Literature summary for 6.1.1.20 extracted from

Fasiolo, F.; Sanni, A.; Potier, S.; Ebel, J.P.; Boulanger, Y.
Identification of the major tRNAPhe binding domain in the tetrameric structure of cytoplasmic phenylalanyl-tRNA synthetase from baker's yeast (1989), FEBS Lett., 242, 351-356.

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Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
cytoplasm	-	Saccharomyces cerevisiae	5737	-

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + L-phenylalanine + tRNAPhe	-	Saccharomyces cerevisiae	AMP + diphosphate + L-phenylalanyl-tRNAPhe	-	?

Subunits

Subunits	Comment	Organism
More	the amino terminal part of each beta-subunit represents the main tRNA binding domain and is not involved in either catalysis or subunit interactions. The trypsin resistant alpha2beta2 core contains the catalytic site as well as contact areas between subunits	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)