BRENDA - Enzyme Database show
show all sequences of 2.1.1.264

Base methylations in the double-stranded RNA by a fused methyltransferase bearing unwinding activity

Kimura, S.; Ikeuchi, Y.; Kitahara, K.; Sakaguchi, Y.; Suzuki, T.; Suzuki, T.; Nucleic Acids Res. 40, 4071-4085 (2012)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene rlmK, expression in Escherichia coli DELTArlmKL mutant
Neisseria meningitidis
gene rlmL, renamed rlmKL, encodes a fused methyltransferase responsible for forming both m7G2069 and m2G2445
Escherichia coli
Engineering
Amino acid exchange
Commentary
Organism
D195A
site-directed mutagenesis, the mutation does not affect the methylation activity
Escherichia coli
D568A
site-directed mutagenesis, the D568A mutation in the C-terminal domain does not rescue m7G2069 formation, but m2G2445 is efficiently formed in this mutant
Escherichia coli
D597A
site-directed mutagenesis, the mutation does not affect the methylation activity
Escherichia coli
N309A
site-directed mutagenesis, the N309A mutation in the NTD impairs m2G2445 formation, but rescues m7G2069 formation
Escherichia coli
N397A
site-directed mutaagenesis, the N397A mutant exhibits no m2G2445 formation but rescues m7G2069 formation
Escherichia coli
R530A
site-directed mutagenesis, the mutation does not affect the methylation activity
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Escherichia coli
the enzyme also catalyzes the N2-methylation of guanine2445 in 23S rRNA, RlmL activity, reaction of EC 2.1.1.173
?
-
-
-
S-adenosyl-L-methionine + guanine2069 in 23S rRNA
Escherichia coli
RlmK activity in helix 74 of Escherichia coli 23S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA
-
-
?
S-adenosyl-L-methionine + guanine2069 in 23S rRNA
Neisseria meningitidis
RlmK activity in helix 74 of Escherichia coli 23S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA
-
-
?
S-adenosyl-L-methionine + guanine2069 in 23S rRNA
Neisseria meningitidis MC58
RlmK activity in helix 74 of Escherichia coli 23S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
gene rlmL, renamed rlmKL
-
Neisseria meningitidis
Q9JYY8
gene rlmK
-
Neisseria meningitidis MC58
Q9JYY8
gene rlmK
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
the enzyme also catalyzes the N2-methylation of guanine2445 in 23S rRNA, RlmL activity, reaction of EC 2.1.1.173
720598
Escherichia coli
?
-
-
-
-
S-adenosyl-L-methionine + guanine2069 in 23S rRNA
RlmK activity in helix 74 of Escherichia coli 23S rRNA
720598
Escherichia coli
S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA
-
-
-
?
S-adenosyl-L-methionine + guanine2069 in 23S rRNA
RlmK activity in helix 74 of Escherichia coli 23S rRNA
720598
Neisseria meningitidis
S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA
-
-
-
?
S-adenosyl-L-methionine + guanine2069 in 23S rRNA
RlmK activity in helix 74 of Escherichia coli 23S rRNA
720598
Neisseria meningitidis MC58
S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA
-
-
-
?
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
assay at
Escherichia coli
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Escherichia coli
Cofactor
Cofactor
Commentary
Organism
Structure
S-adenosyl-L-methionine
-
Escherichia coli
Cloned(Commentary) (protein specific)
Commentary
Organism
gene rlmL, renamed rlmKL, encodes a fused methyltransferase responsible for forming both m7G2069 and m2G2445
Escherichia coli
gene rlmK, expression in Escherichia coli DELTArlmKL mutant
Neisseria meningitidis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
S-adenosyl-L-methionine
-
Escherichia coli
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
D195A
site-directed mutagenesis, the mutation does not affect the methylation activity
Escherichia coli
D568A
site-directed mutagenesis, the D568A mutation in the C-terminal domain does not rescue m7G2069 formation, but m2G2445 is efficiently formed in this mutant
Escherichia coli
D597A
site-directed mutagenesis, the mutation does not affect the methylation activity
Escherichia coli
N309A
site-directed mutagenesis, the N309A mutation in the NTD impairs m2G2445 formation, but rescues m7G2069 formation
Escherichia coli
N397A
site-directed mutaagenesis, the N397A mutant exhibits no m2G2445 formation but rescues m7G2069 formation
Escherichia coli
R530A
site-directed mutagenesis, the mutation does not affect the methylation activity
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Escherichia coli
the enzyme also catalyzes the N2-methylation of guanine2445 in 23S rRNA, RlmL activity, reaction of EC 2.1.1.173
?
-
-
-
S-adenosyl-L-methionine + guanine2069 in 23S rRNA
Escherichia coli
RlmK activity in helix 74 of Escherichia coli 23S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA
-
-
?
S-adenosyl-L-methionine + guanine2069 in 23S rRNA
Neisseria meningitidis
RlmK activity in helix 74 of Escherichia coli 23S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA
-
-
?
S-adenosyl-L-methionine + guanine2069 in 23S rRNA
Neisseria meningitidis MC58
RlmK activity in helix 74 of Escherichia coli 23S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
the enzyme also catalyzes the N2-methylation of guanine2445 in 23S rRNA, RlmL activity, reaction of EC 2.1.1.173
720598
Escherichia coli
?
-
-
-
-
S-adenosyl-L-methionine + guanine2069 in 23S rRNA
RlmK activity in helix 74 of Escherichia coli 23S rRNA
720598
Escherichia coli
S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA
-
-
-
?
S-adenosyl-L-methionine + guanine2069 in 23S rRNA
RlmK activity in helix 74 of Escherichia coli 23S rRNA
720598
Neisseria meningitidis
S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA
-
-
-
?
S-adenosyl-L-methionine + guanine2069 in 23S rRNA
RlmK activity in helix 74 of Escherichia coli 23S rRNA
720598
Neisseria meningitidis MC58
S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA
-
-
-
?
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
assay at
Escherichia coli
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Escherichia coli
General Information
General Information
Commentary
Organism
malfunction
Neisseria meningitidis rlmL and rlmK homologues rescue m2G2445 and m7G2069 formation, respectively, in the Escherichia coli DELTArlmKL strain
Escherichia coli
malfunction
Neisseria meningitidis rlmL and rlmK homologues rescue m2G2445 and m7G2069 formation, respectively, in the Escherichia coli DELTArlmKL strain, overview
Neisseria meningitidis
physiological function
rlmKL encodes a fused methyltransferase responsible for forming both m7G2069 and m2G2445, the N-terminal RlmL activity for m2G2445 formation is significantly enhanced by the C-terminal RlmK. RlmKL has an unwinding activity of Helix 74, facilitating cooperative methylations of m7G2069 and m2G2445 during biogenesis of 50S subunit. For unwinding single-stranded RNA is a good substrate for RlmKL, substrate speccificity, overview. RlmKL is involved in the efficient assembly of 50S subunit in a mutant strain lacking an RNA helicase deaD
Escherichia coli
General Information (protein specific)
General Information
Commentary
Organism
malfunction
Neisseria meningitidis rlmL and rlmK homologues rescue m2G2445 and m7G2069 formation, respectively, in the Escherichia coli DELTArlmKL strain
Escherichia coli
malfunction
Neisseria meningitidis rlmL and rlmK homologues rescue m2G2445 and m7G2069 formation, respectively, in the Escherichia coli DELTArlmKL strain, overview
Neisseria meningitidis
physiological function
rlmKL encodes a fused methyltransferase responsible for forming both m7G2069 and m2G2445, the N-terminal RlmL activity for m2G2445 formation is significantly enhanced by the C-terminal RlmK. RlmKL has an unwinding activity of Helix 74, facilitating cooperative methylations of m7G2069 and m2G2445 during biogenesis of 50S subunit. For unwinding single-stranded RNA is a good substrate for RlmKL, substrate speccificity, overview. RlmKL is involved in the efficient assembly of 50S subunit in a mutant strain lacking an RNA helicase deaD
Escherichia coli
Other publictions for EC 2.1.1.264
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
720987
Kita
Crystal structure of a putativ ...
Staphylococcus aureus
Protein Pept. Lett.
20
530-537
2013
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1
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720598
Kimura
Base methylations in the doubl ...
Escherichia coli, Neisseria meningitidis, Neisseria meningitidis MC58
Nucleic Acids Res.
40
4071-4085
2012
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2
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6
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4
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3
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4
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1
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1
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3
3
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720601
Wang
Structure of the bifunctional ...
Escherichia coli, Escherichia coli BW25113, Streptococcus mutans
Nucleic Acids Res.
40
5138-5148
2012
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2
2
1
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32
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1
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11
2
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3
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