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Literature summary for 6.1.1.10 extracted from

  • Kaminska, M.; Shalak, V.; Mirande, M.
    The appended C-domain of human methionyl-tRNA synthetase has a tRNA-sequestering function (2001), Biochemistry, 40, 14309-14316.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
elongation factor EF-1alpha activates, assists in dissociation of Met-tRNAMet from the enzyme, the aminoacylated tRNA is transfered from to the enzyme to the elongation factor Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
expression of the wild-type, and exchange mutant enzymes in Escherichia coli BL21(DE3), cloning and expression of the catalytic domain, amino acid residues A215-K823, and the C-terminal extension in Escherichia coli BL21(DE3) Homo sapiens

Protein Variants

Protein Variants Comment Organism
K860A site-directed mutagenesis, reduced activity Homo sapiens
K863A site-directed mutagenesis, reduced activity Homo sapiens
K866A site-directed mutagenesis, reduced activity Homo sapiens
K880A site-directed mutagenesis, altered kinetics Homo sapiens
R857A site-directed mutagenesis, reduced activity Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information dissociation constants for wild-type and mutant enzymes Homo sapiens
0.0022
-
tRNAMet C-terminal extension, pH 7.5, 25°C Homo sapiens
0.0033
-
tRNAMet mutant K863A, pH 7.5, 25°C Homo sapiens
0.0035
-
tRNAMet wild-type enzyme, pH 7.5, 25°C Homo sapiens
0.0039
-
tRNAMet wild-type enzyme in the multi-enzyme complex and mutant K866A, pH 7.5, 25°C Homo sapiens
0.0057
-
tRNAMet mutant R857A, pH 7.5, 25°C Homo sapiens
0.0163
-
tRNAMet mutant K880A, pH 7.5, 25°C Homo sapiens
0.0172
-
tRNAMet mutant K860A, pH 7.5, 25°C Homo sapiens
0.032
-
tRNAMet catalytic domain, pH 7.5, 25°C Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-methionine + tRNAMet Homo sapiens
-
AMP + diphosphate + L-methionyl-tRNAMet
-
r

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type enzyme, mutants and fragments from Escherichia coli Homo sapiens

Reaction

Reaction Comment Organism Reaction ID
ATP + L-methionine + tRNAMet = AMP + diphosphate + L-methionyl-tRNAMet mechanism, catalytic domain is formed by amino acid residues A215-K823 Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-methionine + tRNAMet
-
Homo sapiens AMP + diphosphate + L-methionyl-tRNAMet
-
r
ATP + L-methionine + tRNAMet the C-terminal ancillary RNA-binding domain is important for activity and has dual function provided by 2 structural motifs: 1. the helix-turn-helix HTH motif, which confers rate-limiting dissociation of the aminoaclyted tRNA from the enzyme, and 2. the KGKKKK lysine-rich cluster LRC, which is probably involved in accelerating the association step of deacylated tRNA Homo sapiens AMP + diphosphate + L-methionyl-tRNAMet
-
r

Synonyms

Synonyms Comment Organism
Methionine translase
-
Homo sapiens
Methionine--tRNA ligase
-
Homo sapiens
Methionyl tRNA synthetase
-
Homo sapiens
Methionyl-transfer ribonucleate synthetase
-
Homo sapiens
Methionyl-transfer ribonucleic acid synthetase
-
Homo sapiens
Methionyl-transfer RNA synthetase
-
Homo sapiens
MetRS
-
Homo sapiens
Synthetase, methionyl-transfer ribonucleate
-
Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.09
-
tRNAMet C-terminal extension, pH 7.5, 25°C Homo sapiens
0.15
-
tRNAMet wild-type enzyme, pH 7.5, 25°C Homo sapiens
0.22
-
tRNAMet mutant K863A, pH 7.5, 25°C Homo sapiens
0.23
-
tRNAMet mutant K866A, pH 7.5, 25°C Homo sapiens
0.46
-
tRNAMet wild-type enzyme in the multi-enzyme complex, pH 7.5, 25°C Homo sapiens
0.47
-
tRNAMet mutant R857A, pH 7.5, 25°C Homo sapiens
0.85
-
tRNAMet mutant K860A, pH 7.5, 25°C Homo sapiens
1.03
-
tRNAMet mutant K880A, pH 7.5, 25°C Homo sapiens
2.4
-
tRNAMet catalytic domain, pH 7.5, 25°C Homo sapiens
6.08
-
tRNAMet mutant K880A, pH 7.5, 25°C Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Homo sapiens

Cofactor

Cofactor Comment Organism Structure
ATP
-
Homo sapiens