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Literature summary for 2.1.1.204 extracted from

  • Elhardt, W.; Shanmugam, R.; Jurkowski, T.P.; Jeltsch, A.
    Somatic cancer mutations in the DNMT2 tRNA methyltransferase alter its catalytic properties (2015), Biochimie, 112, 66-72.
    View publication on PubMed
Search for more literature for 2.1.1.204

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Homo sapiens

Protein Variants

Protein Variants Comment Organism
D217H site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme Homo sapiens
D226Y site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme Homo sapiens
D255Y site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme Homo sapiens
E185K site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme Homo sapiens
E202Q site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme Homo sapiens
E317G site-directed mutagenesi, the mutant shows activity similar to the wild-type enzyme Homo sapiens
E63K site-directed mutagenesis, the mutation causes a twofold increase in activity compared to the wild-type enzyme Homo sapiens
G155S site-directed mutagenesis, the mutation causes an over fourfold decrease in activity compared to the wild-type enzyme Homo sapiens
G155V site-directed mutagenesis, almost inactive mutant Homo sapiens
L257V site-directed mutagenesis, the mutation causes an over fourfold decrease in activity compared to the wild-type enzyme Homo sapiens
M72I site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme Homo sapiens
N264S site-directed mutagenesi, the mutant shows activity similar to the wild-type enzyme Homo sapiens
R371H site-directed mutagenesis, almost inactive mutant Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine + cytosine38 in tRNAAsp Homo sapiens
-
 S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
additional information Dnmt2 is consistently upregulated in hundreds of tumor samples Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + cytosine38 in tRNAAsp
-
 Homo sapiens S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNAAsp
-
 ?

Synonyms

Synonyms Comment Organism
Dnmt2
-
 Homo sapiens
TRDMT1
-
 Homo sapiens
tRNA-aspartic acid methyltransferase 1
-
 Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Homo sapiens

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine
-
 Homo sapiens

General Information

General Information Comment Organism
evolution the enzyme is a highly conserved cytosine-C5 methyltransferase that introduces the C38 methylation of tRNA-Asp in many species, including lower eukaryotes, plants, insects and humans Homo sapiens
physiological function The DNMT2 protein methylates C38 of tRNA-Asp and it has a role in cellular physiology and stress response and its expression levels are altered in cancer tissues Homo sapiens