Literature summary for 6.1.1.1 extracted from

Bonnefond, L.; Frugier, M.; Touze, E.; Lorber, B.; Florentz, C.; Giege, R.; Sauter, C.; Rudinger-Thirion, J.
Crystal structure of human mitochondrial tyrosyl-tRNA synthetase reveals common and idiosyncratic features (2007), Structure, 15, 1505-1516.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression of His-tagged full-length wild-type and truncated mutant enzymes in Escherichia coli	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
mutant mt-TyrRS-DS4, lacking the C-terminal S4-like domain, in complex with Tyr-AMS, an adenylate analogue, X-ray diffraction structure determination and analysis at 2.2 A resolution, molecular replacement	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
M252A	site-directed mutagenesis, the mutant is fully active in ATP/diphosphate exchange, indicating that the site for tyrosyl-adenylate formation remains unperturbed upon mutation, tRNA mutant U73 is no more charged by mt-TyrRS upon Met252Ala mutation, the weak tyrosylation activity of tRNATyr with G73 is completely abolished, mutating Met252 shows only faint effects on wild-type and mutants mt-tRNATyr charging as compared to the wild-type enzyme	Homo sapiens
Q202A	site-directed mutagenesis, the mutant is fully active in ATP/diphosphate exchange, indicating that the site for tyrosyl-adenylate formation remains unperturbed upon mutation, the weak tyrosylation activity of tRNATyr with G73 is completely abolished, mutating Gln202 shows only faint effects on wild-type and mutants mt-tRNATyr charging as compared to the wild-type enzyme	Homo sapiens
S200A	site-directed mutagenesis, the mutant is fully active in ATP/diphosphate exchange, indicating that the site for tyrosyl-adenylate formation remains unperturbed upon mutation, replacing Ser200 with Glu completely abolishes tyrosylation activity of wild-type and mutated tRNATyr transcripts	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
mitochondrion	the mt-TyrRS is strictly mitochondrial, mitochondrial idiosyncrasies	Homo sapiens	5739	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	-	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + L-tyrosine + tRNATyr	Homo sapiens	-	AMP + diphosphate + L-tyrosyl-tRNATyr	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged full-length wild-type and mutant mitochondrial enzymes, and truncated mutant mt-TyrRS-DS4 mitochondrial enzyme from Escherichia coli by nickel affinity chromatography	Homo sapiens

Reaction

Reaction	Comment	Organism	Reaction ID
ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr	functional importance of Ser200 in the catalytic domain in line with an involvement of A73 rather than N1-N72 in tyrosine identity, active site structure, role of clusters 1 and 2 in tRNATyr acceptor arm	Homo sapiens	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + L-tyrosine + tRNATyr	-	Homo sapiens	AMP + diphosphate + L-tyrosyl-tRNATyr	-	?

Subunits

Subunits	Comment	Organism
dimer	homodimeric mitochondrial enzyme crystal structure analysis, the active mutant mitochondrial enzyme, deprived of the C-terminal S4-like domain, resembles eubacterial TyrRSs with a canonical tyrosine-binding pocket and adenylate-binding residues typical of class I synthetases, mt-TyrRS shows an asymmetry propagating from the dimer interface toward the two catalytic sites and extremities of each subunit, structure comparisons with other TyrRSs, overview	Homo sapiens

Synonyms

Synonyms	Comment	Organism
mitochondrial tyrosyl-tRNA synthetase	-	Homo sapiens
mt-TyrRS	-	Homo sapiens

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Homo sapiens

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Release 2023.1 (January 2023)