comparison of the enzyme-macrolide complex structure with the structures of macrolides bound to their natural target, the 50S ribosome, overview. Nucleotides bind to MPH(2')-I in a cleft between the N-terminal lobe and the core subdomain of the C-terminal lobe, binding site structure analysis
additional information
the large interdomain linker contributes to an expanded antibiotic binding pocket. This pocket is largely hydrophobic, with a negatively charged patch located at a conserved aspartate residue. Comparison of the enzyme-macrolide complex structure with the structures of macrolides bound to their natural target, the 50S ribosome, overview. Nucleotides bind to MPH(2')-II in a cleft between the N-terminal lobe and the core subdomain of the C-terminal lobe, binding site structure analysis
additional information
the large interdomain linker contributes to an expanded antibiotic binding pocket. This pocket is largely hydrophobic, with a negatively charged patch located at a conserved aspartate residue. Comparison of the enzyme-macrolide complex structure with the structures of macrolides bound to their natural target, the 50S ribosome, overview. Nucleotides bind to MPH(2')-II in a cleft between the N-terminal lobe and the core subdomain of the C-terminal lobe, binding site structure analysis
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Q5W3B4_9BACT
301
0
33228
TrEMBL
other Location (Reliability: 1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified isozyme MPH(2')-I in apoform and in complex with GTP analogues and six different macrolides (guanosine 5'-[beta,gamma-imido]triphosphate (GMPPNP) or guanosine diphosphate (GDP) and either a 14-membered lactone macrolide: erythromycin, oleandomycin, or clarithromycin, or the 15-membered lactone macrolide azithromycin), X-ray diffraction structure determination analysis at 1.2-1.6 A resolution, molecular replacement method, modeling. Despite the inclusion of MgCl2 in the crystallization experiments, no evidence of magnesium ions is observed in any of the MPH(2')-I electron density maps
purified isozyme MPH(2')-II in apoform and in complex with GTP analogues and six different macrolides (guanosine diphosphate (GDP) or GDP or GTPgS (guanosine 5'-O-[gamma-thio]triphosphate) and either a 14-membered lactone macrolide: erythromycin, oleandomycin, or clarithromycin, or the 15-membered lactone macrolide azithromycin), X-ray diffraction structure determination analysis at 1.31-1.65 A resolution, molecular replacement method, modeling. At least one divalent metal ion (either Mg2+ or Ca2+, based on the geometry and bond distances) from the crystallization solution is observed in the nucleotide binding pocket
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H198A
-
site-directed mutagenesis, 50% reduction of the minimal inhibitory concentration MIC level of oleandomycin and 50% reduced activity compared to the wild-type enzyme
H205A
-
site-directed mutagenesis, 87.5% reduction of the minimal inhibitory concentration MIC level of oleandomycin and 50% reduced activity compared to the wild-type enzyme
H205N
-
site-directed mutagenesis, unaffected minimal inhibitory concentration MIC level of oleandomycin, but more than 99% reduced activity compared to the wild-type enzyme
H198A
-
site-directed mutagenesis, 50% reduction of the minimal inhibitory concentration MIC level of oleandomycin and 50% reduced activity compared to the wild-type enzyme
-
H205A
-
site-directed mutagenesis, 87.5% reduction of the minimal inhibitory concentration MIC level of oleandomycin and 50% reduced activity compared to the wild-type enzyme
-
H205N
-
site-directed mutagenesis, unaffected minimal inhibitory concentration MIC level of oleandomycin, but more than 99% reduced activity compared to the wild-type enzyme
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, Tris-HCl buffer pH 7, 0.06 M KCl, 0.01 M MgCl2, 0.006 M 2-mercaptoethanol, stable
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli DH5alpha, complete pRSB105 macrolide resistance gene region cloned into the vector pBCSK, recombinant plasmid pNK-mph carries the complete mph gene in pBluescript II KS, transcription from the constructed plasmids analyzed by RT-PCR, constructs tested for conferring erythromycin and azithromycin resistance
expressed in Escherichia coli, strain DH5alpha mcr containing the pBCSK vector carrying a chloramphenicol resistance gene and the pRSB111 erythromycin resistance-conferring region, recombinant expression in Pseudomonas sp. strain B13 GFP1
mph gene for Escherichia coli strain CU1 is identical to that previously reported for mphB from Escherichia coli strain BM 2506
-
mph genes cloned into Escherichia coli AG100A
mphA gene is arranged in close proximity to mrx and MphR(A) which are proteins probably involved in mph regulation, they all form a gene cluster
mph genes cloned into Escherichia coli AG100A
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
competitive assay that mimics in vivo nucleotide triphosphate concentrations and usage by the enzyme. Downstream analysis of reaction products by high-performance liquid chromatography enables the determination of partitioning of phosphate flux from nucleotide triphosphate donors to antibiotics
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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