Information on EC 2.1.1.203 - tRNA (cytosine34-C5)-methyltransferase

Word Map on EC 2.1.1.203
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.1.1.203
-
RECOMMENDED NAME
GeneOntology No.
tRNA (cytosine34-C5)-methyltransferase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + cytosine34 in tRNA precursor = S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA precursor
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
tRNA methylation (yeast)
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:tRNA (cytosine34-C5)-methyltransferase
The human enzyme is specific for C5-methylation of cytosine34 in tRNA precursors. The intron in the human pre-tRNALeu(CAA) is indispensable for the C5-methylation of cytosine in the first position of the anticodon. It is not able to form 5-methylcytosine at positions 48 and 49 of human and yeast tRNA precursors [1].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
nonessential tRNA modifications by methyltransferases are evolutionarily conserved and have been reported to stabilize mature tRNA molecules and prevent rapid tRNA decay. The tRNA modifying enzymes, NSUN2 and METTL1, EC 2.1.1.33, are mammalian orthologues of yeast Trm4 and Trm8, which are required for protecting tRNA against tRNA decay
malfunction
metabolism
-
formation of a covalent complex between dual-cysteine RNA:m5C methyltransferases and methylated RNA provides a unique means by which metabolic factors can influence RNA. By controlling the degree of formation of the enzyme-RNA covalent complex, S-adenosyl-L-homocysteine and pH are likely to influence the extent of m5C formation and the rate of release of methylated RNA from RNA:m5C methyltransferases. Metabolite-induced covalent complexes could plausibly affect the processing and function of m5C-containing RNAs
physiological function
additional information
-
four active-site residues critical for Nsun2-mediated tRNA methylation are also required for the formation of the denaturant-resistant complexes with m5C-containing RNA
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + cytosine34 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA precursor
show the reaction diagram
specific modification of cytosine34 in the intron-containing yeast pre-tRNALeu(CAA)
-
-
?
S-adenosyl-L-methionine + cytosine34 in tRNA precursor
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA precursor
show the reaction diagram
S-adenosyl-L-methionine + microRNA 125b
S-adenosyl-L-homocysteine + ?
show the reaction diagram
-
the tRNA methyltransferase NSun2 methylates primary (pri-miR-125b), precursor (pre-miR-125b), and mature microRNA 125b (miR-125b) in vitro and in vivo
-
-
?
additional information
?
-
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
S-adenosyl-L-methionine + cytosine34 in tRNA
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA precursor
show the reaction diagram
Q08J23
specific modification of cytosine34 in the intron-containing yeast pre-tRNALeu(CAA)
-
-
?
S-adenosyl-L-methionine + cytosine34 in tRNA precursor
S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA precursor
show the reaction diagram
S-adenosyl-L-methionine + microRNA 125b
S-adenosyl-L-homocysteine + ?
show the reaction diagram
-
the tRNA methyltransferase NSun2 methylates primary (pri-miR-125b), precursor (pre-miR-125b), and mature microRNA 125b (miR-125b) in vitro and in vivo
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
required
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
assay at
37
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
simultaneous overexpression of NSUN2 and METTL1, EC 2.1.1.33, is widely observed among human cancers
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 86471, calculated from sequence
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
-
NSUN2 is phosphorylated at Ser139 by Aurora-B to inhibit its enzymatic activity during mitosis
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged NSun2 from Escherichia coli by nickel affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression of the human Trm4 (hTrm4) cDNA in yeast partially complements the lack of the endogenous Trm4p enzyme
expression of wild-type and mutant enzymes in HCC1954 cells and in COS7 cells
-
recombinant expression of His-tagged NSun2 in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G679R
-
site-directed mutaegensis, the mutation to arginine at this residue causes NSUN2 to fail to localize within the nucleolus
K190M
-
site-directed mutagenesis
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
this methyltransferase is a novel downstream Myctarget which mediates Myc-induced cell proliferation and growth. Therefore, the characterization of hTrm4 substrate specificity can be essential since this enzyme is a potential target for cancer therapies
pharmacology
-
enzymes NSUN2 and METTL1 are implicated in 5-fluorouracil sensitivity in HeLa cells. Interfering with methylation of tRNAs might provide a promising rationale to improve 5-fluorouracil chemotherapy of cancer