Literature summary for 6.1.1.20 extracted from

Klipcan, L.; Levin, I.; Kessler, N.; Moor, N.; Finarov, I.; Safro, M.
The tRNA-induced conformational activation of human mitochondrial phenylalanyl-tRNA synthetase (2008), Structure, 16, 1095-1104.

Search for more literature for 6.1.1.20

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified mitochondrial PheRS complexed with Phe-AMP, cryoprotection by mother liquor solution containing 25% glycerol, X-ray diffraction structure determination and analysis at 2.2 A resolution	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
mitochondrion	mitochondrial PheRS is nuclear-encoded	Homo sapiens	5739	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	-	Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
45000	-	mitPheRS, gel filtration	Homo sapiens
49600	-	1 * 49600, sequence calculation	Homo sapiens
71000	-	binary mitPheRS-tRNAPhe complex, gel filtration	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + L-phenylalanine + tRNAPhe	Homo sapiens	-	AMP + diphosphate + L-phenylalanyl-tRNAPhe	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + L-phenylalanine + tRNAPhe	-	Homo sapiens	AMP + diphosphate + L-phenylalanyl-tRNAPhe	-	?
ATP + L-phenylalanine + tRNAPhe	recognition of phenylalanyl-adenylate and substrate binding structure, docking model, overview. Formation of the PheRS-tRNAPhe complex in human mitochondria must be accompanied by considerable rearrangement, i.e. hinge-type rotation through about 160degree, of the anticodon binding domain upon tRNA binding, overview	Homo sapiens	AMP + diphosphate + L-phenylalanyl-tRNAPhe	-	?

Subunits

Subunits	Comment	Organism
monomer	1 * 49600, sequence calculation	Homo sapiens
More	human mitPheRS consists of four major parts: the N-terminal region, residues 1-47, the catalytic domain, residues 48-289, the linker region, residues 290-322, and the C-terminal domain, residues 323-415. Multimeric organization is not a prerequisite for phenylalanylation activity, as monomeric mitochondrial phenylalanyl-tRNA synthetase is also active. The anticodon binding domain of the beta subunit of alphabeta2 PheRS is located at the C-terminus of mitPheRS overlapping with the acceptor stem of phenylalanine transfer RNA, structure, overview	Homo sapiens

Synonyms

Synonyms	Comment	Organism
mitochondrial phenylalanyl-tRNA synthetase	-	Homo sapiens
mitochondrial PheRS	-	Homo sapiens
mitPheRS	-	Homo sapiens
Phenylalanyl-tRNA synthetase	-	Homo sapiens
PheRS	-	Homo sapiens

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Homo sapiens

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Release 2023.1 (January 2023)