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Literature summary for 6.1.1.2 extracted from

  • Guo, L.T.; Chen, X.L.; Zhao, B.T.; Shi, Y.; Li, W.; Xue, H.; Jin, Y.X.
    Human tryptophanyl-tRNA synthetase is switched to a tRNA-dependent mode for tryptophan activation by mutations at V85 and I311 (2007), Nucleic Acids Res., 35, 5934-5943.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.1.1.2

Cloned(Commentary)

Cloned (Comment) Organism
gene trpS, enzyme expression in Escherichia coli strain BL21 Homo sapiens

Protein Variants

Protein Variants Comment Organism
I311E mutation located at the appended beta1-beta2 hairpin and the AIDQ sequence of TrpRS that switch this enzyme to a tRNA-dependent mode in the tryptophan activation step Homo sapiens
I311V mutation located at the appended beta1-beta2 hairpin and the AIDQ sequence of TrpRS that switch this enzyme to a tRNA-dependent mode in the tryptophan activation step Homo sapiens
V85A mutation located at the appended beta1-beta2 hairpin and the AIDQ sequence of TrpRS that switch this enzyme to a tRNA-dependent mode in the tryptophan activation step, the mutant shows decreased, but visible tryptophan activation activity in the ATP-diphosphate exchange reaction Homo sapiens
V85A/V90A mutation located at the appended beta1-beta2 hairpin and the AIDQ sequence of TrpRS that switch this enzyme to a tRNA-dependent mode in the tryptophan activation step Homo sapiens
V85E mutation located at the appended beta1-beta2 hairpin and the AIDQ sequence of TrpRS that switch this enzyme to a tRNA-dependent mode in the tryptophan activation step Homo sapiens
V85K mutation located at the appended beta1-beta2 hairpin and the AIDQ sequence of TrpRS that switch this enzyme to a tRNA-dependent mode in the tryptophan activation step, the V85K mutant has barely detectable aminoacylation activity Homo sapiens
V85L mutation located at the appended beta1-beta2 hairpin and the AIDQ sequence of TrpRS that switch this enzyme to a tRNA-dependent mode in the tryptophan activation step, the V85L mutant is able to acylate bovine tRNATrp with very high effciency Homo sapiens
V85S mutation located at the appended beta1-beta2 hairpin and the AIDQ sequence of TrpRS that switch this enzyme to a tRNA-dependent mode in the tryptophan activation step, the mutant shows no activity in the ATP-diphosphate exchange reaction, but retains aminoacylation activity Homo sapiens
V90A mutation located at the appended beta1-beta2 hairpin and the AIDQ sequence of TrpRS that switch this enzyme to a tRNA-dependent mode in the tryptophan activation step, the mutant shows decreased, but visible tryptophan activation activity in the ATP-diphosphate exchange reaction, the V90 mutation enhances the hydrophobic interaction between V85 and I311 Homo sapiens
V90S mutation located at the appended beta1-beta2 hairpin and the AIDQ sequence of TrpRS that switch this enzyme to a tRNA-dependent mode in the tryptophan activation step, the mutant shows decreased, but visible tryptophan activation activity in the ATP-diphosphate exchange reaction, the V90 mutation enhances the hydrophobic interaction between V85 and I311 Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00029
-
 tRNATrp pH 7.5, 30°C, mutant V85K Homo sapiens
0.0013
-
 tRNATrp pH 7.5, 30°C, wild-type enzyme Homo sapiens
0.00141
-
 tRNATrp pH 7.5, 30°C, mutant V85A Homo sapiens
0.00184
-
 tRNATrp pH 7.5, 30°C, mutant V90A Homo sapiens
0.00214
-
 tRNATrp pH 7.5, 30°C, mutant V85S Homo sapiens
0.00223
-
 tRNATrp pH 7.5, 30°C, mutant V85A/V90A Homo sapiens
0.0052
-
 tRNATrp pH 7.5, 30°C, mutant V90S Homo sapiens
0.0085
-
 tRNATrp pH 7.5, 30°C, mutant V85E Homo sapiens
0.0248
-
 tRNATrp pH 7.5, 30°C, mutant V85L 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-tryptophan + tRNATrp Homo sapiens
-
 AMP + diphosphate + L-tryptophanyl-tRNATrp
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens P23381 gene trpS
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-tryptophan + tRNATrp
-
 Homo sapiens AMP + diphosphate + L-tryptophanyl-tRNATrp
-
 ?
ATP + L-tryptophan + tRNATrp bovine tRNATrp substrate, a two step reaction, the tryptophanyl-tRNA synthetase is a class I amino acid tRNA-synthetase, that catalyzes tryptophan activation in the absence of its cognate tRNA, cognate tRNA is not obligatory to catalyze amino acid activation, the integrated 3’ end of the tRNA is necessary to activate the ATP-diphosphate exchange reaction, overview Homo sapiens AMP + diphosphate + L-tryptophanyl-tRNATrp
-
 ?

Subunits

Subunits Comment Organism
More primary and tertiary structure of human TrpRS, overview Homo sapiens

Synonyms

Synonyms Comment Organism
TrpRS
-
 Homo sapiens
Tryptophanyl-tRNA synthetase
-
 Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0009
-
 tRNATrp pH 7.5, 30°C, mutant V85K Homo sapiens
0.02
-
 tRNATrp pH 7.5, 30°C, mutant V85E Homo sapiens
0.028
-
 tRNATrp pH 7.5, 30°C, mutant V85S Homo sapiens
0.047
-
 tRNATrp pH 7.5, 30°C, mutant V85A/V90A Homo sapiens
0.063
-
 tRNATrp pH 7.5, 30°C, mutant V90S Homo sapiens
0.48
-
 tRNATrp pH 7.5, 30°C, mutant V85A Homo sapiens
1.37
-
 tRNATrp pH 7.5, 30°C, wild-type enzyme Homo sapiens
1.39
-
 tRNATrp pH 7.5, 30°C, mutant V90A Homo sapiens
3.3
-
 tRNATrp pH 7.5, 30°C, mutant V85L Homo sapiens
5.11
-
 tRNATrp pH 7.5, 30°C, mutant V85L 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