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Literature summary for 6.1.1.1 extracted from

  • Venkat, S.; Gregory, C.; Gan, Q.; Fan, C.
    Biochemical characterization of the lysine acetylation of tyrosyl-tRNA synthetase in Escherichia coli (2017), ChemBioChem, 18, 1928-1934 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.1.1.1

Cloned(Commentary)

Cloned (Comment) Organism
gene tyrS, recombinant expression of His6-tagged wild-type enzyme and site-specifically acetylated TyrRS variants in Escherichia coli strain BL21(DE3) cells Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information of recombinantly expressed site-specifically acetylated TyrRS variants, TyrRS-85AcK and -235AcK show dramatic decreases in activity. Variant TyrRS-238AcK has no detectable activity, while variants TyrRS-144AcK and -355AcK have similar activities compared to the wild-type TyrRS. TyrRS-85AcK has a fivefold increase in the KM value for ATP, indicating its role in ATP binding. TyrRS-235AcK has slightly changed KM values for both ATP and tyrosine but a 200fold decrease in catalytic efficiency, suggesting its role in catalysis Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00037
-
 tRNATyr pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant wild-type enzyme Escherichia coli
0.00042
-
 tRNATyr pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant lysine acetylated enzyme mutant 144AcK Escherichia coli
0.00043
-
 ATP pH 7.2, 37°C, Tyr activation activity, recombinant wild-type enzyme Escherichia coli
0.00045
-
 tRNATyr pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant lysine acetylated enzyme mutant 85AcK Escherichia coli
0.00045
-
 ATP pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 144AcK Escherichia coli
0.00048
-
 tRNATyr pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant lysine acetylated enzyme mutant 355AcK Escherichia coli
0.00049
-
 ATP pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 355AcK Escherichia coli
0.00071
-
 ATP pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 235AcK Escherichia coli
0.00223
-
 ATP pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 85AcK Escherichia coli
0.00669
-
 L-tyrosine pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 355AcK Escherichia coli
0.00678
-
 L-tyrosine pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 85AcK Escherichia coli
0.00713
-
 L-tyrosine pH 7.2, 37°C, Tyr activation activity, recombinant wild-type enzyme Escherichia coli
0.00728
-
 L-tyrosine pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 144AcK Escherichia coli
0.00845
-
 L-tyrosine pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 235AcK Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-tyrosine + tRNATyr Escherichia coli
-
 AMP + diphosphate + L-tyrosyl-tRNATyr
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AGJ9
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
acetylation tyrosyl-tRNA synthetase (TyrRS) in Escherichia coli is acetylated at multiple lysine residues. Acetylation at K85, K235, and K238 impairs the enzyme activity, by genetic-code-expansion strategy to site-specifically incorporate Nepsilonacetyl-l-lysine into selected positions of TyrRS for in vitro characterization. Lysine residue K355 is never acetylated. Most acetylated lysine residues in TyrRS are sensitive to the Escherichia coli deacetylase CobB but not YcgC, overview. Mapping of acetylated lysine residues on the crystal structure of TyrRS, PDB ID 1VBM Escherichia coli

Purification (Commentary)

Purification (Comment) Organism
recombinant His6-tagged wild-type enzyme and site-specifically acetylated TyrRS variants from Escherichia coli strain BL21(DE3) cells Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-tyrosine + tRNATyr
-
 Escherichia coli AMP + diphosphate + L-tyrosyl-tRNATyr
-
 ?

Synonyms

Synonyms Comment Organism
Tyrosyl-tRNA synthetase
-
 Escherichia coli
TyrRS
-
 Escherichia coli
tyrS
-
 Escherichia coli

Temperature Optimum [°C]

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

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.1
-
 ATP pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 235AcK Escherichia coli
0.1
-
 L-tyrosine pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 235AcK Escherichia coli
0.15
-
 tRNATyr pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant lysine acetylated enzyme mutant 85AcK Escherichia coli
1.09
-
 tRNATyr pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant lysine acetylated enzyme mutant 355AcK Escherichia coli
1.17
-
 tRNATyr pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant lysine acetylated enzyme mutant 144AcK Escherichia coli
1.32
-
 tRNATyr pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant wild-type enzyme Escherichia coli
2
-
 ATP pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 85AcK Escherichia coli
2
-
 L-tyrosine pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 85AcK Escherichia coli
11.9
-
 ATP pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 355AcK Escherichia coli
11.9
-
 L-tyrosine pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 355AcK Escherichia coli
12.3
-
 ATP pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 144AcK Escherichia coli
12.3
-
 L-tyrosine pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 144AcK Escherichia coli
14.2
-
 ATP pH 7.2, 37°C, Tyr activation activity, recombinant wild-type enzyme Escherichia coli
14.2
-
 L-tyrosine pH 7.2, 37°C, Tyr activation activity, recombinant wild-type enzyme Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
 assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Escherichia coli

Expression

Organism Comment Expression
Escherichia coli lysine acetylation can be a possible mechanism for modulating aminoacyl-tRNA synthetases enzyme activities, thus affecting translation down

General Information

General Information Comment Organism
evolution TyrRS is a member of class I aminoacyl-tRNA synthetases Escherichia coli
malfunction lysine acetylation can be a possible mechanism for modulating aminoacyl-tRNA synthetases enzyme activities, thus affecting translation. Of recombinantly expressed site-specifically acetylated TyrRS variants, TyrRS-85AcK and -235AcK show dramatic decreases in activity. Variant TyrRS-238AcK has no detectable activity, while variants TyrRS-144AcK and -355AcK have similar activities compared to the wild-type TyrRS. TyrRS-85AcK has a fivefold increase in the KM value for ATP, indicating its role in ATP binding. TyrRS-235AcK has slightly changed KM values for both ATP and tyrosine but a 200fold decrease in catalytic efficiency, suggesting its role in catalysis. K235 and K238 of TyrRS characterized in this study are the two lysine residues in the KMSKS motif. Kinetics for acetylated mutant variants, overview Escherichia coli
additional information lysine acetylation could be a possible mechanism for modulating aminoacyl-tRNA synthetases enzyme activities, thus affecting translation Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.33
-
 tRNATyr pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant lysine acetylated enzyme mutant 85AcK Escherichia coli
2.27
-
 tRNATyr pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant lysine acetylated enzyme mutant 355AcK Escherichia coli
2.78
-
 tRNATyr pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant lysine acetylated enzyme mutant 144AcK Escherichia coli
3.51
-
 tRNATyr pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant wild-type enzyme Escherichia coli
10
-
 L-tyrosine pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 235AcK Escherichia coli
140
-
 ATP pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 235AcK Escherichia coli
290
-
 L-tyrosine pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 85AcK Escherichia coli
900
-
 ATP pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 85AcK Escherichia coli
1570
-
 L-tyrosine pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 144AcK Escherichia coli
1780
-
 L-tyrosine pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 355AcK Escherichia coli
1990
-
 L-tyrosine pH 7.2, 37°C, Tyr activation activity, recombinant wild-type enzyme Escherichia coli
24290
-
 ATP pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 355AcK Escherichia coli
27330
-
 ATP pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 144AcK Escherichia coli
33020
-
 ATP pH 7.2, 37°C, Tyr activation activity, recombinant wild-type enzyme Escherichia coli