Information on EC 2.1.1.192 - 23S rRNA (adenine2503-C2)-methyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.1.1.192
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RECOMMENDED NAME
GeneOntology No.
23S rRNA (adenine2503-C2)-methyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine2503 in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin
show the reaction diagram
2 S-adenosyl-L-methionine + adenine37 in tRNA + 2 reduced [2Fe-2S] ferredoxin = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine37 in tRNA + 2 oxidized [2Fe-2S] ferredoxin
show the reaction diagram
(2)
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:23S rRNA (adenine2503-C2)-methyltransferase
Contains an [4Fe-4S] cluster [2]. This enzyme is a member of the 'AdoMet radical' (radical SAM) family. S-Adenosyl-L-methionine acts as both a radical generator and as the source of the appended methyl group. RlmN first transfers an CH2 group to a conserved cysteine (Cys355 in Escherichia coli) [6], the generated radical from a second S-adenosyl-L-methionine then attacks the methyl group, exctracting a hydrogen. The formed radical forms a covalent intermediate with the adenine group of the tRNA [9]. RlmN is an endogenous enzyme used by the cell to refine functions of the ribosome in protein synthesis [2]. The enzyme methylates adenosine by a radical mechanism with CH2 from the S-adenosyl-L-methionine and retention of the hydrogen at C-2 of adenosine2503 of 23S rRNA. It will also methylate 8-methyladenosine2503 of 23S rRNA. cf. EC 2.1.1.224 [23S rRNA (adenine2503-C8)-methyltransferase].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
subsp. subtilis, gene rlmN
UniProt
Manually annotated by BRENDA team
subsp. subtilis, gene rlmN
UniProt
Manually annotated by BRENDA team
; contains the characteristic cysteine-rich CX3CX2C motif
SwissProt
Manually annotated by BRENDA team
gene rlmN
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine2503 in 23S rRNA
show the reaction diagram
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine2503 in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin
show the reaction diagram
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [4Fe-4S] ferredoxin
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine2503 in 23S rRNA + 2 oxidized [4Fe-4S] ferredoxin
show the reaction diagram
S-adenosyl-L-methionine + adenine2503 in 23S rRNA
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine2503 in 23S rRNA
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine2503 in 23S rRNA
show the reaction diagram
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine2503 in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin
show the reaction diagram
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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 + 2-methyladenine2503 in 23S rRNA + 2 oxidized [4Fe-4S] ferredoxin
show the reaction diagram
S-adenosyl-L-methionine + adenine2503 in 23S rRNA
S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine2503 in 23S rRNA
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ferredoxin
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S-adenosyl-L-methionine
[4Fe-4S]-center
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
the enzyme requires an intact [4Fe-S] cluster for catalysis
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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energy profile and thermodynamics, overview
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
mutant C118A, hanging drop vapor diffusion method, using 7.5% (w/v) PEG 6000, 0.1 M HEPES, pH 7.5, and 5% (v/v) 2-methyl-2,4-pentanediol as the precipitant
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
C-terminally His6-tagged wild-type enzyme and mutant enzymes C125A, C129A and C132A
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed as C-terminally His6-tagged enzyme, wild-type and mutant enzymes C125A, C129A and C132A
expressed in Escherichia coli Rosetta2(DE3)pLysS cells
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gene rlmN, sequence comparisons and phylogenetic analysis, primer extension analysis, cloning and expression in Escherichia coli strains TOP10 and AS19
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C118A
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inactive
C118S
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inactive
E105A
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the mutant shows wild type activity
C125A
inactive mutant enzyme
C129A
inactive mutant enzyme
C132A
inactive mutant enzyme
C338A
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the mutant binds S-adenosyl-L-methionine with wild type affinity, while oxidation of the [4Fe-4S] cluster is not observed
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