2.7.1.136: macrolide 2'-kinase
This is an abbreviated version!
For detailed information about macrolide 2'-kinase, go to the full flat file.
Word Map on EC 2.7.1.136
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2.7.1.136
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erythromycin
-
oleandomycin
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erythromycin-resistant
-
phosphotransferases
-
aminoglycoside
-
self-transferable
-
purine
-
roxithromycin
-
triphosphate
-
itp
-
repressor
-
16-membered
-
agarose
-
2'-phosphate
-
iodine
-
edta
-
macrolide-resistance
-
aeruginosa
-
analysis
- 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
Reaction
Synonyms
macrolide 2'-phosphotransferase, macrolide 2'-phosphotransferase II, macrolide 2'-phosphotransferase type I, macrolide 2'-phosphotransferase type II, Mph, MPH (2'), MPH(2'), MPH(2')-I, MPH(2')-II, mphA, mphB, phosphotransferase, macrolide 2'-
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General Information on EC 2.7.1.136 - macrolide 2'-kinase
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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
