Cloned (Comment) | Organism |
---|---|
expression of wild-type and mutant enzymes as His-tagged proteins in Escherichia coli | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
K231A | site-directed mutagenesis, no effect on the catalytic activity of the enzyme | Homo sapiens |
K233A | mutant shows a reduced affinity for ATP | Geobacillus stearothermophilus |
S224A | site-directed mutagenesis, 7.5fold decrease of the forward rate constant | Homo sapiens |
S225A | site-directed mutagenesis, no effect on the catalytic activity of the enzyme | Homo sapiens |
S226A | site-directed mutagenesis, 60fold decrease of the forward rate constant | Homo sapiens |
T234A | decrease of the forward rate constant by 540fold, 3fold increase in affinity of the enzyme for ATP | Geobacillus stearothermophilus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.021 | - |
L-tyrosine | pH 7.5, 25°C, mutant S225A | Homo sapiens | |
0.03 | - |
L-tyrosine | pH 7.5, 25°C, mutant K231A | Homo sapiens | |
0.034 | - |
L-tyrosine | pH 7.5, 25°C, wild-type enzyme | Homo sapiens | |
0.042 | - |
L-tyrosine | pH 7.5, 25°C, mutant S226A | Homo sapiens | |
0.05 | - |
L-tyrosine | pH 7.5, 25°C, mutant S224A | Homo sapiens | |
3 | - |
ATP | pH 7.5, 25°C, mutant S225A and mutant K231A | Homo sapiens | |
4 | - |
ATP | pH 7.5, 25°C, wild-type enzyme and mutant S224A | Homo sapiens | |
4.1 | - |
ATP | pH 7.5, 25°C, mutant S226A | Homo sapiens | |
22 | - |
K+ | pH 7.5, 25°C, mutant S226A | Homo sapiens | |
24 | - |
K+ | pH 7.5, 25°C, mutant S224A | Homo sapiens | |
30 | - |
K+ | pH 7.5, 25°C, mutant S225A | Homo sapiens | |
32 | - |
K+ | pH 7.5, 25°C, wild-type enzyme | Homo sapiens |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
K+ | activates the wild-type enzyme and mutants S225A and K231A, no interaction with the KMSSS motif | Homo sapiens | |
Mg2+ | required | Homo sapiens | |
Mg2+ | required, MgATP2- | Geobacillus stearothermophilus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-tyrosine + tRNATyr | Homo sapiens | - |
AMP + L-Tyr-tRNATyr + diphosphate | - |
r | |
ATP + tyrosine + tRNATyr | Geobacillus stearothermophilus | - |
AMP + Tyr-tRNATyr + diphosphate | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Geobacillus stearothermophilus | - |
- |
- |
Homo sapiens | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant wild-type and mutant His-tagged enzymes | Homo sapiens |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr | S224 and S226 are involved in the catalytic mechanism, the sequence 222KKSSS226, termed KMSSS motif, stabilizes the the transition state for the tyrosine activation reactionby interacting with the diphosphate moiety of ATP | Homo sapiens | |
ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr | the 230KFGKT234 sequence, termed the KMSKS motif, participates in catalysis of the tyrosine activation reaction, specifically Lys230, Lys233, and Thr234 stabilize the transition state by interacting with the diphosphate moiety of the ATP cofactor | Geobacillus stearothermophilus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-tyrosine + tRNATyr | - |
Homo sapiens | AMP + L-Tyr-tRNATyr + diphosphate | - |
r | |
ATP + L-tyrosine + tRNATyr | 2-step reaction mechanism, 1. activation of the amino acid by MgATP2- to form an enzyme-bound aminoacyl-adenylate intermediate, 2. transfer of the amino acid to the 3'-end of its cognate tRNATyr | Homo sapiens | AMP + L-Tyr-tRNATyr + diphosphate | - |
r | |
ATP + tyrosine + tRNATyr | - |
Geobacillus stearothermophilus | AMP + Tyr-tRNATyr + diphosphate | - |
r | |
ATP + tyrosine + tRNATyr | 2-step reaction mechanism, 1. activation of the amino acid by MgATP2- to form an enzyme-bound aminoacyl-adenylate intermediate, 2. transfer of the amino acid to the 3'-end of its cognate tRNATyr | Geobacillus stearothermophilus | AMP + Tyr-tRNATyr + diphosphate | - |
r |
Synonyms | Comment | Organism |
---|---|---|
Tyrosyl-tRNA synthetase | - |
Homo sapiens |
Tyrosyl-tRNA synthetase | - |
Geobacillus stearothermophilus |
TyrRS | - |
Homo sapiens |
TyrRS | - |
Geobacillus stearothermophilus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Homo sapiens |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.78 | - |
L-tyrosine | pH 7.5, 25°C, mutant S226A | Homo sapiens | |
6 | - |
L-tyrosine | pH 7.5, 25°C, mutant S224A | Homo sapiens | |
6.08 | - |
L-tyrosine | pH 7.5, 25°C, mutant S226A | Homo sapiens | |
30 | - |
L-tyrosine | pH 7.5, 25°C, mutant K231A | Homo sapiens | |
31 | - |
L-tyrosine | pH 7.5, 25°C, mutant S225A | Homo sapiens | |
45 | - |
L-tyrosine | pH 7.5, 25°C, wild-type enzyme | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Homo sapiens | |
ATP | dependent on, MgATP2- | Geobacillus stearothermophilus |