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
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optra
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linezolid-resistant
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phenicols
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cobalamin-dependent
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phlopsa
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pleuromutilins
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nosiheptide
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5'-deoxyadenosine
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poxta
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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 + + 2 reduced [2Fe-2S] ferredoxin = + + + + 2 oxidized [2Fe-2S] ferredoxin
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
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Reaction
Reaction on EC 2.1.1.224 - 23S rRNA (adenine2503-C8)-methyltransferase
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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
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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
the enzyme catalyzes adenosine methylation by using a radical mechanism for substrate activation. The radical chemistry is enabled by the [4Fe-4S] cluster
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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
the methyl group is not transferred directly from S-adenosyl-L-methionine to the RNA. Reaction proceeds by a ping-pong mechanism involving intermediate methylation of a conserved cysteine residue
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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
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 [2Fe-2S] ferredoxin = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin
reaction mechanism modeling overview
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
the enzyme uses a mechanism involving radical S-adenosyl methionine to methylate RNA via an intermediate with a methylated cysteine in the enzyme and a transient cross-linking to the RNA