Literature summary for 6.1.1.4 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.

Crystallization (Commentary)

Crystallization (Comment)	Organism
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 enzymes 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

Crystallization (Comment)

Organism

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 enzymes 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

Metals/Ions	Comment	Organism	Structure
Mg2+	-	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Substrates and Products (Substrate)

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

Synonyms

Synonyms	Comment	Organism
leucyl-tRNA ligase	-	Escherichia coli
LeuRS	-	Escherichia coli

pH Optimum

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

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Release 2023.1 (January 2023)