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Literature summary extracted from

  • Mascarenhas, A.P.; Martinis, S.A.
    Functional segregation of a predicted hinge site within the beta-strand linkers of Escherichia coli leucyl-tRNA synthetase (2008), Biochemistry, 47, 4808-4816.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.1.1.4 crystal and cocrystal structures for LeuRS, IleRS, and ValRS suggests that the CP1 domain rotates via its flexible beta-strand linkers relative to the main body along various steps in the enzyme’s reaction pathway. Computational analysis suggested that the end of the N-terminal beta-strand acted as a hinge. A molecular hinge might specifically direct movement of the CP1 domain relative to the main body Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.1.1.4 Mg2+
-
 Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.4 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.4 ATP + L-isoleucine + tRNALeu
-
 Escherichia coli AMP + diphosphate + L-isoleucyl-tRNALeu
-
 ?

Synonyms

EC Number Synonyms Comment Organism
6.1.1.4 leucyl-tRNA ligase
-
 Escherichia coli
6.1.1.4 LeuRS
-
 Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.1.1.4 7.5
-
 assay at Escherichia coli