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

BRENDA support

Literature summary for 6.1.1.19 extracted from

  • Thiebe, R.
    Arginyl-tRNA synthetase from brewer's yeast. Purification, properties, and steady-state mechanism (1983), Eur. J. Biochem., 130, 517-524.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
adenosine 5'-[alpha,beta-methylene]triphosphate
-
Saccharomyces pastorianus
Arginyl hydroxamate
-
Saccharomyces pastorianus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50000
-
gel filtration, enzyme form II Saccharomyces pastorianus
72000
-
1 * 72000, SDS-PAGE Saccharomyces pastorianus
80000
-
gel filtration, enzyme form I Saccharomyces pastorianus

Organism

Organism UniProt Comment Textmining
Saccharomyces pastorianus
-
-
-
Saccharomyces pastorianus C836
-
-
-

Purification (Commentary)

Purification (Comment) Organism
two active forms which are interconvertible, I and II Saccharomyces pastorianus

Reaction

Reaction Comment Organism Reaction ID
ATP + L-arginine + tRNAArg = AMP + diphosphate + L-arginyl-tRNAArg simultaneously with the release of AMP or diphosphate an allosteric rearrangement occurs. Cooperative binding of AMP and diphosphate indicates that aminoacylation reaction and backward reaction are concerted Saccharomyces pastorianus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-arginine + tRNAArg r Saccharomyces pastorianus AMP + diphosphate + L-arginyl-tRNAArg
-
?
ATP + L-arginine + tRNAArg recognizes arginine very specifically Saccharomyces pastorianus AMP + diphosphate + L-arginyl-tRNAArg
-
?
ATP + L-arginine + tRNAArg r Saccharomyces pastorianus C836 AMP + diphosphate + L-arginyl-tRNAArg
-
?
ATP + L-arginine + tRNAArg recognizes arginine very specifically Saccharomyces pastorianus C836 AMP + diphosphate + L-arginyl-tRNAArg
-
?

Subunits

Subunits Comment Organism
monomer 1 * 72000, SDS-PAGE Saccharomyces pastorianus