2.1.1.298: ribosomal protein L3 N5-glutamine methyltransferase
This is an abbreviated version!
For detailed information about ribosomal protein L3 N5-glutamine methyltransferase, go to the full flat file.
Reaction
Synonyms
PrmB, PrmB-type N5-glutamine methyltransferase, YfcB
ECTree
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General Information
General Information on EC 2.1.1.298 - ribosomal protein L3 N5-glutamine methyltransferase
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evolution
malfunction
physiological function
the S-adenosyl-L-methionine-dependent methyltransferase from Azospirillum brasilense is more closely related to a PrmB-type N5-glutamine methyltransferase than to the arsenate detoxifying methyltransferase ArsM. It belongs to the S-adenosylmethionine (SAM)-dependent methyltransferases, a large family of enzymes that transfer methyl groups from SAMto nitrogen, oxygen, or carbon atoms in a wide variety of substrates such as nucleic acids, proteins, and other small molecules
evolution
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the S-adenosyl-L-methionine-dependent methyltransferase from Azospirillum brasilense is more closely related to a PrmB-type N5-glutamine methyltransferase than to the arsenate detoxifying methyltransferase ArsM. It belongs to the S-adenosylmethionine (SAM)-dependent methyltransferases, a large family of enzymes that transfer methyl groups from SAMto nitrogen, oxygen, or carbon atoms in a wide variety of substrates such as nucleic acids, proteins, and other small molecules
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insertional inactivation of prmB gene in Azospirillum brasilense results in an increased sensitivity to chloramphenicol and resistance to tiamulin and clindamycin, which are known to bind at the peptidyl transferase center (PTC) in the ribosome. These observations suggest that the inability of prmB:km mutant to methylate L3 protein might alter hydrophobicity in the antibiotic-binding pocket of the PTC, which might affect the binding of chloramphenicol, clindamycin, and tiamulin differentially
malfunction
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insertional inactivation of prmB gene in Azospirillum brasilense results in an increased sensitivity to chloramphenicol and resistance to tiamulin and clindamycin, which are known to bind at the peptidyl transferase center (PTC) in the ribosome. These observations suggest that the inability of prmB:km mutant to methylate L3 protein might alter hydrophobicity in the antibiotic-binding pocket of the PTC, which might affect the binding of chloramphenicol, clindamycin, and tiamulin differentially
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role of PrmB-type N5-glutamine methyltransferases in conferring resistance to tiamulin and clindamycin in any bacterium. the enzyme is not involved in arsenate detoxification
physiological function
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role of PrmB-type N5-glutamine methyltransferases in conferring resistance to tiamulin and clindamycin in any bacterium. the enzyme is not involved in arsenate detoxification
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