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

BRENDA support

Literature summary extracted from

  • Arnez, J.G.; Augustine, J.G.; Francklyn, C.S.
    The first step of aminoacylation at the atomic level in histidyl-tRNA synthetase (1997), Proc. Natl. Acad. Sci. USA, 8, 7144-7149.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.1.1.21 crystal structure of enzyme-substrate complex with histidyl-tRNA synthetase, ATP, and the amino acid analog histidinyl Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
6.1.1.21 R259H mutant Arg259His, with 1000fold decreased second order rate constant kcat/Km for the ATP-diphosphate exchange, and 500fold decreased kcat/Km for aminoacylation Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.21 Escherichia coli
-
 wild-type and mutant Arg259His
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.21 ATP + L-histidine + tRNAHis
-
 Escherichia coli AMP + diphosphate + L-histidyl-tRNAHis
-
 ?