2.1.1.192: 23S rRNA (adenine2503-C2)-methyltransferase
This is an abbreviated version!
For detailed information about 23S rRNA (adenine2503-C2)-methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.192
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2.1.1.192
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5\'-deoxyadenosyl
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5'-deoxyadenosine
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radical-mediated
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ripps
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desii
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venezuelae
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maturase
- 2.1.1.192
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5\'-deoxyadenosyl
- 5'-deoxyadenosine
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radical-mediated
-
ripps
- desii
- venezuelae
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maturase
Reaction
2 S-adenosyl-L-methionine + + 2 reduced [2Fe-2S] ferredoxin = + + + + 2 oxidized [2Fe-2S] ferredoxin
Synonyms
Cfr, EC 2.1.1.194, methyltransferase YfgB/RlmN, NlmA, radical AdoMet rRNA methyltransferase, radical S-adenosyl-L-methionine enzyme, radical SAM enzyme, RlmN, RlmN methyltransferase, YfgB, YfgB/RlmN
ECTree
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Engineering
Engineering on EC 2.1.1.192 - 23S rRNA (adenine2503-C2)-methyltransferase
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C363A
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mutation in putative metyl-binding residue, substitution alters iron-sulfur cluster stability. Mutant exhibits negligible activity
C118A
C338A
the mutant binds S-adenosyl-L-methionine with wild type affinity, while oxidation of the [4Fe-4S] cluster is not observed
additional information
C118A
mutant is unable to resolve a covalent protein/RNA intermediate during catalysis and becomes cross-linked to the nucleic acid
C118A
site-directed mutagenesis, analysis of the structure of a key intermediate in the RlmN reaction, in which a C118A variant of the protein is cross-linked to a tRNAGlu substrate
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Cfr contains an additional Cys-rich C-terminal domain that binds a mononuclear Fe2+ ion in a rubredoxin-type Cys4 motif. The C-terminal domain can be truncated with minimal impact on Cfr activity, but the rate of turnover is decreased upon disruption of the Fe2+-binding site by Zn2+ substitution or ligand mutation
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
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