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EC Tree
IUBMB Comments This enzyme specifically adds the terminal methyl group of 5-[(methylamino)methyl]-2-thiouridylate.
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
trna 5-methylaminomethyl-2-thiouridylate methyltransferase, 5-methylaminomethyl-2-thiouridylate methyltransferase, 5-methylaminomethyl-2-thiouridylate-methyltransferase,
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5-methylaminomethyl-2-thiouridylate methyltransferase
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5-methylaminomethyl-2-thiouridylate-methyltransferase
methylaminomethyl-2-thiouridylate-methyltransferase
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methyltransferase, transfer ribonucleate 5-methylaminomethyl-2-thiouridylate 5-
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S-adenosyl-L-methionine:tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase
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transfer ribonucleate 5-methylaminomethyl-2-thiouridylate 5-methyltransferase
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tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase
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tRNA 5-methylaminomethyl-2-thiouridylate 5'-methyltransferase
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tRNA 5-methylaminomethyl-2-thiouridylate methyltransferase
5-methylaminomethyl-2-thiouridylate-methyltransferase
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5-methylaminomethyl-2-thiouridylate-methyltransferase
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TRMU
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tRNA 5-methylaminomethyl-2-thiouridylate methyltransferase
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tRNA 5-methylaminomethyl-2-thiouridylate methyltransferase
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S-adenosyl-L-methionine + 5-aminomehtyl-2-thiouridine34 in tRNALys = S-adenosyl-L-homocysteine + 5-methylaminomehtyl-2-thiouridine34 in tRNALys
S-adenosyl-L-methionine + 5-aminomehtyl-2-thiouridine34 in tRNALys = S-adenosyl-L-homocysteine + 5-methylaminomehtyl-2-thiouridine34 in tRNALys
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S-adenosyl-L-methionine + 5-aminomehtyl-2-thiouridine34 in tRNALys = S-adenosyl-L-homocysteine + 5-methylaminomehtyl-2-thiouridine34 in tRNALys
mechanismn
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methyl group transfer
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S-adenosyl-L-methionine:tRNA 5-(aminomethyl)-2-thiouridylate N-methyltransferase
This enzyme specifically adds the terminal methyl group of 5-[(methylamino)methyl]-2-thiouridylate.
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S-adenosyl-L-methionine + 5-aminomethyl-2-thiouridine in tRNA
S-adenosyl-L-homocysteine + 5-methylaminomethyl-2-thiouridylate in tRNA
S-adenosyl-L-methionine + tRNA containing 5-aminomethyl-2-thiouridine
S-adenosyl-L-homocysteine + tRNA containing 5-methylaminomethyl-2-thiouridylate
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additional information
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the enzyme exhibits two activities: enzyme from trmC1 mutant reacts with 5-carboxymethylaminomethyl-2-thiouridine to form 5-aminomethyl-2-thiouridine without S-adenosyl-L-methionine, enzyme from trmC2 mutant methylates 5-aminomethyl-2-thiouridine in the presence of S-adenosyl-L-methionine
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S-adenosyl-L-methionine + 5-aminomethyl-2-thiouridine in tRNA
S-adenosyl-L-homocysteine + 5-methylaminomethyl-2-thiouridylate in tRNA
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S-adenosyl-L-methionine + 5-aminomethyl-2-thiouridine in tRNA
S-adenosyl-L-homocysteine + 5-methylaminomethyl-2-thiouridylate in tRNA
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tRNA from E. coli mutants
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S-adenosyl-L-methionine + 5-aminomethyl-2-thiouridine in tRNA
S-adenosyl-L-homocysteine + 5-methylaminomethyl-2-thiouridylate in tRNA
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specific, methyl group acceptor is methyl deficient tRNAGlu from E. coli
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S-adenosyl-L-methionine + 5-aminomethyl-2-thiouridine in tRNA
S-adenosyl-L-homocysteine + 5-methylaminomethyl-2-thiouridylate in tRNA
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S-adenosyl-L-methionine + 5-aminomethyl-2-thiouridine in tRNA
S-adenosyl-L-homocysteine + 5-methylaminomethyl-2-thiouridylate in tRNA
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specific, methyl group acceptor is methyl deficient tRNAGlu from E. coli
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S-adenosyl-L-methionine + 5-aminomethyl-2-thiouridine in tRNA
S-adenosyl-L-homocysteine + 5-methylaminomethyl-2-thiouridylate in tRNA
enzyme plays a role in tRNA modification and protein synthesis, pivotal in the fidelity of the translational process
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S-adenosyl-L-methionine + 5-aminomethyl-2-thiouridine in tRNA
S-adenosyl-L-homocysteine + 5-methylaminomethyl-2-thiouridylate in tRNA
nucleotide modification at the wobble position 34 of anticodons
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S-adenosyl-L-methionine + 5-aminomethyl-2-thiouridine in tRNA
S-adenosyl-L-homocysteine + 5-methylaminomethyl-2-thiouridylate in tRNA
S-adenosyl-L-methionine + 5-aminomethyl-2-thiouridine in tRNA
S-adenosyl-L-homocysteine + 5-methylaminomethyl-2-thiouridylate in tRNA
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S-adenosyl-L-methionine + 5-aminomethyl-2-thiouridine in tRNA
S-adenosyl-L-homocysteine + 5-methylaminomethyl-2-thiouridylate in tRNA
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S-adenosyl-L-methionine + 5-aminomethyl-2-thiouridine in tRNA
S-adenosyl-L-homocysteine + 5-methylaminomethyl-2-thiouridylate in tRNA
enzyme plays a role in tRNA modification and protein synthesis, pivotal in the fidelity of the translational process
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NaCl
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mutant trmC1: 100 mM, mutant trmC2: 200 mM
p-chloromercuribenzoate
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additional information
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no inhibition by putrescine or spermidine
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additional information
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no activation by putrescine or spermidine
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Liver Failure
Hepatic Copper Accumulation: A Novel Feature in Transient Infantile Liver Failure Due to TRMU Mutations?
Liver Failure
Reversible infantile mitochondrial diseases.
Liver Failure, Acute
Hepatic Copper Accumulation: A Novel Feature in Transient Infantile Liver Failure Due to TRMU Mutations?
Liver Failure, Acute
Leigh syndrome associated with TRMU gene mutations.
Mitochondrial Diseases
Altered 2-thiouridylation impairs mitochondrial translation in reversible infantile respiratory chain deficiency.
Mitochondrial Diseases
Reversible infantile mitochondrial diseases.
Mitochondrial Myopathies
Reversible infantile mitochondrial diseases.
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1.23
tRNA containing 5-aminomethyl-2-thiouridine
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8.7
amino acid sequence calculation
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B
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B
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K12 strain pTH32/1100, harbouring multi-copy plasmid
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SwissProt
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gene trmU
SwissProt
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low level
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abundantly expressed in tissues with high metabolic rates
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low level
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low level
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moderately expressed
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abundantly expressed in tissues with high metabolic rates
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moderately expressed
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moderately expressed
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low level
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moderately expressed
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abundantly expressed in tissues with high metabolic rates
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low level
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additional information
the trmU gene is expressed in various tissues, but abundantly in tissues with high metabolic rates
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additional information
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the trmU gene is expressed in various tissues, but abundantly in tissues with high metabolic rates
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localizes exclusively to mitochondria, even when overexpressed
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physiological function
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the enzyme regulates mitochondrial function and reactive oxygen species levels
malfunction
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cell death and apoptosis are significantly increased after neomycin injury in cells with downregulated enzyme expression
malfunction
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enzyme mutations cause transient infantile liver failure
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47240
x * 47240, amino acid sequence calculation
79000
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1 * 79000, SDS-PAGE
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monomer
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1 * 79000, SDS-PAGE
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x * 46000, SDS-PAGE
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x * 47240, amino acid sequence calculation
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G14S
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the mutation is associated with acute liver failure in infancy
G272D
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the mutation is associated with acute liver failure in infancy
L233F/A10S
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the mutation is associated with acute liver failure in infancy
M1K
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the mutation is associated with acute liver failure in infancy
V279M
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the mutation is associated with acute liver failure in infancy
Y77H
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the mutation is associated with acute liver failure in infancy
A10S
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the mutation is associated with acute liver failure in infancy
A10S
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the mutation alters the structure and function of the enzyme, thereby causing mitochondrial dysfunction, and interacts with 12S rRNA 1555A->G mutation to cause deafness. The mutation causes marked decreases in 2-thiouridine modification of U34 of tRNALys (48% decrease), tRNAGlu (38% decrease) and tRNAGln (50% decrease). However, the mutation mildly increases the aminoacylated efficiency of tRNA
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45.9
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melting temperature of the mutant enzyme A10S
49.1
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melting temperature of the wild type enzyme
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affinity chromatography
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cloning and mapping of trmC gene
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gene trmU, DNA and amino acid sequence determination and analysis, expression in NIH3T3 cells mitochondria as N-terminal GFP-fusion protein
TRMU-GFP fusion protein transfected into 143B cell line
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enzyme expression is significantly decreased after 24 h neomycin treatment
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medicine
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the enzyme is a target for the prevention of aminoglycoside-induced hair cell death
additional information
putative nuclear modifier gene TRMU may modulate the phenotypic manifestation of the deafness-associated mitochondrial 12S rRNA mutations
additional information
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putative nuclear modifier gene TRMU may modulate the phenotypic manifestation of the deafness-associated mitochondrial 12S rRNA mutations
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Taya, Y.; Nishimura, S.
Biosynthesis of 5-methylaminomethyl-2-thiouridylate. I. Isolation of a new tRNA-methylase specific for 5-methylaminomethyl-2-thiouridylate
Biochem. Biophys. Res. Commun.
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1062-1068
1973
Escherichia coli, Escherichia coli B / ATCC 11303
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Hagervall, T.G.; Edmonds, C.G.; McCloskey, J.A.; Bjrk, G.R.
Transfer RNA(5-methylaminomethyl-2-thiouridine)-methyltransferase from Escherichia coli K-12 has two enzymatic activities
J. Biol. Chem.
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8488-8495
1987
Escherichia coli
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Hagervall, T.G.; Bjrk, G.R.
Genetic mapping and cloning of the gene (trmC) responsible for the synthesis of tRNA (mnm5s2U)methyltransferase in Escherichia coli K12
Mol. Gen. Genet.
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201-207
1984
Escherichia coli
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Yan, Q.; Guan, M.X.
Identification and characterization of mouse TRMU gene encoding the mitochondrial 5-methylaminomethyl-2-thiouridylate-methyltransferase
Biochim. Biophys. Acta
1676
119-126
2004
Mus musculus (Q9DAT5), Mus musculus
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Yan, Q.; Bykhovskaya, Y.; Li, R.; Mengesha, E.; Shohat, M.; Estivill, X.; Fischel-Ghodsian, N.; Guan, M.X.
Human TRMU encoding the mitochondrial 5-methylaminomethyl-2-thiouridylate-methyltransferase is a putative nuclear modifier gene for the phenotypic expression of the deafness-associated 12S rRNA mutations
Biochem. Biophys. Res. Commun.
342
1130-1136
2006
Homo sapiens (O75648), Homo sapiens
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Zeharia, A.; Shaag, A.; Pappo, O.; Mager-Heckel, A.M.; Saada, A.; Beinat, M.; Karicheva, O.; Mandel, H.; Ofek, N.; Segel, R.; Marom, D.; Roetig, A.; Tarassov, I.; Elpeleg, O.
Acute infantile liver failure due to mutations in the TRMU gene
Am. J. Hum. Genet.
85
401-407
2009
Homo sapiens
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Meng, F.; Cang, X.; Peng, Y.; Li, R.; Zhang, Z.; Li, F.; Fan, Q.; Guan, A.S.; Fischel-Ghosian, N.; Zhao, X.; Guan, M.X.
Biochemical evidence for a nuclear modifier allele (A10S) in TRMU (methylaminomethyl-2-thiouridylate-methyltransferase) related to mitochondrial tRNA modification in the phenotypic manifestation of deafness-associated 12S rRNA mutation
J. Biol. Chem.
292
2881-2892
2017
Homo sapiens
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Grover, Z.; Lewindon, P.; Clousten, A.; Shaag, A.; Elpeleg, O.; Coman, D.
Hepatic copper accumulation a novel feature in transient infantile liver failure due to TRMU mutations?
JIMD Rep.
21
109-113
2015
Homo sapiens
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He, Z.; Sun, S.; Waqas, M.; Zhang, X.; Qian, F.; Cheng, C.; Zhang, M.; Zhang, S.; Wang, Y.; Tang, M.; Li, H.; Chai, R.
Reduced TRMU expression increases the sensitivity of hair-cell-like HEI-OC-1 cells to neomycin damage in vitro
Sci. Rep.
6
29621
2016
Mus musculus
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