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Literature summary extracted from

  • Ntokou, E.; Hansen, L.; Kongsted, J.; Vester, B.
    Biochemical and computational analysis of the substrate specificities of Cfr and RlmN Methyltransferases (2015), PLoS ONE, 10, e0145655 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.192 gene rlmN, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain JW2501-1 (rlmN knockout) and AS19 Mammaliicoccus sciuri
2.1.1.224 gene cfr, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain JW2501-1 (rlmN knockout) and AS19 Mammaliicoccus sciuri

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.1.192 homology modeling of structure and comparison with Cfr from Staphylococcus sciuri, EC 2.1.1.194 Escherichia coli
2.1.1.224 homology modeling of structure and comparison with RlmN from Echerichia coli, EC 2.1.1.192 Mammaliicoccus sciuri

Protein Variants

EC Number Protein Variants Comment Organism
2.1.1.192 additional information construction of chimera between Cfr from Staphylococcus sciuri and RlmN to analyze C2/C8 and C2 methylation specificity, respectively. The catalytic site is expected to be responsible for the C2/C8 specificity of Cfr. Almost all replacements show no function in the primer extension assay, apart from a few that have a weak effect Escherichia coli
2.1.1.192 additional information construction of chimeric mutants of gene rlmN, cfr1234567rrlmN and rlmN1234567rcfr, and construction of mixed genes containing gene fragment of cfr and rlmN genes, overview. Analysis of effects of the mutations on catalytic activity and antibiotics resistance. pBRCfr2XrRlmN and pBRCfr7XrRlmN show no reduced antibiotic sensitivity. The enzyme encoded by plasmid pBRCfr3XrRlmN shows a reduced susceptibility to all three antibiotics, although the effect is smaller than that caused by pBRCfr. Thus, the Cfr3XrRlmN mixed enzyme has a decreased function compared to the Cfr enzyme Mammaliicoccus sciuri
2.1.1.224 additional information construction of chimera between Cfr and RlmN from Echerichia coli to analyze C2/C8 and C2 methylation specificity, respectively. The catalytic site is expected to be responsible for the C2/C8 specificity. Almost all replacements show no function in the primer extension assay, apart from a few that have a weak effect Mammaliicoccus sciuri
2.1.1.224 additional information construction of chimeric mutants of gene cfr, cfr1234567rrlmN and rlmN1234567rcfr, and construction of mixed genes containing gene fragment of cfr and rlmN genes, overview. Analysis of effects of the mutations on catalytic activity and antibiotics resistance Mammaliicoccus sciuri

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.192 2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin Mammaliicoccus sciuri
-
 S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin
-
 ?
2.1.1.192 2 S-adenosyl-L-methionine + adenine37 in tRNA + 2 reduced [2Fe-2S] ferredoxin Mammaliicoccus sciuri
-
 2 S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine37 in tRNA + 2 oxidized [2Fe-2S] ferredoxin
-
 ?
2.1.1.224 2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin Mammaliicoccus sciuri
-
 S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.192 Escherichia coli P36979
-
-
2.1.1.192 Mammaliicoccus sciuri A0A1X0U0N1
-
-
2.1.1.224 Mammaliicoccus sciuri Q9FBG4
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.192 2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin
-
 Escherichia coli S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine2503 in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin
-
 ?
2.1.1.192 2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin
-
 Mammaliicoccus sciuri S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin
-
 ?
2.1.1.192 2 S-adenosyl-L-methionine + adenine37 in tRNA + 2 reduced [2Fe-2S] ferredoxin
-
 Mammaliicoccus sciuri 2 S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine37 in tRNA + 2 oxidized [2Fe-2S] ferredoxin
-
 ?
2.1.1.192 additional information Cfr methylates A2503 of 23S rRNA at C8 and C2, while RlmN only performs a C2 methylation using the same mechanism of function Mammaliicoccus sciuri ?
-
-
2.1.1.224 2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA
-
 Mammaliicoccus sciuri 2 S-adenosyl-L-homocysteine + 2,8-dimethyladenine2503 in 23S rRNA
-
 ?
2.1.1.224 2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin
-
 Mammaliicoccus sciuri S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin
-
 ?
2.1.1.224 additional information Cfr methylates A2503 of 23S rRNA at C8 and C2, while RlmN only performs a C2 methylation using the same mechanism of function Mammaliicoccus sciuri ?
-
-

Synonyms

EC Number Synonyms Comment Organism
2.1.1.192 NlmA
-
 Escherichia coli
2.1.1.192 RlmN
-
 Mammaliicoccus sciuri
2.1.1.224 Cfr
-
 Mammaliicoccus sciuri

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.1.192 4Fe-4S-center
-
 Escherichia coli
2.1.1.192 reduced [2Fe-2S] ferredoxin
-
 Mammaliicoccus sciuri
2.1.1.192 S-adenosyl-L-methionine
-
 Mammaliicoccus sciuri
2.1.1.192 [4Fe-4S] cluster
-
 Mammaliicoccus sciuri
2.1.1.224 4Fe-4S-center
-
 Mammaliicoccus sciuri
2.1.1.224 reduced [2Fe-2S] ferredoxin
-
 Mammaliicoccus sciuri
2.1.1.224 S-adenosyl-L-methionine
-
 Mammaliicoccus sciuri
2.1.1.224 [4Fe-4S] cluster
-
 Mammaliicoccus sciuri

General Information

EC Number General Information Comment Organism
2.1.1.192 evolution evolutionary relationship between the Cfr (EC 2.1.1.224) and RlmN enzymes, phylogenetic analysis, overview Mammaliicoccus sciuri
2.1.1.192 additional information mechanisms of catalytic action of Cfr (EC 2.1.1.224) and related RlmN, the methylation mechanism involves a transitory methylation of Cys338 for Cfr and Cys355 for RlmN, investigation of target binding to the active sites of the two enzymes, overview. Cfr and RlmN are methylated before transfer of the methyl group to the substrate. Molecular dynamics simulations, and calculation of the binding free energy, using the structure of Escherichia coli RlmN (PDB ID 3RFA). Defining regions of the active site to be interchanged to investigate C8/C2 specificity Mammaliicoccus sciuri
2.1.1.192 physiological function antibiotic resistance effects of wild-type and mutant enzymes, overview Mammaliicoccus sciuri
2.1.1.224 evolution evolutionary relationship between the Cfr and RlmN (EC 2.1.1.192) enzymes, phylogenetic analysis, overview Mammaliicoccus sciuri
2.1.1.224 additional information mechanisms of catalytic action of Cfr and related RlmN (EC 2.1.1.192), the methylation mechanism involves a transitory methylation of Cys338 for Cfr and Cys355 for RlmN, investigation of target binding to the active sites of the two enzymes, overview. Cfr and RlmN are methylated before transfer of the methyl group to the substrate. Homology structure modelling, molecular dynamics simulations, and calculation of the binding free energy, using structure of Escherichia coli RlmN (PDB ID 3RFA), the homology model is made with the [4Fe-4S] cluster and a SAM molecule positioned in the same way as seen in the RlmN X-ray structure. Defining regions of the active site to be interchanged to investigate C8/C2 specificity Mammaliicoccus sciuri
2.1.1.224 physiological function antibiotic resistance effects of wild-type and mutant enzymes, overview Mammaliicoccus sciuri