BRENDA - Enzyme Database

Coevolution of specificity determinants in eukaryotic glutamyl- and glutaminyl-tRNA synthetases

Hadd, A.; Perona, J.J.; J. Mol. Biol. 426, 3619-3633 (2014)

Data extracted from this reference:

Cloned(Commentary)
EC Number
Commentary
Organism
6.1.1.17
gene GUS1, phylogenetic analysis
Saccharomyces cerevisiae
6.1.1.18
gene GLN4, phylogenetic analysis
Saccharomyces cerevisiae
Engineering
EC Number
Amino acid exchange
Commentary
Organism
6.3.5.7
additional information
construction of an an N-terminal deletion mutant lacking amino acids 1-186 corresponding to the eukaryote-specific protein domains. The domains substantially influence amino acid binding, tRNA binding and aminoacylation efficiency, but they play no role in either specific nucleotide readout or discrimination against noncognate tRNA
Saccharomyces cerevisiae
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
6.1.1.17
additional information
-
additional information
steady-state and transient kinetic analysis
Saccharomyces cerevisiae
6.1.1.17
0.0012
-
tRNAGlu
pH and temperature not specified in the publication
Saccharomyces cerevisiae
6.1.1.17
20
-
L-glutamate
pH and temperature not specified in the publication
Saccharomyces cerevisiae
6.1.1.18
additional information
-
additional information
steady-state and transient kinetic analysis
Saccharomyces cerevisiae
6.1.1.18
0.00019
-
tRNAGln
pH and temperature not specified in the publication
Saccharomyces cerevisiae
6.1.1.18
1.7
-
L-glutamine
pH and temperature not specified in the publication
Saccharomyces cerevisiae
6.3.5.7
0.16
-
L-glutamine
wild-type, pH 7.5, 37C
Saccharomyces cerevisiae
6.3.5.7
0.19
-
L-glutamyl-tRNAGln
wild-type, pH 7.5, 37C
Saccharomyces cerevisiae
6.3.5.7
1.2
-
L-glutamine
N-terminal deletion mutant, pH 7.5, 37C
Saccharomyces cerevisiae
6.3.5.7
5.6
-
L-glutamyl-tRNAGln
N-terminal deletion mutant, pH 7.5, 37C
Saccharomyces cerevisiae
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
6.1.1.17
Mg2+
required
Saccharomyces cerevisiae
6.1.1.18
Mg2+
required
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
6.1.1.17
ATP + L-glutamate + tRNAGlu
Saccharomyces cerevisiae
-
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
?
6.1.1.17
ATP + L-glutamate + tRNAGlu
Saccharomyces cerevisiae ATCC 204508 / S288c
-
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
?
6.1.1.18
ATP + L-glutamine + tRNAGln
Saccharomyces cerevisiae
-
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
?
6.1.1.18
ATP + L-glutamine + tRNAGln
Saccharomyces cerevisiae ATCC 204508 / S288c
-
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
6.1.1.17
Saccharomyces cerevisiae
P46655
-
-
6.1.1.17
Saccharomyces cerevisiae ATCC 204508 / S288c
P46655
-
-
6.1.1.18
Saccharomyces cerevisiae
P13188
-
-
6.1.1.18
Saccharomyces cerevisiae ATCC 204508 / S288c
P13188
-
-
6.3.5.7
Saccharomyces cerevisiae
P13188
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
6.1.1.17
ATP + L-glutamate + tRNAGlu
-
745552
Saccharomyces cerevisiae
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
6.1.1.17
ATP + L-glutamate + tRNAGlu
a two-step aminoacylation reaction
745552
Saccharomyces cerevisiae
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
6.1.1.17
ATP + L-glutamate + tRNAGlu
-
745552
Saccharomyces cerevisiae ATCC 204508 / S288c
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
6.1.1.17
ATP + L-glutamate + tRNAGlu
a two-step aminoacylation reaction
745552
Saccharomyces cerevisiae ATCC 204508 / S288c
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
6.1.1.18
ATP + L-glutamine + tRNAGln
-
745552
Saccharomyces cerevisiae
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
6.1.1.18
ATP + L-glutamine + tRNAGln
a two-step aminoacylation reaction
745552
Saccharomyces cerevisiae
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
6.1.1.18
ATP + L-glutamine + tRNAGln
-
745552
Saccharomyces cerevisiae ATCC 204508 / S288c
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
6.1.1.18
ATP + L-glutamine + tRNAGln
a two-step aminoacylation reaction
745552
Saccharomyces cerevisiae ATCC 204508 / S288c
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
6.3.5.7
ATP + L-glutamyl-tRNAGln + L-glutamine
-
745552
Saccharomyces cerevisiae
ADP + phosphate + L-glutaminyl-tRNAGln + L-glutamate
-
-
-
?
6.3.5.7
ATP + L-glutamyl-tRNAGln + L-glutamine
-
745552
Saccharomyces cerevisiae ATCC 204508 / S288c
ADP + phosphate + L-glutaminyl-tRNAGln + L-glutamate
-
-
-
?
Subunits
EC Number
Subunits
Commentary
Organism
6.1.1.18
More
Saccharomyces cerevisiae GlnRS contains an N-terminal domain that is conserved in eukaryotic enzymes and is not present in bacterial homologues, The N-terminal domain consists of 187 amino acids organized in two helical subdomains and is followed by an unstructured 26-residue linker that links it with the main catalytic portion of the enzyme, the C-terminal domain, computational modeling
Saccharomyces cerevisiae
Turnover Number [1/s]
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
6.1.1.17
1.5
-
L-glutamate
pH and temperature not specified in the publication
Saccharomyces cerevisiae
6.1.1.17
1.5
-
tRNAGlu
pH and temperature not specified in the publication
Saccharomyces cerevisiae
6.1.1.18
1.4
-
L-glutamine
pH and temperature not specified in the publication
Saccharomyces cerevisiae
6.1.1.18
1.4
-
tRNAGln
pH and temperature not specified in the publication
Saccharomyces cerevisiae
6.3.5.7
1.4
-
L-glutamine
wild-type, pH 7.5, 37C
Saccharomyces cerevisiae
6.3.5.7
1.7
-
L-glutamine
N-terminal deletion mutant, pH 7.5, 37C
Saccharomyces cerevisiae
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
6.1.1.17
ATP
-
Saccharomyces cerevisiae
6.1.1.18
ATP
-
Saccharomyces cerevisiae
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
6.1.1.17
gene GUS1, phylogenetic analysis
Saccharomyces cerevisiae
6.1.1.18
gene GLN4, phylogenetic analysis
Saccharomyces cerevisiae
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
6.1.1.17
ATP
-
Saccharomyces cerevisiae
6.1.1.18
ATP
-
Saccharomyces cerevisiae
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
Organism
6.3.5.7
additional information
construction of an an N-terminal deletion mutant lacking amino acids 1-186 corresponding to the eukaryote-specific protein domains. The domains substantially influence amino acid binding, tRNA binding and aminoacylation efficiency, but they play no role in either specific nucleotide readout or discrimination against noncognate tRNA
Saccharomyces cerevisiae
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
6.1.1.17
additional information
-
additional information
steady-state and transient kinetic analysis
Saccharomyces cerevisiae
6.1.1.17
0.0012
-
tRNAGlu
pH and temperature not specified in the publication
Saccharomyces cerevisiae
6.1.1.17
20
-
L-glutamate
pH and temperature not specified in the publication
Saccharomyces cerevisiae
6.1.1.18
additional information
-
additional information
steady-state and transient kinetic analysis
Saccharomyces cerevisiae
6.1.1.18
0.00019
-
tRNAGln
pH and temperature not specified in the publication
Saccharomyces cerevisiae
6.1.1.18
1.7
-
L-glutamine
pH and temperature not specified in the publication
Saccharomyces cerevisiae
6.3.5.7
0.16
-
L-glutamine
wild-type, pH 7.5, 37C
Saccharomyces cerevisiae
6.3.5.7
0.19
-
L-glutamyl-tRNAGln
wild-type, pH 7.5, 37C
Saccharomyces cerevisiae
6.3.5.7
1.2
-
L-glutamine
N-terminal deletion mutant, pH 7.5, 37C
Saccharomyces cerevisiae
6.3.5.7
5.6
-
L-glutamyl-tRNAGln
N-terminal deletion mutant, pH 7.5, 37C
Saccharomyces cerevisiae
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
6.1.1.17
Mg2+
required
Saccharomyces cerevisiae
6.1.1.18
Mg2+
required
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
6.1.1.17
ATP + L-glutamate + tRNAGlu
Saccharomyces cerevisiae
-
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
?
6.1.1.17
ATP + L-glutamate + tRNAGlu
Saccharomyces cerevisiae ATCC 204508 / S288c
-
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
?
6.1.1.18
ATP + L-glutamine + tRNAGln
Saccharomyces cerevisiae
-
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
?
6.1.1.18
ATP + L-glutamine + tRNAGln
Saccharomyces cerevisiae ATCC 204508 / S288c
-
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
?
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
6.1.1.17
ATP + L-glutamate + tRNAGlu
-
745552
Saccharomyces cerevisiae
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
6.1.1.17
ATP + L-glutamate + tRNAGlu
a two-step aminoacylation reaction
745552
Saccharomyces cerevisiae
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
6.1.1.17
ATP + L-glutamate + tRNAGlu
-
745552
Saccharomyces cerevisiae ATCC 204508 / S288c
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
6.1.1.17
ATP + L-glutamate + tRNAGlu
a two-step aminoacylation reaction
745552
Saccharomyces cerevisiae ATCC 204508 / S288c
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
6.1.1.18
ATP + L-glutamine + tRNAGln
-
745552
Saccharomyces cerevisiae
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
6.1.1.18
ATP + L-glutamine + tRNAGln
a two-step aminoacylation reaction
745552
Saccharomyces cerevisiae
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
6.1.1.18
ATP + L-glutamine + tRNAGln
-
745552
Saccharomyces cerevisiae ATCC 204508 / S288c
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
6.1.1.18
ATP + L-glutamine + tRNAGln
a two-step aminoacylation reaction
745552
Saccharomyces cerevisiae ATCC 204508 / S288c
AMP + diphosphate + L-glutaminyl-tRNAGln
-
-
-
?
6.3.5.7
ATP + L-glutamyl-tRNAGln + L-glutamine
-
745552
Saccharomyces cerevisiae
ADP + phosphate + L-glutaminyl-tRNAGln + L-glutamate
-
-
-
?
6.3.5.7
ATP + L-glutamyl-tRNAGln + L-glutamine
-
745552
Saccharomyces cerevisiae ATCC 204508 / S288c
ADP + phosphate + L-glutaminyl-tRNAGln + L-glutamate
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
6.1.1.18
More
Saccharomyces cerevisiae GlnRS contains an N-terminal domain that is conserved in eukaryotic enzymes and is not present in bacterial homologues, The N-terminal domain consists of 187 amino acids organized in two helical subdomains and is followed by an unstructured 26-residue linker that links it with the main catalytic portion of the enzyme, the C-terminal domain, computational modeling
Saccharomyces cerevisiae
Turnover Number [1/s] (protein specific)
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
6.1.1.17
1.5
-
L-glutamate
pH and temperature not specified in the publication
Saccharomyces cerevisiae
6.1.1.17
1.5
-
tRNAGlu
pH and temperature not specified in the publication
Saccharomyces cerevisiae
6.1.1.18
1.4
-
L-glutamine
pH and temperature not specified in the publication
Saccharomyces cerevisiae
6.1.1.18
1.4
-
tRNAGln
pH and temperature not specified in the publication
Saccharomyces cerevisiae
6.3.5.7
1.4
-
L-glutamine
wild-type, pH 7.5, 37C
Saccharomyces cerevisiae
6.3.5.7
1.7
-
L-glutamine
N-terminal deletion mutant, pH 7.5, 37C
Saccharomyces cerevisiae
General Information
EC Number
General Information
Commentary
Organism
6.1.1.17
evolution
the enzyme evolved by gene duplication in early eukaryotes from a nondiscriminating glutamyl-tRNAsynthetase (GluRSND, EC 6.1.1.24) that aminoacylates both tRNAGln and tRNAGlu with glutamate. This ancient GluRS also separately differentiated to exclude tRNAGln as a substrate, and the resulting discriminating GluRS and GlnRS further acquired additional protein domains assisting function in cis (the GlnRS N-terminal Yqey domain) or in trans (the Arc1p protein associating with GluRS), evolutionary modeling, detailed overview. These added domains are absent in contemporary bacterial GlnRS and GluRS. The eukaryote-specific protein domains substantially influence amino acid binding, tRNA binding and aminoacylation efficiency, but they play no role in either specific nucleotide readout or discrimination against noncognate tRNA. Eukaryotic tRNAGln and tRNAGlu recognition determinants are found in equivalent positions and aremutually exclusive to a significant degree, with key nucleotides located adjacent to portions of the protein structure that differentiated during the evolution of archaeal nondiscriminating GluRS to GlnRS. The added eukaryotic domains arose in response to distinctive selective pressures associated with the greater complexity of the eukaryotic translational apparatus. The affinity of GluRS for glutamate is significantly increased when Arc1p is not associated with the enzyme. GluRS and GlnRS are among just four aaRS families (the others are arginyl-tRNA synthetase and class I LysRS) that require the presence of tRNA for synthesis of the aminoacyl adenylate reaction intermediate. Each cytoplasmic GlxRS-tRNA pair has fully lost the ancestral nondiscriminating activity in the course of coevolution, and the more stringent specificities of Saccharomyces cerevisiae GlnRS and GluRS arise from the conserved catalytic portions of each enzyme
Saccharomyces cerevisiae
6.1.1.17
additional information
analysis of the contributions to aminoacylation efficiency made by the N-terminal Arc1p domain of Saccharomyces cerevisiae GluRS. tRNA recognition determinants in the acceptor arm, at the 3'-anticodon position and in the globular core, overview, overview
Saccharomyces cerevisiae
6.1.1.18
evolution
the enzyme evolved by gene duplication in early eukaryotes from a nondiscriminating glutamyl-tRNAsynthetase (GluRSND, EC 6.1.1.24) that aminoacylates both tRNAGln and tRNAGlu with glutamate. This ancient GluRS also separately differentiated to exclude tRNAGln as a substrate, and the resulting discriminating GluRS and GlnRS further acquired additional protein domains assisting function in cis (the GlnRS N-terminal Yqey domain) or in trans (the Arc1p protein associating with GluRS), evolutionary modeling, detailed overview. These added domains are absent in contemporary bacterial GlnRS and GluRS. The eukaryote-specific protein domains substantially influence amino acid binding, tRNA binding and aminoacylation efficiency, but they play no role in either specific nucleotide readout or discrimination against noncognate tRNA. Eukaryotic tRNAGln and tRNAGlu recognition determinants are found in equivalent positions and aremutually exclusive to a significant degree, with key nucleotides located adjacent to portions of the protein structure that differentiated during the evolution of archaeal nondiscriminating GluRS to GlnRS. The added eukaryotic domains arose in response to distinctive selective pressures associated with the greater complexity of the eukaryotic translational apparatus. GluRS and GlnRS are among just four aaRS families (the others are arginyl-tRNA synthetase and class I LysRS) that require the presence of tRNA for synthesis of the aminoacyl adenylate reaction intermediate. Each cytoplasmic GlxRS-tRNA pair has fully lost the ancestral nondiscriminating activity in the course of coevolution, and the more stringent specificities of Saccharomyces cerevisiae GlnRS and GluRS arise from the conserved catalytic portions of each enzyme
Saccharomyces cerevisiae
6.1.1.18
additional information
analysis of the contributions to aminoacylation efficiency made by the N-terminal Yqey domain of Saccharomyces cerevisiae GlnRS. tRNA recognition determinants in the acceptor arm, at the 3'-anticodon position and in the globular core, overview
Saccharomyces cerevisiae
6.3.5.7
metabolism
eukaryotic tRNAGln and tRNAGlu recognition determinants are found in equivalent positions of glutaminyl-tRNA synthetase and glutamyl-tRNA synthetase, respectively, and are mutually exclusive to a significant degree, with key nucleotides located adjacent to portions of the protein structure that differentiated during the evolution of archaeal nondiscriminating luRS to GlnRS
Saccharomyces cerevisiae
General Information (protein specific)
EC Number
General Information
Commentary
Organism
6.1.1.17
evolution
the enzyme evolved by gene duplication in early eukaryotes from a nondiscriminating glutamyl-tRNAsynthetase (GluRSND, EC 6.1.1.24) that aminoacylates both tRNAGln and tRNAGlu with glutamate. This ancient GluRS also separately differentiated to exclude tRNAGln as a substrate, and the resulting discriminating GluRS and GlnRS further acquired additional protein domains assisting function in cis (the GlnRS N-terminal Yqey domain) or in trans (the Arc1p protein associating with GluRS), evolutionary modeling, detailed overview. These added domains are absent in contemporary bacterial GlnRS and GluRS. The eukaryote-specific protein domains substantially influence amino acid binding, tRNA binding and aminoacylation efficiency, but they play no role in either specific nucleotide readout or discrimination against noncognate tRNA. Eukaryotic tRNAGln and tRNAGlu recognition determinants are found in equivalent positions and aremutually exclusive to a significant degree, with key nucleotides located adjacent to portions of the protein structure that differentiated during the evolution of archaeal nondiscriminating GluRS to GlnRS. The added eukaryotic domains arose in response to distinctive selective pressures associated with the greater complexity of the eukaryotic translational apparatus. The affinity of GluRS for glutamate is significantly increased when Arc1p is not associated with the enzyme. GluRS and GlnRS are among just four aaRS families (the others are arginyl-tRNA synthetase and class I LysRS) that require the presence of tRNA for synthesis of the aminoacyl adenylate reaction intermediate. Each cytoplasmic GlxRS-tRNA pair has fully lost the ancestral nondiscriminating activity in the course of coevolution, and the more stringent specificities of Saccharomyces cerevisiae GlnRS and GluRS arise from the conserved catalytic portions of each enzyme
Saccharomyces cerevisiae
6.1.1.17
additional information
analysis of the contributions to aminoacylation efficiency made by the N-terminal Arc1p domain of Saccharomyces cerevisiae GluRS. tRNA recognition determinants in the acceptor arm, at the 3'-anticodon position and in the globular core, overview, overview
Saccharomyces cerevisiae
6.1.1.18
evolution
the enzyme evolved by gene duplication in early eukaryotes from a nondiscriminating glutamyl-tRNAsynthetase (GluRSND, EC 6.1.1.24) that aminoacylates both tRNAGln and tRNAGlu with glutamate. This ancient GluRS also separately differentiated to exclude tRNAGln as a substrate, and the resulting discriminating GluRS and GlnRS further acquired additional protein domains assisting function in cis (the GlnRS N-terminal Yqey domain) or in trans (the Arc1p protein associating with GluRS), evolutionary modeling, detailed overview. These added domains are absent in contemporary bacterial GlnRS and GluRS. The eukaryote-specific protein domains substantially influence amino acid binding, tRNA binding and aminoacylation efficiency, but they play no role in either specific nucleotide readout or discrimination against noncognate tRNA. Eukaryotic tRNAGln and tRNAGlu recognition determinants are found in equivalent positions and aremutually exclusive to a significant degree, with key nucleotides located adjacent to portions of the protein structure that differentiated during the evolution of archaeal nondiscriminating GluRS to GlnRS. The added eukaryotic domains arose in response to distinctive selective pressures associated with the greater complexity of the eukaryotic translational apparatus. GluRS and GlnRS are among just four aaRS families (the others are arginyl-tRNA synthetase and class I LysRS) that require the presence of tRNA for synthesis of the aminoacyl adenylate reaction intermediate. Each cytoplasmic GlxRS-tRNA pair has fully lost the ancestral nondiscriminating activity in the course of coevolution, and the more stringent specificities of Saccharomyces cerevisiae GlnRS and GluRS arise from the conserved catalytic portions of each enzyme
Saccharomyces cerevisiae
6.1.1.18
additional information
analysis of the contributions to aminoacylation efficiency made by the N-terminal Yqey domain of Saccharomyces cerevisiae GlnRS. tRNA recognition determinants in the acceptor arm, at the 3'-anticodon position and in the globular core, overview
Saccharomyces cerevisiae
6.3.5.7
metabolism
eukaryotic tRNAGln and tRNAGlu recognition determinants are found in equivalent positions of glutaminyl-tRNA synthetase and glutamyl-tRNA synthetase, respectively, and are mutually exclusive to a significant degree, with key nucleotides located adjacent to portions of the protein structure that differentiated during the evolution of archaeal nondiscriminating luRS to GlnRS
Saccharomyces cerevisiae
KCat/KM [mM/s]
EC Number
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
6.1.1.17
0.824
-
L-glutamate
pH and temperature not specified in the publication
Saccharomyces cerevisiae
6.1.1.17
1250
-
tRNAGlu
pH and temperature not specified in the publication
Saccharomyces cerevisiae
6.1.1.18
0.824
-
L-glutamine
pH and temperature not specified in the publication
Saccharomyces cerevisiae
6.1.1.18
7368.4
-
tRNAGln
pH and temperature not specified in the publication
Saccharomyces cerevisiae
6.3.5.7
1.4
-
L-glutamine
wild-type, pH 7.5, 37C
Saccharomyces cerevisiae
6.3.5.7
1.7
-
L-glutamine
N-terminal deletion mutant, pH 7.5, 37C
Saccharomyces cerevisiae
KCat/KM [mM/s] (protein specific)
EC Number
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
6.1.1.17
0.824
-
L-glutamate
pH and temperature not specified in the publication
Saccharomyces cerevisiae
6.1.1.17
1250
-
tRNAGlu
pH and temperature not specified in the publication
Saccharomyces cerevisiae
6.1.1.18
0.824
-
L-glutamine
pH and temperature not specified in the publication
Saccharomyces cerevisiae
6.1.1.18
7368.4
-
tRNAGln
pH and temperature not specified in the publication
Saccharomyces cerevisiae
6.3.5.7
1.4
-
L-glutamine
wild-type, pH 7.5, 37C
Saccharomyces cerevisiae
6.3.5.7
1.7
-
L-glutamine
N-terminal deletion mutant, pH 7.5, 37C
Saccharomyces cerevisiae