BRENDA - Enzyme Database

Role of zinc in tRNA-acceptor stem binding by glutamyl-tRNA synthetase from E. coli: a molecular modeling study

Bothra, A.K.; Roy, S.; Mandal, C.; Mukhophadhyay, C.; J. Biomol. Struct. Dyn. 15, 19-25 (1997)

Data extracted from this reference:

Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
6.1.1.17
Zinc
enzyme molecule contains one atom of zinc; no direct interaction of the zinc atom with tRNA. It may stabilize a region of polypeptide chain which is involved in acceptor stem binding; zinc metalloenzyme
Escherichia coli
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
6.1.1.17
Escherichia coli
-
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
6.1.1.17
ATP + L-glutamate + tRNAGlu
-
232
Escherichia coli
AMP + diphosphate + L-glutamyl-tRNAGlu
-
232
Escherichia coli
-
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
6.1.1.17
Zinc
enzyme molecule contains one atom of zinc; no direct interaction of the zinc atom with tRNA. It may stabilize a region of polypeptide chain which is involved in acceptor stem binding; zinc metalloenzyme
Escherichia coli
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
6.1.1.17
ATP + L-glutamate + tRNAGlu
-
232
Escherichia coli
AMP + diphosphate + L-glutamyl-tRNAGlu
-
232
Escherichia coli
-