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Literature summary for 6.1.1.B3 extracted from

  • Blaise, M.; Becker, H.; Lapointe, J.; Cambillau, C.; Giege, R.; Kern, D.
    Glu-Q-tRNAAsp synthetase coded by the yadB gene, a new paralog of aminoacyl-tRNA synthetase that glutamylates tRNAAsp anticodon (2005), Biochimie, 87, 847-861.
    View publication on PubMed
Search for more literature for 6.1.1.B3

Inhibitors

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 [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

Organism UniProt Comment Textmining
Escherichia coli P27305
-
-

Substrates and Products (Substrate)

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

Synonyms Comment Organism
gluQ
-
 Escherichia coli
Glutamyl-Q tRNA(Asp) synthetase
-
 Escherichia coli
YadB
-
 Escherichia coli

Turnover Number [1/s]

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 [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