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Literature summary for 6.1.1.4 extracted from

  • Tang, Y.; Wang, P.; Van Deventer, J.; Link, A.; Tirrell, D.
    Introduction of an aliphatic ketone into recombinant proteins in a bacterial strain that overexpresses an editing-impaired leucyl-tRNA synthetase (2009), ChemBioChem, 10, 2188-2190.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.1.1.4

Protein Variants

Protein Variants Comment Organism
T252Y mutant is unable to proofread amino acids with unbranched side chains, and enables insertion of a variety of noncanonical amino acids into recombinant proteins in place of leucine Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.018
-
 L-leucine mutant T252Y Escherichia coli
1.034
-
 L-didehydroleucine mutant T252Y Escherichia coli
2.245
-
 L-oxonorvaline mutant T252Y Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-didehydroleucine + tRNALeu reaction is catalyzed by mutant T252Y, not by wild-type Escherichia coli AMP + diphosphate + didehydroleucyl-tRNALeu
-
 ?
ATP + L-leucine + tRNALeu
-
 Escherichia coli AMP + diphosphate + L-leucyl-tRNALeu
-
 ?
ATP + L-oxonorvaline + tRNALeu reaction is catalyzed by mutant T252Y, not by wild-type Escherichia coli AMP + diphosphate + oxonorvalyl-tRNALeu
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.06
-
 L-oxonorvaline mutant T252Y Escherichia coli
1.08
-
 L-didehydroleucine mutant T252Y Escherichia coli
2.2
-
 L-leucine mutant T252Y Escherichia coli