Inhibitors | Comment | Organism | Structure |
---|---|---|---|
glutamol-adenosine monophosphate | non-hydrolyzable analog of glutamyl-AMP, inhibits the ATP-diphosphate exchange competitively with respect to L-glutamate and ATP | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.4 | - |
ATP | pH 7.2, 37°C | Escherichia coli | |
0.43 | - |
ATP | pH 7.2, 37°C, presence of tRNAGlu | Escherichia coli | |
0.5 | - |
L-glutamate | pH 7.2, 37°C, presence of tRNAGlu | Escherichia coli | |
5.3 | - |
L-glutamate | pH 7.2, 37°C | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P27305 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-glutamate + tRNAAsp | enzyme YadB activates glutamate in the absence of tRNA and transfers the activated glutamate not on tRNAGlu but instead on tRNAAsp. tRNAAsp is able to accept two amino acids: aspartate charged by aspartyl-tRNA synthetase and glutamate charged byYadB. YadB transfers the activated glutamate on the cyclopenthene-diol ring of the modified nucleoside queuosine posttranscriptionally inserted at the wobble position of the anticodon-loop to form glutamylqueuosine | Escherichia coli | AMP + diphosphate + L-glutamyl-tRNAAsp | - |
? | |
additional information | among Escherichia coli tRNAs containing queuosine in the wobble position, only tRNAAsp is substrate ofYadB. No substrate: D-glutamate | Escherichia coli | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
gluQ | - |
Escherichia coli |
Glutamyl-Q tRNA(Asp) synthetase | - |
Escherichia coli |
YadB | - |
Escherichia coli |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
12 | - |
L-glutamate | pH 7.2, 37°C, presence of tRNAGlu | Escherichia coli | |
18 | - |
L-glutamate | pH 7.2, 37°C | Escherichia coli |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0002 | - |
glutamol-adenosine monophosphate | pH 7.2, 37°C, cosubstrate ATP | Escherichia coli | |
0.00044 | - |
glutamol-adenosine monophosphate | pH 7.2, 37°C, cosubstrate L-glutamate | Escherichia coli |