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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

Reaction

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

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 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.224 23S rRNA (adenine2503-C8)-methyltransferase

Engineering

Engineering on EC 2.1.1.224 - 23S rRNA (adenine2503-C8)-methyltransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C105A
-
mutation eliminates the resistance to both florfenicol and tiamulin
C110A
-
mutation does not affect Cfr activity
C112A
C116A
C119A
C338A
-
mutation eliminates the resistance to both florfenicol and tiamulin
E91A
-
mutation eliminates the resistance to both florfenicol and tiamulin
F118A
-
mutation eliminates the resistance to both florfenicol and tiamulin
H214A
-
moderately decreased resistance to both florfenicol and tiamulin
Q28A
-
mutation eliminates the resistance to both florfenicol and tiamulin
R25A
-
mutation lowers the resistance to both florfenicol and tiamulin considerably
S189A
-
mutation lowers the resistance to both florfenicol and tiamulin considerably
S212A
-
mutation eliminates the resistance to both florfenicol and tiamulin
C113A
no significant reduction in activity
C115A
mutation of the cysteines in the presumed radical S-adenosyl-L-methionine motif CxxxCxxC abolishes Cfr activity
C119A
mutation of the cysteines in the presumed radical S-adenosyl-L-methionine motif CxxxCxxC abolishes Cfr activity
C122A
mutation of the cysteines in the presumed radical S-adenosyl-L-methionine motif CxxxCxxC abolishes Cfr activity
C338A
the mutant binds S-adenosyl-L-methionine with wild type affinity, while oxidation of the [4Fe-4S] cluster is not observed
C119A
-
site-directed mutagenesis, the mutant Cfr is inactive, and mutant cells show no resistance against antibiotics
C338A
-
site-directed mutagenesis, Cys338Ala Cfr binds S-adenosyl-L-methionine with equivalent affinity, oxidation of the [4Fe-4S] cluster is not observed
C119A
-
site-directed mutagenesis, the mutant Cfr is inactive, and mutant cells show no resistance against antibiotics
-
additional information