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

BRENDA support

Literature summary extracted from

  • Khodyreva, S.N.; Moor, N.A.; Ankilova, V.N.; Lavrik, O.I.
    Phenylalanyl-tRNA synthetase from E. coli MRE-600: analysis of the active site distribution on the enzyme subunit by affinity labelling (1985), Biochim. Biophys. Acta, 830, 206-212.
    View publication on PubMed

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.20 Escherichia coli
-
-
-
6.1.1.20 Escherichia coli MRE 600
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.20 ATP + L-phenylalanine + tRNAPhe
-
Escherichia coli AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
?
6.1.1.20 ATP + L-phenylalanine + tRNAPhe
-
Escherichia coli MRE 600 AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
?

Subunits

EC Number Subunits Comment Organism
6.1.1.20 More the tRNA-binding sites are formed on heavy beta-subunits of the enzyme. The catalytic center of tRNA aminoacylation is formed in the contact region of subunits Escherichia coli