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Overview for MACiE Entry M0318

Version history

General Information

EC Number: 6.1.1.17 (A member of the Ligases, Forming carbon-oxygen bonds, Ligases forming aminoacyl-tRNA and related compounds)

Enzyme Name: glutamate-tRNA ligase

Biological Species: Thermus thermophilus (Bacteria)

Catalytic Chain UniprotKB Accession Codes:

  • P27000 - Glutamyl-tRNA synthetase

Representative PDB Code: 1j09 - CRYSTAL STRUCTURE OF THERMUS THERMOPHILUS GLUTAMYL-TRNASYNTHETASE COMPLEXED WITH ATP AND GLU (Resolution = 1.80 Å).

Catalytic CATH Codes:

"Other" CATH Codes:

Display structure information

Overall Reaction:

Image of L-glutamate

Image of ATP

Image of tRNA (glutamate)

right arrow

Image of L-glutamate tRNA

Image of AMP

Image of diphosphate

L-glutamate
C00025
CHEBI:29985
ATP
C00002
CHEBI:15422
tRNA (glutamate)
C01641
CHEBI:29175
L-glutamate tRNA
C02987
CHEBI:29157
AMP
C00020
CHEBI:16027
diphosphate
C00013
CHEBI:45212

Overall Comment: The first reaction step only occurs in the presence of the bound cognate tRNA molecule.


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Stepwise Description of the Reaction

Step 1The alpha carboxylate group of L-glutamate attacks the alpha phosphate of ATP, forming an activated intermediate and releasing pyrophosphate.
Step 2The alpha phosphate group of the activated adduct deprotonates the 3'OH of tRNA-Glu, activating the hydroxyl towards attack at the phospho-carbonyl. An anionic tetrahedral intermediate is formed.
Step 3The anionic intermediate collapses, eliminating AMP and Glu-tRNA.

View similar reactions (composite manual annotation)


Catalytic Residues Involved

Type Number Chain Location of Function
Lys 246 A Side Chain

Metal Cofactors for M0318

Type Het group Number Chain
magnesium MG 502 A Overview

References

  1. S. Sekine et al. (0), The EMBO Journal, 22, 676-688, 2003-0. .
    Medline: 12554668
  2. J. J. Perona et al. (1993), Biochemistry, 32, 8758-8771. Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.
    Medline: 8364025
  3. D. Kern et al. (1980), Eur. J. Biochem., 106, 137-150. The catalytic mechanism of glutamyl-tRNA synthetase of Escherichia coli. Evidence for a two-step aminoacylation pathway, and study of the reactivity of the intermediate complex.
    Medline: 6280993

Homologue information for M0318 (1j09)

CSA Homologues

MACiE Homologues (within the PDB)

MACiE Homologues (within UniprotKB/SwissProt)


Links to this entry in other databases

Link to EC-PDB-SUM Link to PDB-SUM Link to RCSB PDB Link to PDBe Link to CSA
Link to MetaCyc Link to KEGG Link to BRENDA Link to ExplorENZ

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