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Literature summary for 2.1.2.9 extracted from

  • Sinha, A.; Koehrer, C.; Weber, M.H.; Masuda, I.; Mootha, V.K.; Hou, Y.M.; RajBhandary, U.L.
    Biochemical characterization of pathogenic mutations in human mitochondrial methionyl-tRNA formyltransferase (2014), J. Biol. Chem., 289, 32729-32741.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
A172L site-directed mutagenesis, the mutation causes a 6fold decrease in enzyme activity compared to wild-type, the Vmax/Km of the mutant is about 4fold lower than that of the wild-type enzyme Escherichia coli
A172S site-directed mutagenesis, the mutation does not significantly affect the enzyme activity Escherichia coli
A89L site-directed mutagenesis, the Vmax/Km of the mutant is about 144fold lower than that of the wild-type enzyme Escherichia coli
A89S site-directed mutagenesis, the mutation does not significantly affect the enzyme activity Escherichia coli
S125L naturally occurring mutation, the mutant has a 653fold lower activity compared to the wild-type Homo sapiens
S209L naturally occurring mutation, the mutant has a 36fold lower activity compared to the wild-type Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michaelis-Menten kinetics of wild-type and mutant enzymes Escherichia coli
additional information
-
additional information Michaelis-Menten kinetics of wild-type and mutant enzymes with human mitochondrial mt-tRNAMet and with Escherichia coli tRNA2fMet, overview Homo sapiens
0.00051
-
L-methionyl-tRNAfMet Escherichia coli tRNA2fMet, pH 7.6, 37°C, wild-type enzyme Escherichia coli
0.00107
-
L-methionyl-tRNAfMet Escherichia coli tRNA2fMet, pH 7.6, 37°C, mutant A172L Escherichia coli
0.00587
-
L-methionyl-tRNAfMet Escherichia coli tRNA2fMet, pH 7.6, 37°C, mutant A89L Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Homo sapiens 5739
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli
Mg2+ required Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
10-formyltetrahydrofolate + L-methionyl-tRNAfMet Escherichia coli
-
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet Homo sapiens
-
tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P23882
-
-
Homo sapiens Q96DP5
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
10-formyltetrahydrofolate + L-methionyl-tRNAfMet
-
Escherichia coli tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet
-
Homo sapiens tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet Escherichia coli tRNA2fMet Escherichia coli tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
?
10-formyltetrahydrofolate + L-methionyl-tRNAfMet human mt-tRNAMet Homo sapiens tetrahydrofolate + N-formylmethionyl-tRNAfMet
-
?

Synonyms

Synonyms Comment Organism
mitochondrial methionyl-tRNA formyltransferase
-
Escherichia coli
mitochondrial methionyl-tRNA formyltransferase
-
Homo sapiens
MTF
-
Escherichia coli
MTF
-
Homo sapiens

Temperature Optimum [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6
-
assay at Escherichia coli
7.6
-
assay at Homo sapiens

Cofactor

Cofactor Comment Organism Structure
10-formyltetrahydrofolate
-
Escherichia coli
10-formyltetrahydrofolate
-
Homo sapiens

General Information

General Information Comment Organism
malfunction mutations of conserved enzyme residues affect enzyme activity and lead to poor formylation of mitochondrial methionyl-tRNA and thereby reduced mitochondrial translation efficiency, causing Leigh syndrome Escherichia coli
malfunction mutations of conserved enzyme residues affect enzyme activity and lead to poor formylation of mitochondrial methionyl-tRNA and thereby reduced mitochondrial translation efficiency, causing Leigh syndrome Homo sapiens
physiological function N-formylation of initiator methionyl-tRNA (Met-tRNAMet) by methionyl-tRNA formyltransferase is important for translation initiation in bacteria, mitochondria, and chloroplasts Escherichia coli
physiological function N-formylation of initiator methionyl-tRNA (Met-tRNAMet) by methionyl-tRNA formyltransferase is important for translation initiation in bacteria, mitochondria, and chloroplasts Homo sapiens