BRENDA - Enzyme Database

Influence of supramolecular structure on the enzyme mechanism of rat liver lysyl-tRNA synthetase-catalyzed reactions

Wahab, S.Z.; Yang, D.C.H.; J. Biol. Chem. 260, 12735-12739 (1985)

Data extracted from this reference:

Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
6.1.1.6
Rattus norvegicus
-
-
-
Source Tissue
EC Number
Source Tissue
Commentary
Organism
Textmining
6.1.1.6
liver
-
Rattus norvegicus
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
6.1.1.6
ATP + ATP
the mechanism of the the enzyme in the 18S multienzyme complex is ordered bi uni uni bi ping-pong, the mechanism of the free enzyme is random
503
Rattus norvegicus
diadenosine 5',5''-P1,P4-tetraphosphate + diphosphate
-
503
Rattus norvegicus
-
6.1.1.6
ATP + lysine + tRNALys
-
503
Rattus norvegicus
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
-
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
Organism
Textmining
6.1.1.6
liver
-
Rattus norvegicus
-
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
6.1.1.6
ATP + ATP
the mechanism of the the enzyme in the 18S multienzyme complex is ordered bi uni uni bi ping-pong, the mechanism of the free enzyme is random
503
Rattus norvegicus
diadenosine 5',5''-P1,P4-tetraphosphate + diphosphate
-
503
Rattus norvegicus
-
6.1.1.6
ATP + lysine + tRNALys
-
503
Rattus norvegicus
AMP + L-lysyl-tRNALys + diphosphate
-
-
-
-