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Information on EC 6.1.1.1 - tyrosine-tRNA ligase and Organism(s) Aeropyrum pernix and UniProt Accession Q9YA64

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Aeropyrum pernix
UNIPROT: Q9YA64 not found.
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The taxonomic range for the selected organisms is: Aeropyrum pernix
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
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Tyrosine translase
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-
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Tyrosine tRNA synthetase
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-
-
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Tyrosine--tRNA ligase
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-
-
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Tyrosine-transfer ribonucleate synthetase
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-
-
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Tyrosine-transfer RNA ligase
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-
-
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Tyrosyl--tRNA ligase
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-
-
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Tyrosyl-transfer ribonucleate synthetase
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-
-
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Tyrosyl-transfer ribonucleic acid synthetase
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-
-
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Tyrosyl-transfer RNA synthetase
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-
-
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Tyrosyl-tRNA ligase
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-
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Tyrosyl-tRNA synthetase
TyrRS
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
esterification
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-
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Acylation
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-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
L-tyrosine:tRNATyr ligase (AMP-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9023-45-4
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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 + 3-(5-hydroxypyridin-2-yl)-L-alanine + tRNATyr
?
show the reaction diagram
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
show the reaction diagram
-
-
-
?
additional information
?
-
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
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00022
tRNATyr
55°C, pH 8.0
0.00022
tRNATyr
wild type enzyme, at 55°C, in 100 mM HEPES-NaOH (pH 8.0), 10 mM MgCl2, 10 mM KCl
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.29
tRNATyr
55°C, pH 8.0
0.29
tRNATyr
wild type enzyme, at 55°C, in 100 mM HEPES-NaOH (pH 8.0), 10 mM MgCl2, 10 mM KCl
additional information
additional information
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1318
tRNATyr
55°C, pH 8.0
1300
tRNATyr
wild type enzyme, at 55°C, in 100 mM HEPES-NaOH (pH 8.0), 10 mM MgCl2, 10 mM KCl
additional information
additional information
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal of SeMet-substituted TyrRS is obtained by the microbatch method, using an automatic crystallization robot. The crystals are grown at 20°C in a month. The crystal of native TyrRS is obtained by hanging-drop, vapor-diffusion method. Crystals of SeMet-substituted TyrRS belong to the space group P4(3)2(1)2, with unit cell parameters a = b = 66.66 A, c = 197.48 A. Crystals of native TyrRS belong to the space group P4(3)2(1)2 with unit cell parameters a = b = 65.91 A, c = 196.17 A
hanging-drop vapour-diffusion method, The crystals belong to the tetragonal space group P4(3)2(1)2, with unit-cell parameters a = b = 66.1, c= 196.2 A, and diffract to beyond 2.15 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D172H
mutant enzyme shows a significant reductions in tyrosylation activity
D172N
mutant enzyme shows a significant reductions in tyrosylation activity
D172P
mutant enzyme shows a significant reductions in tyrosylation activity
Y39E
mutant enzyme maintains tyrosylation activity
Y39G
mutant enzyme maintains tyrosylation activity. Although the wild-type enzyme shows specific tyrosylation activity but not aminoacylation activity for 4-azido-L-phenylalanine, the Y39G mutant exhibits near identical aminoacylation activity of both tyrosine and 4-azido-L-phenylalanine
Y39G/D172P
reduction in tyrosylation activity, the mutant shows specific aminoacylation activity for 4-azide-L-phenylalanine
Y39K
mutant enzyme maintains tyrosylation activity
D172P
the mutation completely abolishes tyrosylation activity
Y39G
the mutant exhibits near identical aminoacylation activity of both L-tyrosine and 4-azide-L-phenylalanine
Y39G/D172P
the double mutant shows a reduction in tyrosylation activity
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Cibacron Blue 3GA column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expressed in Escherichia coli BL21-CodonPlus (DE3)-RIL cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kuratani, M.; Sakai, H.; Takahashi, M.; Yanagisawa, T.; Kobayashi, T.; Murayama, K.; Chen, L.; Liu, Z.J.; Wang, B.C.; Kuroishi, C.; Kuramitsu, S.; Terada, T.; Bessho, Y.; Shirouzu, M.; Sekine, S.; Yokoyama, S.
Crystal structures of tyrosyl-tRNA synthetases from Archaea
J. Mol. Biol.
355
395-408
2006
Archaeoglobus fulgidus (O29482), Archaeoglobus fulgidus, Pyrococcus horikoshii (O58739), Pyrococcus horikoshii, Aeropyrum pernix (Q9YA64), Aeropyrum pernix
Manually annotated by BRENDA team
Iwaki, J.; Suzuki, R..; Fujimoto, Z.; Momma, M.; Kuno, A.; Hasegawa, T.
Overexpression, purification and crystallization of tyrosyl-tRNA synthetase from the hyperthermophilic archaeon Aeropyrum pernix K1
Acta Crystallogr. Sect. F
61
1003-1005
2005
Aeropyrum pernix (Q9YA64), Aeropyrum pernix DSM 11879 (Q9YA64)
Manually annotated by BRENDA team
Iwaki, J.; Endo, K.; Ichikawa, T.; Suzuki, R.; Fujimoto, Z.; Momma, M.; Kuno, A.; Nishimura, S.; Hasegawa, T.
Studies on crenarchaeal tyrosylation accuracy with mutational analyses of tyrosyl-tRNA synthetase and tyrosine tRNA from Aeropyrum pernix
J. Biochem.
152
539-548
2012
Aeropyrum pernix, Aeropyrum pernix (Q9YA64), Aeropyrum pernix DSM 11879 (Q9YA64)
Manually annotated by BRENDA team