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Literature summary for 6.1.1.10 extracted from

  • Yoo, T.H.; Tirrell, D.A.
    High-throughput screening for methionyl-tRNA synthetases that enable residue-specific incorporation of noncanonical amino acids into recombinant proteins in bacterial cells (2007), Angew. Chem., 46, 5340-5343.
    View publication on PubMed
Search for more literature for 6.1.1.10

Cloned(Commentary)

Cloned (Comment) Organism
gene metE, genetic library construction and expression, expression of His-tagged mutant enzymes in strains DH10B and in DH10B Met- Escherichia coli

Protein Variants

Protein Variants Comment Organism
A256X random mutagnesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme Escherichia coli
A256X random mutagenesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme Escherichia coli
H301L saturation mutagenesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme Escherichia coli
L13S saturation mutagenesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme Escherichia coli
M218A random mutagnesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme Escherichia coli
M218A random mutagenesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme Escherichia coli
M233I random mutagnesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme Escherichia coli
M233I random mutagenesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme Escherichia coli
M78L random mutagnesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme Escherichia coli
M78L random mutagenesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme Escherichia coli
M88F random mutagnesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme Escherichia coli
M88F random mutagenesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme Escherichia coli
additional information high-throughput screening for mutant enzymes that enable residue-specific incorporation of noncanonical amino acids into the recombinant mutant enzymes in the bacterial cells, overview Escherichia coli
P257X saturation mutagenesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme Escherichia coli
Y260L saturation mutagenesis, the mutant shows altered amino acid substrate binding compared to the wild-type enzyme Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-methionine + tRNAMet Escherichia coli
-
 AMP + diphosphate + L-methionyl-tRNAMet
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 gene metE
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged mutant enzymes from strain DH10B by nickel affinity chromatography Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-methionine + tRNAMet
-
 Escherichia coli AMP + diphosphate + L-methionyl-tRNAMet
-
 ?
ATP + L-methionine + tRNAMet residues L13, P257, Y260, and H301 are involved in the Met binding site Escherichia coli AMP + diphosphate + L-methionyl-tRNAMet
-
 ?

Synonyms

Synonyms Comment Organism
methionyl-tRNA synthetase
-
 Escherichia coli
MetRS
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Escherichia coli