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Information on EC 6.1.1.1 - tyrosine-tRNA ligase and Organism(s) Acanthamoeba polyphaga mimivirus and UniProt Accession Q5UPJ7

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Acanthamoeba polyphaga mimivirus
UNIPROT: Q5UPJ7 not found.
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The taxonomic range for the selected organisms is: Acanthamoeba polyphaga mimivirus
The enzyme appears in selected viruses and cellular organisms
Synonyms
tyrosyl-trna synthetase, tyrrs, cyt-18, mitochondrial tyrosyl-trna synthetase, mini-tyrrs, tyrrss, tyrosyl trna synthetase, cyt-18 protein, mttyrrs, ldtyrrs, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Tyrosyl-tRNA synthetase
-
Tyrosine translase
-
-
-
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Tyrosine tRNA synthetase
-
-
-
-
Tyrosine--tRNA ligase
-
-
-
-
Tyrosine-transfer ribonucleate synthetase
-
-
-
-
Tyrosine-transfer RNA ligase
-
-
-
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Tyrosyl--tRNA ligase
-
-
-
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Tyrosyl-transfer ribonucleate synthetase
-
-
-
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Tyrosyl-transfer ribonucleic acid synthetase
-
-
-
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Tyrosyl-transfer RNA synthetase
-
-
-
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Tyrosyl-tRNA ligase
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-
-
-
Tyrosyl-tRNA synthetase
TyrRS
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
esterification
-
-
-
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Acylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
L-tyrosine:tRNATyr ligase (AMP-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9023-45-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
show the reaction diagram
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
show the reaction diagram
-
-
-
-
?
additional information
?
-
mimivirus aminoacyl-tRNA synthetases function as regular translation enzymes in infected amoebas
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
show the reaction diagram
the TyrRS specificity for tyrosine and conformity with the identity rules for tRNATyr for archea/eukarya, anticodon binding site, overview
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
show the reaction diagram
-
-
-
-
?
additional information
?
-
mimivirus aminoacyl-tRNA synthetases function as regular translation enzymes in infected amoebas
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
kinetics with Escherichia coli tRNATyr, Plasmodium falciparum tRNATyr, and diverse wild-type and mutant Saccharomyces cerevisiae tRNATyrs, overview
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
activity with Escherichia coli tRNATyr, Plasmodium falciparum tRNATyr, and diverse wild-type and mutant Saccharomyces cerevisiae tRNATyrs, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SYY_MIMIV
346
0
39723
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
84134
-
2 * 84134, calculated from amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
dimer interface structure from crystal structure analysis, modeling, overview
dimer
-
2 * 84134, calculated from amino acid sequence
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified selenomethionyl-TyrRSapm in complex with tyrosinol, crystallization is improved by introducing anion-exchange chromatography, vapour diffusion method, 0.002 ml of 14 mg/ml protein in 20 mM Tris-HCl, pH 7.4, 25°C, is mixed with 500 nl reservoir solution containing 0.1 M sodium citrate, pH 5.5, and 6-9% PEG 4000 w/v, 15% 2-methyl-2,4-pentane-d12-diol, 0.1 M KCl, 1 mM MgCl2, X-ray diffraction structure determination and analysis at 2.2 A resolution, molecular replacement
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
TyrRS, phylogenetic analysis, the viral aminoacyl tRNA synthetases have not been acquired recently by horizontal gene transfer from a cellular host but rather militate in favor of an intricate evolutionary relationship between large DNA viruses and ancestral eukaryotes
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Abergel, C.; Rudinger-Thirion, J.; Giege, R.; Claverie, J.M.
Virus-encoded aminoacyl-tRNA synthetases: structural and functional characterization of mimivirus TyrRS and MetRS
J. Virol.
81
12406-12417
2007
Acanthamoeba polyphaga Mimivirus (Q5UPJ7)
Manually annotated by BRENDA team
Choudhury, A.; Banerjee, R.
The N-terminal fragment of Acanthamoeba polyphaga mimivirus tyrosyl-tRNA synthetase (TyrRS(apm)) is a monomer in solution
FEBS Lett.
587
590-599
2013
Acanthamoeba polyphaga Mimivirus
Manually annotated by BRENDA team