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Literature summary extracted from

  • Singh, S.; Singh, C.; Tripathi, A.K.
    A SAM-dependent methyltransferase cotranscribed with arsenate reductase alters resistance to peptidyl transferase center-binding antibiotics in Azospirillum brasilense Sp7 (2014), Appl. Microbiol. Biotechnol., 98, 4625-4636.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.298 gene prmB, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, recombinant expression in Escherichia coli strain BL21(DE3) and in the arsenite-hypersensitive Escherichia coli strain AW3110(DE3), subcloning in Escherichia coli strain DH5alpha Azospirillum brasilense

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.1.1.298 39000
-
 x * 39000, about, recombinant enzyme, SDS_PAGE Azospirillum brasilense

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.298 Azospirillum brasilense A0A0P0ETL9 gene prmB
-
2.1.1.298 Azospirillum brasilense ATCC 29729 A0A0P0ETL9 gene prmB
-

Subunits

EC Number Subunits Comment Organism
2.1.1.298 ? x * 39000, about, recombinant enzyme, SDS_PAGE Azospirillum brasilense

Synonyms

EC Number Synonyms Comment Organism
2.1.1.298 PrmB-type N5-glutamine methyltransferase
-
 Azospirillum brasilense

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.1.298 S-adenosyl-L-methionine
-
 Azospirillum brasilense

General Information

EC Number General Information Comment Organism
2.1.1.298 evolution 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 Azospirillum brasilense
2.1.1.298 malfunction 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 Azospirillum brasilense
2.1.1.298 physiological function 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 Azospirillum brasilense