Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 6.1.1.B3 extracted from

  • Campanacci, V.; Dubois, D.Y.; Becker, H.D.; Kern, D.; Spinelli, S.; Valencia, C.; Pagot, F.; Salomoni, A.; Grisel, S.; Vincentelli, R.; Bignon, C.; Lapointe, J.; Giege, R.; Cambillau, C.
    The Escherichia coli YadB gene product reveals a novel aminoacyl-tRNA synthetase like activity (2004), J. Mol. Biol., 337, 273-283.
    View publication on PubMed
Search for more literature for 6.1.1.B3

Cloned(Commentary)

Cloned (Comment) Organism
-
 Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
determination of strucure by molecular replacement, to 1.5 A resolution. Enzyme possesses a Zn2+ located in the putative tRNA acceptor stem-binding domain. The Zn2+ ion is coordinated by three cysteine and a tyrosine ligand Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
glutamol-adenosine monophosphate
-
 Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.5
-
 ATP pH 7.2, 37°C, activation of L-glutamate Escherichia coli
6
-
 L-glutamate pH 7.2, 37°C, activation of L-glutamate Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ enzyme possesses a Zn2+ ion located in the putative tRNA acceptor stem-binding domain. The Zn2+ ion is coordinated by three cysteine and a tyrosine ligand 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 + tRNA acceptor is unfractionated RNA Escherichia coli AMP + diphosphate + L-glutamyl-tRNA the activation step of L-glutamate is tRNA-independent ?
additional information enzyme does not catalyse attachment of the activated L-glutamate to Escherichia coli tRNAGlu Escherichia coli ?
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
14
-
 L-glutamate pH 7.2, 37°C, activation of L-glutamate Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.2
-
 glutamol-adenosine monophosphate pH 7.2, 37°C, substrate ATP, activation of L-glutamate Escherichia coli
0.44
-
 glutamol-adenosine monophosphate pH 7.2, 37°C, substrate L-glutamate, activation of L-glutamate Escherichia coli