2.1.1.224: 23S rRNA (adenine2503-C8)-methyltransferase
This is an abbreviated version!
For detailed information about 23S rRNA (adenine2503-C8)-methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.224
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2.1.1.224
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linezolid
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oxazolidinone
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5\'-deoxyadenosyl
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thiopeptide
-
optra
-
linezolid-resistant
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phenicols
-
cobalamin-dependent
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phlopsa
-
pleuromutilins
-
nosiheptide
-
5'-deoxyadenosine
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poxta
-
ribosome-targeting
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cobiialamin
- 2.1.1.224
- linezolid
-
oxazolidinone
-
5\'-deoxyadenosyl
-
thiopeptide
-
optra
-
linezolid-resistant
-
phenicols
-
cobalamin-dependent
-
phlopsa
-
pleuromutilins
-
nosiheptide
- 5'-deoxyadenosine
-
poxta
-
ribosome-targeting
-
cobiialamin
Reaction
2 S-adenosyl-L-methionine
+
Synonyms
antibiotic resistance protein, Ba Cfr, C8 adenine RNA methylase, Cd Cfr, Cfr, Cfr methyltransferase, Cfr rRNA methyltransferase, cfr(C), Cfr(E), cfr-like, Cfr-like protein, ClbA, ClbB, ClbC, EC 2.1.1.194, Ef Cfr, Pl Cfr, radical AdoMet rRNA methyltransferase, radical S-adenosylmethionine enzyme, radical S-adenosylmethionine methylase, radical-S-adenosyl-L-methionine enzyme, radical-SAM enzyme, radical-SAM rRNA methyltransferase, RS methylase
ECTree
2.1.1.224 23S rRNA (adenine2503-C8)-methyltransferaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 2.1.1.224 - 23S rRNA (adenine2503-C8)-methyltransferase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 S-adenosyl-L-methionine + 2-methyladenine2503 in 23S rRNA
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2,8-dimethyladenine2503 in 23S rRNA
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S-adenosylmethionine is both the methyl donor and the source of a 5'-deoxyadenosyl radical, which activates the substrate for methylation
incubation of Cfr with the wild-type 23S rRNA, already modified at the C2 position by the endogenous RlmN, provides 2,8-dimethyladenosine as the sole product
-
?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA
2 S-adenosyl-L-homocysteine + 2,8-dimethyladenine2503 in 23S rRNA
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-
-
?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [4Fe-4S] ferredoxin
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [4Fe-4S] ferredoxin
S-adenosyl-L-methionine + adenine2503 in 23S rRNA + reduced [2Fe-2S] ferredoxin
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + oxidized [2Fe-2S] ferredoxin
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-
-
?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA
-
verification of RNA methylation at A2503 in 23S rRNA by primer extension method
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?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA
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the enzyme methylates the 8 position of 23S rRNA residue A2503 to confer resistance to multiple antibiotic classes acting upon the large subunit of the bacterial ribosome
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-
?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA
-
in the presence of sodium dithionite reconstituted Cfr is both reducible and able to cleave S-adenosyl-L-methionine to 5'-deoxyadeonsine, DOA
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-
?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA
-
-
verification of RNA methylation at A2503 in 23S rRNA by primer extension method
-
?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA
-
-
verification of RNA methylation at A2503 in 23S rRNA by primer extension method
-
?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA
-
verification of RNA methylation at A2503 in 23S rRNA by primer extension method
-
?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA
-
verification of RNA methylation at A2503 in 23S rRNA by primer extension method
-
?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA
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Cfr is an plasmid-acquired methyltransferase that protects cells from the action of antibiotics
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-
?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA
-
S-adenosylmethionine is both the methyl donor and the source of a 5'-deoxyadenosyl radical, which activates the substrate for methylation. The enzyme can utilize protein-free 23S rRNA as a substrate, but not the fully assembled large ribosomal subunit, suggesting that the methylations take place during the assembly of the ribosome. The key recognition elements in the 23S rRNA are helices 90-92 and the adjacent single stranded RNA that encompasses A2503
identification of the reaction products as 8-methyladenine2503, and 2,8-dimethyladenine2503
-
?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA
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the newly introduced methyl group is assembled from an S-adenosyl-L-methionine (SAM)-derived methylene fragment and a hydrogen atom that had migrated from the substrate amidine carbon. Rather than activating the adenosine nucleotide of the substrate by hydrogen atom abstraction from an amidine carbon, the 5'-deoxyadenosyl radical abstracts hydrogen from the second equivalent of SAM to form the SAM-derived radical cation. This species, or its corresponding sulfur ylide, subsequently adds into the substrate, initiating hydride shift and S-adenosylhomocysteine elimination to complete the formation of the methyl group
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-
?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA
-
-
-
?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA
-
-
-
-
?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA
-
-
-
-
?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin
-
-
-
?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin
-
-
-
?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin
-
-
-
-
?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin
-
-
-
?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin
-
-
-
-
?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin
-
-
-
?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin
-
-
-
?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin
-
-
-
-
?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin
-
-
-
-
?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin
-
-
-
?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin
-
-
-
?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin
-
-
-
-
?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin
-
-
-
?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin
-
-
-
?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin
Paenibacillus lautus Y412MC10
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-
-
?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin
-
-
-
?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin
-
-
-
-
?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [4Fe-4S] ferredoxin
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [4Fe-4S] ferredoxin
-
-
-
?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [4Fe-4S] ferredoxin
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [4Fe-4S] ferredoxin
-
-
-
?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [4Fe-4S] ferredoxin
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [4Fe-4S] ferredoxin
-
-
-
-
?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [4Fe-4S] ferredoxin
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [4Fe-4S] ferredoxin
-
-
-
?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [4Fe-4S] ferredoxin
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [4Fe-4S] ferredoxin
-
enzyme Cfr consumes two AdoMet equivalents per reaction cycle to support both methyl transfer to Cfr Cys338 (AdoMet1, step 1) and subsequently generation of the 59dA. radical (AdoMet2, step2)
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-
?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [4Fe-4S] ferredoxin
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [4Fe-4S] ferredoxin
two S-adenosyl-L-methionine molecules serve as the cofactor by providing the 5'-deoxyadenosyl radical for substrate activation and the methyl
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?
additional information
?
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kinetic analysis of methylation of a 155mer rRNA substrate by Cfr enzymes under limiting and under excess substrate conditions initiated with a protein-based reductant, substrate sequence, overview
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additional information
?
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kinetic analysis of methylation of a 155mer rRNA substrate by Cfr enzymes under limiting and under excess substrate conditions initiated with a protein-based reductant, substrate sequence, overview
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additional information
?
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in vitro assays with Escherichia coli RNA
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additional information
?
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kinetic analysis of methylation of a 155mer rRNA substrate by Cfr enzymes under limiting and under excess substrate conditions initiated with a protein-based reductant, substrate sequence, overview
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additional information
?
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in vitro assays with Escherichia coli RNA
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additional information
?
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kinetic analysis of methylation of a 155mer rRNA substrate by Cfr enzymes under limiting and under excess substrate conditions initiated with a protein-based reductant, substrate sequence, overview
-
-
-
additional information
?
-
kinetic analysis of methylation of a 155mer rRNA substrate by Cfr enzymes under limiting and under excess substrate conditions initiated with a protein-based reductant, substrate sequence, overview
-
-
-
additional information
?
-
kinetic analysis of methylation of a 155mer rRNA substrate by Cfr enzymes under limiting and under excess substrate conditions initiated with a protein-based reductant, substrate sequence, overview
-
-
-
additional information
?
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Cfr confers a phenotype with resistance to phenicols, lincosamides, oxazolidinones, pleuromutilins, and streptogramin A antibiotics. Methylation of position 8 is the dominant antibiotic resistance determinant, but indigenous modification at position 2 also contributes to low-level resistance
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?
additional information
?
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Cfr methylates A2503 of 23S rRNA at C8 and C2, while RlmN only performs a C2 methylation using the same mechanism of function
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additional information
?
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kinetic analysis of methylation of a 155mer rRNA substrate by Cfr enzymes under limiting and under excess substrate conditions initiated with a protein-based reductant, substrate sequence, overview
-
-
-
additional information
?
-
Paenibacillus lautus Y412MC10
kinetic analysis of methylation of a 155mer rRNA substrate by Cfr enzymes under limiting and under excess substrate conditions initiated with a protein-based reductant, substrate sequence, overview
-
-
-
additional information
?
-
-
enzyme Cfr methylates adenosine 2503 of the 23S rRNA in the peptidyltransferase centre (P-site) of the bacterial ribosome. In wild-type Cfr, where Cys338 is methylated, S-adenosyl-L-methionine binding leads to rapid oxidation of the [4Fe-4S] cluster and production of 5'-deoxyadenosine
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?
additional information
?
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methylation at C8 is similar to that at C2, cf. EC 2.1.1.192
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?
additional information
?
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the enzyme employs a [4Fe-4S] cluster to supply the requisite electron for reductive cleavage of SAM, usually to L-methionine and a 5'-deoxyadenosyl 5'-radical. SAM is the source of both the 5'-deoxyadenosyl 5'-radical and the appended methyl group
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