Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.1.1.192 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
Search for more literature for 2.1.1.192

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
homology modeling of structure and comparison with Cfr from Staphylococcus sciuri, EC 2.1.1.194 Escherichia coli

Protein Variants

Protein Variants Comment Organism
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
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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 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
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P36979
-
-
Mammaliicoccus sciuri A0A1X0U0N1
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 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 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
-
 ?
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

Synonyms Comment Organism
NlmA
-
 Escherichia coli
RlmN
-
 Mammaliicoccus sciuri

Cofactor

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

General Information

General Information Comment Organism
evolution evolutionary relationship between the Cfr (EC 2.1.1.224) and RlmN enzymes, phylogenetic analysis, overview Mammaliicoccus sciuri
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
physiological function antibiotic resistance effects of wild-type and mutant enzymes, overview Mammaliicoccus sciuri