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Enzyme Nomenclature
Information on EC 6.1.1.1 - tyrosine-tRNA ligase
for references in articles please use BRENDA:EC6.1.1.1
Word Map on EC 6.1.1.1
- 6.1.1.1
-
synthetases
-
aminoacylation
-
tyrosylation
- stearothermophilus
-
anticodon
-
amber
- neurospora
- trprs
-
kmsks
- jannaschii
-
aarss
-
methanococcus
-
tryptophanyl-trna
- medicine
-
brome
-
half-of-the-sites
- biotechnology
-
charcot-marie-tooth
-
tyrts
-
anticodon-binding
- 3-iodo-l-tyrosine
-
self-splicing
- phenylalanyl-trna
-
mischarging
-
misacylation
-
methionyl-trna
-
non-cognate
- elr
- d-tyrosine
-
fersht
-
trna-like
- pharmacology
- glnrs
- trnaphe
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
6.1.1.1
-
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RECOMMENDED NAME
GeneOntology No.
tyrosine-tRNA ligase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr
mechanism
-
ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr
the adenine ring is important to the binding of tyrosinyl adenylate to the enzyme, important water-mediated hydrogen interactions
-
ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr
the adenine ring is important to the binding of tyrosinyl adenylate to the enzyme, important water-mediated hydrogen interactions
-
ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr
mechanism, class I enzyme has a class II mode of cognate tRNA recognition
-
ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr
S356 and K395 play key roles in tRNA binding, H306, a residue at the junction of the catalytic and tRNA binding domains, stabilizes the Tyr-AMP:enzyme complex
-
ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr
the 230KFGKT234 sequence, termed the KMSKS motif, participates in catalysis of the tyrosine activation reaction, specifically Lys230, Lys233, and Thr234 stabilize the transition state by interacting with the diphosphate moiety of the ATP cofactor
-
ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr
S224 and S226 are involved in the catalytic mechanism, the sequence 222KKSSS226, termed KMSSS motif, stabilizes the the transition state for the tyrosine activation reactionby interacting with the diphosphate moiety of ATP
-
ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr
mechanism, residues Asp78, Tyr169, Gln173, Asp194, and Gln195 are involved in catalysis
-
ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr
amino acid residues Y37 and Q195 are involved in substrate specificity determination
-
ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr
mechanism
-
ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr
reaction via reactive aminoacyl-adenylate intermediate, anticodon recognition mode and involved residues Tyr43, Asp177, Tyr170, Gln174 and Gln192, overview, the lack of cross-reactivity between archaeal/eukaryotic and bacterial TyrRS-tRNATyr pairs most probably lies in the different sequence of the last base pair of the acceptor stem, C1-G72 vs G1-C72, of tRNATyr
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
-
ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr
molecular dynamics simulations of TyrRS in its free form and complexed with Tyr, ATP, tyrosyl adenylate and inhibitor respectively are carried out to investigate the ligand-linked conformational stability changes associated with its catalytic cycle. Unliganded TyrRS samples a more relaxed conformational space than substrate-bound TyrRS. There are three high flexibility regions encompassing residues 114-118, 128-133, and 226-238 respectively. The region which includes the KFGKS motif shows the highest difference in fluctuations
ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr
mechanism, class I enzyme has a class II mode of cognate tRNA recognition
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acylation
esterification
Acylation
-
-
-
-
esterification
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
L-tyrosine:tRNATyr ligase (AMP-forming)
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CAS REGISTRY NUMBER
COMMENTARY
9023-45-4
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
a model for human dominant-intermediate Charcot-Marie-Tooth neuropathy type C is established
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-
-
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the enzyme's C-terminal domain is a endothelial monocyte activating polypeptide II-like, i.e. an EMAP II-like, protein with cytokine activity
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
phylogenetic relationship of TyrRS sequences, schematic overview
physiological function
additional information
-
dissociating quaternary structures regulating novel functions of other tRNA synthetases
physiological function
-
CYT-18 also promotes self-splicing of group I intron RNAs by stabilizing the functional structure in the conserved core
physiological function
-
tyrosyl-tRNA synthetase functions in group I intron splicing
physiological function
-
although native TyrRS has no known cytokine functions, natural proteolysis of secreted TyrRS releases TyrRSMini, which not only has the same aminoacylation activity as native TyrRS when occuring as a dimer, the monomer is inactive, but TyrRSMini also has strong activity for stimulating migration of polymorphonuclear leukocytes. The migration-stimulating activity is dependent on an ELR tripeptide motif, similar to that in CXC cytokines like IL-8, and also has the familiar bell-shaped concentration dependence seen for CXC cytokines. But TyrRSMini does not induce internalization of CXCR1/2. The TyrRSMini monomer is an agonist, while TyrRSMini dimer is an antagonist of induced PMN cell migration
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 3-amino-L-tyrosine + tRNATyr
AMP + 3-amino-L-Tyr-tRNATyr + diphosphate
-
mutant Y43G, aminoacylation assay
-
?
ATP + 3-azido-L-tyrosine + tRNATyr
AMP + 3-azido-L-Tyr-tRNATyr + diphosphate
-
mutant Y43G, aminoacylation assay
-
?
ATP + 3-chloro-L-tyrosine + tRNATyr
AMP + 3-chloro-L-Tyr-tRNATyr + diphosphate
-
mutant Y43G, aminoacylation assay
-
?
ATP + 3-iodo-L-tyrosine + tRNATyr
AMP + 3-iodo-L-Tyr-tRNATyr + diphosphate
-
mutant Y43G, aminoacylation assay
-
?
ATP + 3-iodo-L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
-
mutant Y73V/Q195C and other mutants, no activity with the wild-type enzyme
-
?
ATP + 3-methoxy-L-tyrosine + tRNATyr
AMP + 3-methoxy-L-Tyr-tRNATyr + diphosphate
-
mutant Y43G, aminoacylation assay
-
?
ATP + 3-nitro-L-tyrosine + tRNATyr
AMP + 3-nitro-L-Tyr-tRNATyr + diphosphate
-
mutant Y43G, aminoacylation assay
-
?
ATP + D-3,4-dihydroxyphenylalanine + tRNATyr
AMP + D-3,4-dihydroxyphenylalanine-tRNATyr + diphosphate
-
mutant Y43G, aminoacylation assay
-
?
ATP + D-tyrosine + tRNATyr
AMP + D-Tyr-tRNATyr + diphosphate
-
mutant Y43G, aminoacylation assay
-
?
ATP + L-3,4-dihydroxyphenylalanine + tRNATyr
AMP + L-3,4-dihydroxyphenylalanine-tRNATyr + diphosphate
-
mutant Y43G, aminoacylation assay
-
?
ATP + L-beta-(5-hydroxy-2-pyridyl)-alanine + tRNATyr
AMP + L-beta-(5-hydroxy-2-pyridyl)-alanine-tRNATyr + diphosphate
ATP + m-fluoro-D,L-tyrosine + tRNATyr
AMP + m-fluoro-D,L-Tyr-tRNATyr + diphosphate
-
mutant Y43G, aminoacylation assay
-
?
ATP + N-acetyl-L-tyrosine + tRNATyr
AMP + N-acetyl-L-Tyr-tRNATyr + diphosphate
-
wild-type and mutant Y43G, aminoacylation assay
-
?
ATP + N-formyl-L-tyrosine + tRNATyr
AMP + N-formyl-L-Tyr-tRNATyr + diphosphate
-
wild-type and mutant Y43G, aminoacylation assay
-
?
ATP + N-o-nitrophenylsulfenyl-L-tyrosine + tRNATyr
AMP + N-o-nitrophenylsulfenyl-L-Tyr-tRNATyr + diphosphate
-
wild-type and mutant Y43G, aminoacylation assay
-
?
ATP + O-dansyl-L-tyrosine + tRNATyr
AMP + O-dansyl-L-Tyr-tRNATyr + diphosphate
-
wild-type and mutant Y43G, aminoacylation assay
-
?
ATP + O-phospho-L-tyrosine + tRNATyr
AMP + O-phospho-L-Tyr-tRNATyr + diphosphate
-
wild-type and mutant Y43G, aminoacylation assay
-
?
ATP + p-acetyl-L-phenylalanine + tRNATyr
AMP + diphosphate + p-acetyl-L-phenylalanyl-tRNATyr
-
aminoacyl-tRNA synthetases are designed through a combination of homology modeling, molecular docking and binding affinity computation with the purpose of incorporating pACPhe into proteins in Escherichia coli
-
-
?
ATP + p-iodophenylalanine + tRNATyr
AMP + diphosphate + p-iodophenylalanyl-tRNATyr
-
a variant of the Methanococcus jannaschii tyrosyl synthetase that selectively incorporates para-iodophenylalanine in response to an amber stop codon is identified
-
-
?
ATP + 3-(2-naphthyl)alanine + tRNATyr
AMP + diphosphate + 3-(2-naphthyl)alanyl-tRNATyr
-
activity of a natural mutant enzyme, NpAla TyrRS activity
-
-
?
ATP + 3-(2-naphthyl)alanine + tRNATyr
AMP + diphosphate + 3-(2-naphthyl)alanyl-tRNATyr
-
activity of a natural mutant enzyme, NpAla TyrRS activity, altered specificity is due to both side-chain and backbone rearrangements within the active site that modify hydrogen bonds and packing interactions with substrate, as well as disrupt the alpha8-helix, which spans the WT active site
-
-
?
ATP + 3-azido-L-tyrosine + tRNATyr
AMP + diphosphate + 3-azido-L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + 3-azido-L-tyrosine + tRNATyr
AMP + diphosphate + 3-azido-L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + 3-azido-L-tyrosine + tRNATyr
AMP + diphosphate + 3-azido-L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + 3-iodo-L-tyrosine + tRNATyr
AMP + diphosphate + 3-iodo-L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + 3-iodo-L-tyrosine + tRNATyr
AMP + diphosphate + 3-iodo-L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + 3-iodo-L-tyrosine + tRNATyr
AMP + diphosphate + 3-iodo-L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + 4-acetylphenylalanine + tRNATyr
AMP + diphosphate + 4-acetylphenylalanyl-tRNATyr
-
activity of a natural mutant enzyme
-
-
?
ATP + 4-acetylphenylalanine + tRNATyr
AMP + diphosphate + 4-acetylphenylalanyl-tRNATyr
-
activity of a natural mutant enzyme, altered specificity is due to both side-chain and backbone rearrangements within the active site that modify hydrogen bonds and packing interactions with substrate, as well as disrupt the alpha8-helix, which spans the WT active site
-
-
?
ATP + 4-bromophenylalanine + tRNATyr
AMP + diphosphate + 4-bromophenylalanyl-tRNATyr
-
activity of a natural mutant enzyme, p-BrPhe TyrRS activity
-
-
?
ATP + 4-bromophenylalanine + tRNATyr
AMP + diphosphate + 4-bromophenylalanyl-tRNATyr
-
activity of a natural mutant enzyme, p-BrPhe TyrRS activity, altered specificity is due to both side-chain and backbone rearrangements within the active site that modify hydrogen bonds and packing interactions with substrate, as well as disrupt the alpha8-helix, which spans the WT active site
-
-
?
ATP + L-beta-(5-hydroxy-2-pyridyl)-alanine + tRNATyr
AMP + L-beta-(5-hydroxy-2-pyridyl)-alanine-tRNATyr + diphosphate
-
L-beta-(5-hydroxy-2-pyridyl)-alanine i.e. azatyrosine, mutant F130S, and wild-type enzyme the latter showing low activity
-
?
ATP + L-beta-(5-hydroxy-2-pyridyl)-alanine + tRNATyr
AMP + L-beta-(5-hydroxy-2-pyridyl)-alanine-tRNATyr + diphosphate
-
L-beta-(5-hydroxy-2-pyridyl)-alanine i.e. azatyrosine, mutant F130S shows 17fold higher activity in vivo than the wild-type enzyme
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
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
functional idiosyncrasies of the viral TyrRS, activity with Escherichia coli tRNATyr, Plasmodium falciparum tRNATyr, and diverse wild-type and mutant Saccharomyces cerevisiae tRNATyrs, overview, the TyrRS specificity for tyrosine and recognition of the tRNATyr acceptor stem show conformity with the identity rules for tRNATyr for archea/eukarya, anticodon binding site, overview
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
-
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
wild-type activity
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
identitification of determinants in the cognate tRNATyr, the tRNATyr molecule forms an L-shaped structure, the acceptor stem and anticodon loop of the tRNATyr interact with different subunits of the dimeric TyrRS molecule, overview
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
-
2-step reaction mechanism, 1. activation of the amino acid by MgATP2- to form an enzyme-bound aminoacyl-adenylate intermediate, 2. transfer of the amino acid to the 3'-end of its cognate tRNATyr
-
r
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
-
2-step reaction, 1. activation of L-tyrosine with ATP to form L-Tyr-AMP, 2. transfer of the tyrosyl-group to tRNATyr
-
?
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
the enzyme aminoacylates Escherichia coli tRNA as well as in vitro transcribed human mitochondrial tRNAs
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
-
wild-type and mutant Y43G, aminoacylation assay
-
?
ATP + L-tyrosine + tRNATyr(G34C)
AMP + diphosphate + L-tyrosyl-tRNATyr(G34C)
-
the enzyme strictly recognizes the C1-G72 base pair, whereas the enzyme from Thermus thermophilus recognizes the G1-C72 in a different manner using different residues
-
-
?
ATP + L-tyrosine + tRNATyr(G34C)
AMP + diphosphate + L-tyrosyl-tRNATyr(G34C)
the enzyme strictly recognizes the C1-G72 base pair, whereas the enzyme from Thermus thermophilus recognizes the G1-C72 in a different manner using different residues
-
-
?
ATP + L-tyrosine + tRNATyr(wild-type)
AMP + diphosphate + L-tyrosyl-tRNATyr(wild-type)
-
the enzyme strictly recognizes the C1-G72 base pair, whereas the enzyme from Thermus thermophilus recognizes the G1-C72 in a different manner using different residues
-
-
?
ATP + L-tyrosine + tRNATyr(wild-type)
AMP + diphosphate + L-tyrosyl-tRNATyr(wild-type)
the enzyme strictly recognizes the C1-G72 base pair, whereas the enzyme from Thermus thermophilus recognizes the G1-C72 in a different manner using different residues
-
-
?
ATP + O-methyl-L-tyrosine + tRNATyr
AMP + O-methyl-L-Tyr-tRNATyr + diphosphate
-
-
?
ATP + O-methyl-L-tyrosine + tRNATyr
AMP + O-methyl-L-Tyr-tRNATyr + diphosphate
-
wild-type and mutant Y43G, aminoacylation assay
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
K2ATP2- or Na2ATP2-
-
-
-
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
same affinity for tRNA or tRNA acylated with tyrosine
-
-
-
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
r
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
r
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
Na2ATP2-, specific for tyrosine as amino acid
-
-
-
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
phosphorothioate analogs of ATP
-
-
-
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
2-step reaction mechanism, 1. activation of the amino acid by MgATP2- to form an enzyme-bound aminoacyl-adenylate intermediate, 2. transfer of the amino acid to the 3'-end of its cognate tRNATyr
-
r
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
2-step reaction: 1. tyrosine activation to form the tyrosinyl-adenylate intermediate, 2. transfer of tyrosine from the tyrosinyl-adenylate intermediate to the tRNATyr
-
r
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
extreme high fidelity in charging the tRNA with an amino acid
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
tRNATyr substrate from Escherichia coli
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
enzyme plays a key role in protein biosynthesis
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
-
-
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
specificity for amino acids, with regard to the specificity for ATP the hydroxy group of ribose and the amino group in position 6 of the base are essential
-
-
-
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
heterologous tRNATyr from Escherichia coli and Methanococcus jannashii, tyrosylation efficiency of tRNA variants: determinants are base pair C1-G72, discriminator residue A73, and the 3 anticodon bases G34, U35, and A36
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
extreme high fidelity in charging the tRNA with an amino acid
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
enzyme plays a key role in protein biosynthesis
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
tRNATyr structure requirements, the C-terminal domain has a crucial role in the recognition of tRNATyr, first by recognizing the tRNA's unique shape and secondly by participating in specific interactions with one of the anticodon bases
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
tRNATyr structure requirements, the C-terminal domain has a crucial role in the recognition of tRNATyr, first by recognizing the tRNA's unique shape and secondly by participating in specific interactions with one of the anticodon bases
-
?
additional information
?
-
mimivirus aminoacyl-tRNA synthetases function as regular translation enzymes in infected amoebas
-
-
-
additional information
?
-
-
no activity with 4-azido-L-phenylalanine, 4-amino-L-phenylalanine, 4-nitro-L-phenylalanine, 4-methyl-L-phenylalanine, 4-fluoro-L-phenylalanine, 4-chloro-L-phenylalanine, 4-bromo-L-phenylalanine
-
-
-
additional information
?
-
-
conformational flexibility of cytokine-like C-module of the enzyme
-
-
-
additional information
?
-
-
the enzyme's C-terminal domain, an EMAP II-like protein, is active in angiogenesis pathways and stimulates immune cells, when cleaved off the enzyme, it stimulates blood vessel development
-
?
additional information
?
-
-
TyrRS deficiency is involved in the autosomal dominant intermediate Charcot-Marie-Tooth neuropathy type C disorder, overview
-
-
-
additional information
?
-
-
two distinct conformational states of the active site in the three Leishmania major TyrRS structures
-
-
-
additional information
?
-
-
high degree of structural plasticity that is observed in these aminoacyl-tRNA synthetases, overview
-
-
-
additional information
?
-
-
CYT-18 protein is a tyrosyl-tRNA synthetase adapted to function in group I intron splicing by acquiring a new RNA binding surface
-
-
-
additional information
?
-
-
no activity with tRNAAsp and tRNAPhe
-
?
additional information
?
-
the lack of cross-reactivity between archaeal/eukaryotic and bacterial TyrRS-tRNATyr pairs most probably lies in the different sequence of the last base pair of the acceptor stem, C1-G72 vs G1-C72, of tRNATyr, the recognition mode of Tyr-AMP is conserved among the TyrRSs from the three kingdoms, overview
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 3-(2-naphthyl)alanine + tRNATyr
AMP + diphosphate + 3-(2-naphthyl)alanyl-tRNATyr
-
activity of a natural mutant enzyme, NpAla TyrRS activity
-
-
?
ATP + 4-acetylphenylalanine + tRNATyr
AMP + diphosphate + 4-acetylphenylalanyl-tRNATyr
-
activity of a natural mutant enzyme
-
-
?
ATP + 4-bromophenylalanine + tRNATyr
AMP + diphosphate + 4-bromophenylalanyl-tRNATyr
-
activity of a natural mutant enzyme, p-BrPhe TyrRS activity
-
-
?
ATP + L-beta-(5-hydroxy-2-pyridyl)-alanine + tRNATyr
AMP + L-beta-(5-hydroxy-2-pyridyl)-alanine-tRNATyr + diphosphate
-
L-beta-(5-hydroxy-2-pyridyl)-alanine i.e. azatyrosine, mutant F130S shows 17fold higher activity in vivo than the wild-type enzyme
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
Q5UPJ7
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
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
P00952
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
-
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
wild-type activity
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
Q57834
-
-
-
-
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
P36421
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
Q57834
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
r
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
r
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
enzyme plays a key role in protein biosynthesis
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
enzyme plays a key role in protein biosynthesis
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
-
-
?
additional information
?
-
Q5UPJ7
mimivirus aminoacyl-tRNA synthetases function as regular translation enzymes in infected amoebas
-
-
-
additional information
?
-
-
the enzyme's C-terminal domain, an EMAP II-like protein, is active in angiogenesis pathways and stimulates immune cells, when cleaved off the enzyme, it stimulates blood vessel development
-
?
additional information
?
-
-
TyrRS deficiency is involved in the autosomal dominant intermediate Charcot-Marie-Tooth neuropathy type C disorder, overview
-
-
-
additional information
?
-
-
CYT-18 protein is a tyrosyl-tRNA synthetase adapted to function in group I intron splicing by acquiring a new RNA binding surface
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
Mg2+
K+
-
dependent on, required for catalysis of the tyrosine activation step, 260fold increase of the froward reaction constant
K+
-
activates the wild-type enzyme and mutants S225A and K231A, no interaction with the KMSSS motif
Mg2+
-
required, shows regulatory function, binding of 1 Mg2+ per tRNA molecule for the transfer reaction, binding to the tRNA is weakened by chloride
Mg2+
-
required, spermidine can substitute for Mg2+ in the transacylation reaction, i.e. transfer of tyrosine from the tyrosine-AMP-enzyme complex to tRNA, but not in the tyrosine activation reaction, i.e. formation of the tyrosine-AMP-enzyme complex from tyrosine + ATP + enzyme
Mg2+
-
10 mM, can be replaced by Mn2+ with equal efficiency and by Ca2+, Co2+, Sr2+, Ba2+, spermine with reduced efficiency
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-(3,4-dichlorophenyl)-4-(2-(4-methylpiperazin-1-yl)ethoxy)furan-2(5H)-one
-
-
3-(3,4-dimethoxyphenyl)-4-(2-(4-methylpiperazin-1-yl)ethoxy)furan-2(5H)-one
-
-
3-(3,4-dimethoxyphenyl)-4-(2-(piperidin-1-yl)ethoxy)furan-2(5H)-one
-
-
3-(4-hydroxyphenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
-
replacement of the morpholine-ring in the side chain of the compound with a substituent containing more hydrophilic groups is probably more suitable for further modification. Most potent agent against Staphylococcus aureus ATCC 25923 with MIC50 value of 0.00023 mg/ml
4-(2-(3-bromophenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
-
-
4-(2-(3-chlorophenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
-
-
4-(2-(3-chlorophenylformyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
-
-
4-(2-(3-trifluoromethylphenylformyoxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(4-bromophenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
-
-
4-(2-(4-chlorophenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
-
-
4-(2-(4-fluorophenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
-
-
4-(2-(4-hydroxyphenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
-
-
4-(2-(6-hydroxynaphthalen-2-ylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(cyclohexylamino)ethoxy)-3-(3,4-dimethoxyphenyl)furan-2(5H)-one
-
-
O-(adenosine-5'-O-yl) N-(L-tyrosyl)phosphoramidate
i.e. Tyr-AMPN, a non-hydrolyzable Tyr-AMP analog, binding structure, overview
tyrosyl aryl dipeptides
-
inhibitor interacts with and occupies the key catalytic residues in the tyrosyl binding pocket of the catalytic site
chloride
-
inhibition in presence of 1 mM free Mg2+, no inhibition in presence of 10 mM free Mg2+
chloride
-
inhibition in presence of 1 mM free Mg2+, no inhibition in presence of 10 mM free Mg2+
L-tyrosinyl 1-beta-naphthyl-1,4-anhydro-D-ribitol-5-O-phosphate
-
-
additional information
-
no inhibition by acetate up to 200 mM in presence of 1 mM free Mg2+
-
additional information
-
no inhibition by L-tyrosinyl 1-beta-(E)-(3-ethoxycarbonyl-2-methylprop-2-enyl)-1,4-anhydro-D-ribitol-5-O-phosphate, N-(L-tyrosinyl)-N'-(5'-deoxy-5'-adenosinyl)-sulfamide, and 2(S)-amino-3-(4-hydroxyphenyl)propyl 1-(adenine-9-yl)-(E)-5,6-dideoxy-beta-D-ribohept-5-enfuranuronate hydrochloride
-
additional information
-
synthesis of a series of novel 4-alkoxy-3-arylfuran-2(5H)-ones as tyrosyl-tRNA synthetase inhibitors, binding model and structure-activity relationship, MIC50 values, overview
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.07
ATP
-
phosphate exchange reaction, pH 8.0, wild-type enzyme
0.0021
L-tyrosine
-
wild-type enzyme and mutant L105V, pH 7.8, 25°C
0.0043
L-tyrosine
-
mutant TyrRS, RMSSS; wild-type TyrRS, KMSSS
0.012
L-tyrosine
-
pH 7.6, 30°C, wild-type enzyme, radioisotopic assay
0.014
L-tyrosine
-
pH 7.6, 30°C, wild-type enzyme, spectrophotometric assay
0.021
L-tyrosine
-
phosphate exchange reaction, pH 8.0, wild-type enzyme
0.027
L-tyrosine
-
aminoacylation reaction, pH 8.0, wild-type enzyme
0.00022
tRNATyr
-
55°C, pH 8.0; wild type enzyme, at 55°C, in 100 mM HEPES-NaOH (pH 8.0), 10 mM MgCl2, 10 mM KCl
0.0025
tRNATyr
-
aminoacylation reaction, pH 8.0, wild-type enzyme
0.0014
tRNATyr(wild-type)
-
37°C, pH 7.5, mutant enzyme D268R
-
additional information
additional information
-
role of threonine 234 in catalysis
-
additional information
additional information
-
role of lysine 233 in catalysis
-
additional information
additional information
-
kinetic analysis of mutation
-
additional information
additional information
-
role of a mobile loop, corresponding to KMSKS signature sequence in catalytic mechanism
-
additional information
additional information
-
stoichiometry of substrate binding
-
additional information
additional information
-
kinetics, influence of assay conditions, Km for diverse tRNA variants, overview
-
additional information
additional information
-
fluorescence emission measurement for determination of steady-state kinetics for the His-tagged and the non-His-tagged recombinant enzyme
-
additional information
additional information
-
energy profiles for wild-type and mutant enzymes, kinetics for the second reaction step: wild-type enzyme and mutants D78A, Y169A, Q173A, D194A, and Q195A, kinetics for the first reaction step: wild-type enzyme, and mutants D194A and Q195A
-
additional information
additional information
-
the C-terminal His-tag of the recombinant enzyme has little effect on the catalytic activity
-
additional information
additional information
kinetics with Escherichia coli tRNATyr, Plasmodium falciparum tRNATyr, and diverse wild-type and mutant Saccharomyces cerevisiae tRNATyrs, overview
-
additional information
additional information
-
kinetic parameters for anticodon mutants of tRNATyr and for for acceptor stem mutants of tRNATyr
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.3
ATP
-
phosphate exchange reaction, pH 8.0, wild-type enzyme
5.29
ATP
-
phosphate exchange reaction, pH 8.0, wild-type enzyme
3.3
L-tyrosine
-
phosphate exchange reaction, pH 8.0, wild-type enzyme
4.4
L-tyrosine
-
pH 7.6, 30°C, wild-type enzyme, radioisotopic assay
4.6
L-tyrosine
-
pH 7.6, 30°C, wild-type enzyme, spectrophotometric assay
5.29
L-tyrosine
-
phosphate exchange reaction, pH 8.0, wild-type enzyme
7.7
L-tyrosine
-
aminoacylation reaction, pH 8.0, wild-type enzyme
0.29
tRNATyr
-
55°C, pH 8.0; wild type enzyme, at 55°C, in 100 mM HEPES-NaOH (pH 8.0), 10 mM MgCl2, 10 mM KCl
additional information
additional information
-
influence of assay conditions, kcat for diverse tRNA variants, overview
-
additional information
additional information
-
the C-terminal His-tag of the recombinant enzyme has little effect on the catalytic activity
-
additional information
additional information
-
kinetic parameters for anticodon mutants of tRNATyr and for for acceptor stem mutants of tRNATyr
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetic parameters for anticodon mutants of tRNATyr and for for acceptor stem mutants of tRNATyr
-
1300
tRNATyr
-
wild type enzyme, at 55°C, in 100 mM HEPES-NaOH (pH 8.0), 10 mM MgCl2, 10 mM KCl
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.32
AMP
-
in absence of KCl, and in presence of 1 mM free Mg2+, pH 7.4, 30°C
0.5
AMP
-
in presence of 50 mM KCl, and in presence of 1 mM free Mg2+, pH 7.4, 30°C
2.15
AMP
-
in presence of 150 mM KCl, and in presence of 1 mM free Mg2+, pH 7.4, 30°C
0.048
diphosphate
-
in presence of 150 mM KCl, and in presence of 1 mM free Mg2+, pH 7.4, 30°C
0.1
diphosphate
-
in presence of 50 mM KCl, and in presence of 1 mM free Mg2+, pH 7.4, 30°C
0.23
diphosphate
-
in absence of KCl, and in presence of 1 mM free Mg2+, pH 7.4, 30°C
0.076
L-tyrosinyl 1,4-anhydro-D-ribitol-5-O-phosphate
-
pH 7.9, 37°C
0.0057
L-tyrosinyl 1-beta-naphthyl-1,4-anhydro-D-ribitol-5-O-phosphate
-
pH 7.9, 37°C
0.15
L-tyrosinyl 1-beta-naphthyl-1,4-anhydro-D-ribitol-5-O-phosphate
-
pH 7.9, 37°C
0.0000093
L-tyrosinyl-2',3'-O-isopropylidene adenylate
-
pH 7.9, 37°C
additional information
additional information
-
inhibition kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1
3-(3,4-dichlorophenyl)-4-(2-(4-methylpiperazin-1-yl)ethoxy)furan-2(5H)-one
Staphylococcus aureus
-
above, pH not specified in the publication, temperature not specified in the publication
0.1
3-(3,4-difluorophenyl)-4-(2-(piperidin-1-yl)ethoxy)furan-2(5H)-one
Staphylococcus aureus
-
above, pH not specified in the publication, temperature not specified in the publication
0.1
3-(3,4-dimethoxyphenyl)-4-(2-(4-methylpiperazin-1-yl)ethoxy)furan-2(5H)-one
Staphylococcus aureus
-
above, pH not specified in the publication, temperature not specified in the publication
0.1
3-(3,4-dimethoxyphenyl)-4-(2-(piperidin-1-yl)ethoxy)furan-2(5H)-one
Staphylococcus aureus
-
above, pH not specified in the publication, temperature not specified in the publication
0.0243
3-(3-bromophenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0205
3-(3-chlorophenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0256
3-(3-hydroxyphenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0375
3-(3-methoxyphenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0024
3-(4-bromophenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.00062
3-(4-chlorophenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0001
3-(4-hydroxyphenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0328
3-(4-methoxyphenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0536
3-phenyl-4-(2-(piperidin-1-yl)ethoxy)furan-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0291
3-phenyl-4-(2-(propylamino)ethoxy)furan-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0355
3-phenyl-4-(2-(pyrrolidin-1-yl)ethoxy)furan-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0165
4-(2-(2,4-dichlorophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0502
4-(2-(2,4-dihydroxyphenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0052
4-(2-(2,5-dichlorophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.1
4-(2-(2-(4-nitrophenyl)hydrazinyl)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
above, pH not specified in the publication, temperature not specified in the publication
0.0568
4-(2-(2-chlorophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0414
4-(2-(2-hydroxyphenylformyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0647
4-(2-(2-methoxyphenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.1
4-(2-(2-methylphenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
IC50 above 0.1 mM, in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0182
4-(2-(2-nitrophenylformyloxyl)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0334
4-(2-(3,4-dichlorophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0753
4-(2-(3,4-dihydroxyphenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0838
4-(2-(3,4-dimethoxyphenylacetyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0067
4-(2-(3,5-dihydroxyphenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0035
4-(2-(3-bromophenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0011
4-(2-(3-chlorophenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.1
4-(2-(3-chlorophenylacetyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
IC50 above 0.1 mM, in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0009
4-(2-(3-chlorophenylformyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.081
4-(2-(3-methylphenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.1
4-(2-(3-nitrophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
IC50 above 0.1 mM, in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.026
4-(2-(3-pyridylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0043
4-(2-(3-trifluoromethylphenylformyoxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0167
4-(2-(4-bromophenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0481
4-(2-(4-bromophenylacetyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0093
4-(2-(4-chlorophenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0088
4-(2-(4-chlorophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0057
4-(2-(4-fluorophenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0936
4-(2-(4-fluorophenylacetyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0075
4-(2-(4-fluorophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0079
4-(2-(4-hydroxyphenylacetyloxy)ethoxy)-3-(4-chlorophenyl)furan-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.1
4-(2-(4-hydroxyphenylacetyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
IC50 above 0.1 mM, in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0112
4-(2-(4-hydroxyphenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0178
4-(2-(4-methylphenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0086
4-(2-(4-methylpiperazin-1-yl)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0052
4-(2-(4-nitrophenylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0168
4-(2-(6-hydroxynaphthalen-2-ylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.1
4-(2-(benzylamino)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
above, pH not specified in the publication, temperature not specified in the publication
0.0719
4-(2-(butylamino)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.1
4-(2-(cyclohexylamino)ethoxy)-3-(3,4-dimethoxyphenyl)furan-2(5H)-one
Staphylococcus aureus
-
above, pH not specified in the publication, temperature not specified in the publication
0.0874
4-(2-(cyclohexylamino)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0177
4-(2-(naphthalen-2-ylformyloxy)ethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0846
4-(2-butyryloxyethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0478
4-(2-hexanoyloxyethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0062
4-(2-morpholinoethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.041
4-(2-octanoyloxyethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
0.0128
4-(2-phenylacetyloxylethoxy)-3-phenylfuran-2(5H)-one
Staphylococcus aureus
-
in 100 mM Tris/Cl pH 7.9, 50 mM KCl, 16 mM MgCl2, at 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
activity with Escherichia coli tRNATyr, Plasmodium falciparum tRNATyr, and diverse wild-type and mutant Saccharomyces cerevisiae tRNATyrs, overview
additional information
-
in vitro tyrosylation efficiency is decreased 600fold for mutant A22G (mitochondrial gene mutation T5874C), 40fold for G15A (C5877T), and is without significant effect on U54C (A5843G)
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.5
7.5
7.6
7.9
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
-
a model is proposed, in which the KMSKS signature sequence is conformationally constrained and unable to participate in catalysis below 25°C
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
mini-TyrRS is reduced in extracts of ischemic calf muscle and in thoracic aorta explants exposed to hypoxia or VEGF
-
differentiating, YARS locates mostly in the granular structures of the growth cone, branch points and the most distal part of of projecting neurites, co-localization with synaptophysin
additional information
-
YARS is expressed ubiquitously, in neuronal cells making extensions, the enzyme is located at outgrowth behaving like an early polarity maker, overview
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
axonal termini in differentiating primary motor neuron and neuroblastoma cultures
additional information
human mitochondrial and cytosolic enzymes are encoded by two different sets of genes
-
the mt-TyrRS is strictly mitochondrial, mitochondrial idiosyncrasies
additional information
-
the C-terminal EMAP II-like protein domain of the enzyme is probably responsible for mediation of enzyme export
-
additional information
-
subcellular localization of wild-type and mutant YARS, overview
-
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
62000
-
1 * 62000 + 1 * 62000, nonidentical, Factor A, role unclear + Factor B, responsible for the activation of tyrosine, SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
dimer
dimer interface structure from crystal structure analysis, modeling, overview
dimer
-
three-dimensional structures of subunits A and B, modelling, overview
dimer
-
2 * 40000-45000, identical, sequence of tryptic peptides, SDS-PAGE
dimer
-
binding of substrates alters the structure of the subunits
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
dimer
-
1 * 62000 + 1 * 62000, nonidentical, Factor A, role unclear + Factor B, responsible for the activation of tyrosine, SDS-PAGE
additional information
-
NMR structure of the C-terminal domain of a tyrosyl-tRNA synthetase, modeling of the C-terminal domain/group I intron interactions, overview
additional information
-
computational structure analysis using fluorescence quenching experiment data, analysis of Trp144 microenvironment, temperature-induced conformational change of the module Trp144 microenvironment and red-edge excitation of the C-module tryptophan fluorescence, overview
additional information
-
three-dimensional modeling of the Escherichia coli enzyme constructed on the basis of the X-ray crystal structure of Bacillus stearothermophilus enzyme complexed with tyrosinyl adenylate, PDB code 3TS1
additional information
-
the single tyrosyl-tRNA synthetase gene in trypanosomatid genomes codes for a protein that is twice the length of TyrRS from virtually all other organisms. Each half of the double-length TyrRS contains a catalytic domain and an anticodon-binding domain. Leishmania major TyrRS shows, that the two halves of a single molecule form a pseudo-dimer resembling the canonical TyrRS dimer. The C-terminal copy of the catalytic domain has lost the catalytically important HIGH and KMSKS motifs characteristic of class I aminoacyl-tRNA synthetases. Thus, the TyrRS pseudo-dimer is inherently asymmetric and contains only one functional active site, contributed by the N-terminal half, and only one functional anticodon recognition site, contributed by the C-terminal half
additional information
structural comparison of TyrRS of different origin, overview
additional information
-
in the complex of enzyme and substrates, e.g. tRNATyr, the C-terminal domain of the enzyme is stabilized by binding in the elbow between the long variable arm and the anti-codon stem, and the linker peptide connecting it to the last helix of the alpha-helical domain becomes ordered
additional information
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
in the complex of enzyme and substrates, e.g. tRNATyr, the C-terminal domain of the enzyme is stabilized by binding in the elbow between the long variable arm and the anti-codon stem, and the linker peptide connecting it to the last helix of the alpha-helical domain becomes ordered
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
-
the C-terminal domain of the enzyme, which has cytokine and angiogenic activity and stimulates immune cells, is isolated by proteolytic cleavage or alternative splicing, the mini enzyme is a stimulator of blood vessel development, the full-length enzyme is inactive
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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
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
-
hanging-drop, vapor-diffusion method. Crystals belong to the space group P2(1), with unit cell parameters a = 40.62 A, b = 96.16 A, c = 92.64 A, beta = 94.41°
hanging drop vapor-diffusion method. Crystal structures of TyrRS catalytic domain, in complex with L-tyrosine and L-tyrosyladenylate analogue, 5'-O-[N-(L-tyrosyl)sulfamoyl]adenosine, are solved at 2.0 A and 2.7 A resolution
-
the iodoTyrRS-ec-3-azide-L-tyrosine structure is determined at a resolution of 1.8 A
-
X-ray diffraction, at 2.7 A resolution, structure analysis of the enzyme-ligand complex, e.g. with specific synthetic inhibitors, molecular modeling
-
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
-
purified recombinant C-terminally His6-tagged tyrosyl aminoacyl-tRNA synthetase, sitting-drop vapor diffusion technique, 15 mg/ml protein in 20 mM Tris, pH 8.5, 50 mM NaCl, 10 mM 2-mercaptoethanol, crystals are grown either in the presence of 2 mM 4-bromophenylalanine or 3-(2-naphthyl)alanine at 20°C or 4°C, against a mother liquor composed of 16-20% PEG 300, 3-5% PEG 8000, 100 mM Tris, pH 8.8-pH 8.2, and 10% glycerol by mixing of equla volumes, X-ray diffraction structure determination and analysis at 1.9 A resolution
-
sitting-drop vapor-diffusion method. Space group P2(1)2(1)2(1) with two molecules per asymmetric unit, with unit cell dimensions a = 45.12 A, b = 185.29 A, and c = 95.48 A. Crystal structures for the apo wild-type and O-methyl-L-tyrosine-specific mutant enzyme are determined at 2.66 A and 3.0 A
-
structure of the TyrRS-tRNA(Tyr)-L-tyrosine complex, solved at a resolution of 1.95 A
-
hanging-drop vapour diffusion method. The crystals belong to the monoclinic space group P2(1) with unit-cell parameters a = 49.2 A, b = 156.5 A, c = 55.2 A, beta = 94.2
-
1.95 A crystal structure of mutant DELTA424-669 of CYT-18 protein. DELTA424-669 crystals are grown by sitting-drop vapor diffusion. The crystals are in space group C2 with unit cell dimensions: a = 104.88 A, b = 73.21 A, c = 56.79 A, beta = 111.35°
-
a 4.5 A co-crystal structure of the Twort orf 142-I2 group I intron ribozyme bound to splicing-active, carboxy-terminally truncated CYT-18. Structure shows that the group I intron binds across the two subunits of the homodimeric protein with a newly evolved RNA-binding surface distinct from that which binds tRNATyr. This RNA binding surface provides an extended scaffold for the phosphodiester backbone of the conserved catalytic core of the intron RNA, allowing the protein to promote the splicing of a wide variety of group I introns. The group I intron-binding surface includes three small insertions and additional structural adaptations relative to non-splicing bacterial TyrRSs, indicating a multistep adaptation for splicing function
-
hanging-drop, vapor-diffusion method. Crystals belong to the space group P2(1)2(1)2(1), with unit cell parameters a = 74.35 A, b = 88.26 A, c = 162.92 A
purified recombinant modified enzyme, SceTyrRS comprising residues 1-364, as ternary complex with cognate tRNATyr and Tyr-AMP analog O-(adenosine-5'-O-yl) N-(L-tyrosyl)phosphoramidate, i.e. Tyr-AMPN, hanging-drop vapor diffusion method, mixing of equal volumes of protein solution containing ca. 0.2 mM SceTyrRS, 5 mM Tyr-AMPN, ca. 0.2 mM tRNATyr, 40 mM KCl in 20 mM Tris buffer at pH 7.5, with reservoir solution containing 25% v/v PEG 400 and 100 mM CaCl2 in 100 mM Tris buffer at pH 7.5, X-ray diffraction structure determination and analysis at 2.4 A resolution
crystal structure determination by X-ray diffraction, enzyme complexed with inhibitors at 2.8 A resolution, and truncated enzyme complexed with inhibitors at 2.2 A resolution
-
enzyme complexed to a tyrosyl aryl dipeptide inhibitor, structure analysis
-
pure enzyme, 12 mg/ml, or in complex with tyrosinol, hanging drop vapour diffusion technique, equal volumes of protein and a reservoir solution that contains 1.2 M ammonium sulfate, 10 mM MgCl2, 0.5 mM dithiothreitol, 50 mM MES, pH 5.8, X-ray diffraction structure determination and analysis, enzyme in complex with tyrosinol, ATP and tRNATyr, at 293K, equilibration of 0.004 ml protein-RNA solution against 1 ml reservoir solution, protein-RNA solution: 4-5 mg/ml of enzyme in a molar ratio of 1:1 or 1:2 with RNA, 5 mM tyrosinol, 10 mg MgCl2, 10 mM ATP, 50 mM HEPES, pH 7.0, 0.8 M ammonium sulfate, reservoir solution: 1.5-1.6 M ammonium sulfate, 0.1 M HEPES, pH 7.0, 2-4 weeks, X-ray diffraction structure determination at 2.0-2.1 A resolution and analysis
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
46
-
40% loss of activity in 4-12 min, depending on the bacterial strains used for purification, stabilization by substrates
50
-
10 min, wild-type enzyme is not affected, while the mutant F130S is almost completely inactivated
additional information
-
effects of mutations and of coupling of mutations on thermal parameters and stability, overview
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable to immediate freezing and thawing, but not for longer periods, no stabilization by potassium borohydrite, MgCl2, ATP, Vitamin B12
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 0.025 M potassium phosphate buffer, pH 6.7, 0.01 M 2-mercaptoethanol, 50% glycerol, no loss of activity in 6 months
-
4°C, 20 mM Tris-HCl buffer, pH 7, 80% loss of activity within 48 h, 5% loss of activity in presence of 10% glycerol and 3 mM 2-mercaptoethanol
-