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Literature summary extracted from

  • Obranic, S.; Babic, F.; Mocibob, M.; Maravic-Vlahovicek, G.
    Ribosomal A site binding pattern differs between Arm methyltransferases from clinical pathogens and a natural producer of aminoglycosides (2024), Int. J. Biol. Macromol., 282, 137015.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.179 gene armA, recombinant expression in Escherichia coli strain MC338 Escherichia coli
2.1.1.179 gene rmtB, recombinant expression in Escherichia coli strain MC338 Escherichia coli
2.1.1.179 gene rmtC, recombinant expression in Escherichia coli strain MC338 Proteus mirabilis
2.1.1.179 gene rmtD, recombinant expression in Escherichia coli strain MC338 Escherichia coli
2.1.1.179 gene sgm, recombinant expression in Escherichia coli strain MC338 Micromonospora zionensis

Protein Variants

EC Number Protein Variants Comment Organism
2.1.1.179 additional information introduction of single mutations at the ribosomal A site near the G1405 nucleotide in helix 44 of 16S rRNA to assess their impact on the methylation ability of the Arm methyltransferase in Escherichia coli cells with homogeneous mutant ribosomes Escherichia coli
2.1.1.179 additional information introduction of single mutations at the ribosomal A site near the G1405 nucleotide in helix 44 of 16S rRNA to assess their impact on the methylation ability of the Arm methyltransferase in Escherichia coli cells with homogeneous mutant ribosomes Proteus mirabilis
2.1.1.179 additional information introduction of single mutations at the ribosomal A site near the G1405 nucleotide in helix 44 of 16S rRNA to assess their impact on the methylation ability of the Arm methyltransferase in Escherichia coli cells with homogeneous mutant ribosomes Micromonospora zionensis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.179 S-adenosyl-L-methionine + guanine1405 in 16S rRNA Escherichia coli
-
 S-adenosyl-L-homocysteine + N7-methylguanine1405 in 16S rRNA
-
 ?
2.1.1.179 S-adenosyl-L-methionine + guanine1405 in 16S rRNA Proteus mirabilis
-
 S-adenosyl-L-homocysteine + N7-methylguanine1405 in 16S rRNA
-
 ?
2.1.1.179 S-adenosyl-L-methionine + guanine1405 in 16S rRNA Micromonospora zionensis
-
 S-adenosyl-L-homocysteine + N7-methylguanine1405 in 16S rRNA
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.179 Escherichia coli B8YJJ8
-
-
2.1.1.179 Escherichia coli Q763K9
-
-
2.1.1.179 Escherichia coli M4TDG9
-
-
2.1.1.179 Escherichia coli G4WZ44
-
-
2.1.1.179 Micromonospora zionensis Q7M0R2
-
-
2.1.1.179 Proteus mirabilis Q33DX5
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.179 additional information substrates are wild-type and mutant rRNA and ribosomes from Escherichia coli strains, substrate specificity, overview. Arm methyltransferases isolated from clinical bacterial strains are able to methylate their target nucleotide, G1405, on most mutant ribosomes, but methyltransferases RmtB, ArmA, and RmtC are unable to methylate G1405 on ribosomes with the U1406A mutation (RmtB, ArmA) or the A1408G mutation (RmtC). Structure-function analysis, overview Escherichia coli ?
-
-
2.1.1.179 additional information substrates are wild-type and mutant rRNA and ribosomes from Escherichia coli strains, substrate specificity, overview. Arm methyltransferases isolated from clinical bacterial strains are able to methylate their target nucleotide, G1405, on most mutant ribosomes, but methyltransferases RmtB, ArmA, and RmtC are unable to methylate G1405 on ribosomes with the U1406A mutation (RmtB, ArmA) or the A1408G mutation (RmtC). RmtB also cannot methylate G1405 in ribosomes containing the G1491U mutation. Structure-function analysis, overview Escherichia coli ?
-
-
2.1.1.179 additional information substrates are wild-type and mutant rRNA and ribosomes from Escherichia coli strains, substrate specificity, overview. Arm methyltransferases isolated from clinical bacterial strains are able to methylate their target nucleotide, G1405, on most mutant ribosomes, but methyltransferases RmtB, ArmA, and RmtC are unable to methylate G1405 on ribosomes with the U1406A mutation (RmtB, ArmA) or the A1408G mutation (RmtC). Structure-function analysis, functional differences between Sgm and RmtC methyltransferases, overview Proteus mirabilis ?
-
-
2.1.1.179 additional information substrates are wild-type and mutant rRNA and ribosomes from Escherichia coli strains, substrate specificity, overview. Arm methyltransferases isolated from clinical bacterial strains are able to methylate their target nucleotide, G1405, on most mutant ribosomes. Structure-function analysis, functional differences between Sgm and RmtC methyltransferases , overview Escherichia coli ?
-
-
2.1.1.179 additional information substrates are wild-type and mutant rRNA and ribosomes from Escherichia coli strains, substrate specificity, overview. Sgm methyltransferase is unable to methylate G1405 in ribosomes containing A1408G, G1491U, or U1495A mutations. Structure-function analysis, overview Micromonospora zionensis ?
-
-
2.1.1.179 additional information substrates are wild-type and mutant rRNA and ribosomes from Escherichia coli strains, substrate specificity, overview. Arm methyltransferases isolated from clinical bacterial strains re able to methylate their target nucleotide, G1405, on most mutant ribosomes, but methyltransferases RmtB, ArmA, and RmtC are unable to methylate G1405 on ribosomes with the U1406A mutation (RmtB, ArmA) or the A1408G mutation (RmtC). Structure-function analysis, functional differences between Sgm and RmtC methyltransferases, overview Escherichia coli ?
-
-
2.1.1.179 S-adenosyl-L-methionine + guanine1405 in 16S rRNA
-
 Escherichia coli S-adenosyl-L-homocysteine + N7-methylguanine1405 in 16S rRNA
-
 ?
2.1.1.179 S-adenosyl-L-methionine + guanine1405 in 16S rRNA
-
 Proteus mirabilis S-adenosyl-L-homocysteine + N7-methylguanine1405 in 16S rRNA
-
 ?
2.1.1.179 S-adenosyl-L-methionine + guanine1405 in 16S rRNA
-
 Micromonospora zionensis S-adenosyl-L-homocysteine + N7-methylguanine1405 in 16S rRNA
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.1.1.179 16S rRNA (guanine(1405)-N(7))-methyltransferase UniProt Escherichia coli
2.1.1.179 16S rRNA (guanine(1405)-N(7))-methyltransferase SwissProt Proteus mirabilis
2.1.1.179 16S rRNA (guanine(1405)-N(7))-methyltransferase SwissProt Micromonospora zionensis
2.1.1.179 Arm methyltransferase
-
 Escherichia coli
2.1.1.179 Arm methyltransferase
-
 Proteus mirabilis
2.1.1.179 ArmA
-
 Escherichia coli
2.1.1.179 RmtB
-
 Escherichia coli
2.1.1.179 RmtC
-
 Proteus mirabilis
2.1.1.179 RmtC
-
 Escherichia coli
2.1.1.179 RmtD
-
 Escherichia coli
2.1.1.179 RmtD1
-
 Escherichia coli
2.1.1.179 sgm
-
 Micromonospora zionensis
2.1.1.179 Sgm methyltransferase
-
 Micromonospora zionensis

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.1.179 S-adenosyl-L-methionine
-
 Escherichia coli
2.1.1.179 S-adenosyl-L-methionine
-
 Proteus mirabilis
2.1.1.179 S-adenosyl-L-methionine
-
 Micromonospora zionensis

General Information

EC Number General Information Comment Organism
2.1.1.179 metabolism the ribosomal A site binding patterns of Arm methyltransferases from clinical pathogens (ArmA, RmtB, RmtC, and RmtD) with those of the Sgm methyltransferase from a natural aminoglycoside producer. Sgm methyltransferase exhibited a distinct methylation pattern compared to Arm methyltransferases from clinical strains. Structural comparisons of Sgm, RmtB, and RmtC reveal different spatial orientations of key amino acids involved in ribosomal binding, highlighting evolutionary differences Escherichia coli
2.1.1.179 metabolism the ribosomal A site binding patterns of Arm methyltransferases from clinical pathogens (ArmA, RmtB, RmtC, and RmtD) with those of the Sgm methyltransferase from a natural aminoglycoside producer. Sgm methyltransferase exhibited a distinct methylation pattern compared to Arm methyltransferases from clinical strains. Structural comparisons of Sgm, RmtB, and RmtC reveal different spatial orientations of key amino acids involved in ribosomal binding, highlighting evolutionary differences Proteus mirabilis
2.1.1.179 metabolism the ribosomal A site binding patterns of Arm methyltransferases from clinical pathogens (ArmA, RmtB, RmtC, and RmtD) with those of the Sgm methyltransferase from a natural aminoglycoside producer. Sgm methyltransferase exhibited a distinct methylation pattern compared to Arm methyltransferases from clinical strains. Structural comparisons of Sgm, RmtB, and RmtC reveal different spatial orientations of key amino acids involved in ribosomal binding, highlighting evolutionary differences Micromonospora zionensis
2.1.1.179 additional information comparison of the 3D structures of Escherichia coli and a member of the aminoglycoside-producing genera Micromonospora sp. 16S rRNA by aligning the 16S rRNA from the known crystal structure of the small ribosomal subunit of Escherichia coli with a model of Micromonospora sp. 16S rRNA Micromonospora zionensis