Information on EC 6.1.1.1 - Tyrosine-tRNA ligase

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The expected taxonomic range for this enzyme is: dsDNA viruses, no RNA stage, Bacteria, Archaea, Eukaryota

EC NUMBER
COMMENTARY
6.1.1.1
-
RECOMMENDED NAME
GeneOntology No.
Tyrosine-tRNA ligase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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
mechanism
-
ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr
show the reaction diagram
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
show the reaction diagram
mechanism, class I enzyme has a class II mode of cognate tRNA recognition
-
ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
mechanism, residues Asp78, Tyr169, Gln173, Asp194, and Gln195 are involved in catalysis
-
ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr
show the reaction diagram
amino acid residues Y37 and Q195 are involved in substrate specificity determination
-
ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr
show the reaction diagram
mechanism
-
ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr
show the reaction diagram
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
P36421
ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr
show the reaction diagram
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
show the reaction diagram
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
A6QHR2
PATHWAY
KEGG Link
MetaCyc Link
Aminoacyl-tRNA biosynthesis
-
tRNA charging
-
SYSTEMATIC NAME
IUBMB Comments
L-Tyrosine:tRNATyr ligase (AMP-forming)
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
CYT-18
P12063
bifunctional, aminoacylates mitochondrial tRNATyr and promotes the splicing of mitochondrial group I introns
CYT-18 protein
-
-
mini-tyrosyl-tRNA synthetase
-
N-terminal domain of tyrosyl-tRNA synthetase
mini-TyrRS
-
-
mitochondrial tyrosyl-tRNA synthetase
-
-
mitochondrial tyrosyl-tRNA synthetase
-
-
mt-TyrRS
-
-
mtTyrRS
-
bifunctional mitochondrial tyrosyl-tRNA synthetase (CYT-18 protein) both aminoacylates mitochondrial tRNATyr and acts as a structure-stabilizing splicing cofactor for group I introns
tRNATyr/tyrosyl-tRNA synthetase
-
-
Tyrosine translase
-
-
-
-
Tyrosine tRNA synthetase
-
-
-
-
Tyrosine tRNA synthetase
-
-
Tyrosine tRNA synthetase
-
-
Tyrosine tRNA synthetase
-
-
Tyrosine tRNA synthetase
-
-
Tyrosine--tRNA ligase
-
-
-
-
Tyrosine-transfer ribonucleate synthetase
-
-
-
-
Tyrosine-transfer RNA ligase
-
-
-
-
tyrosyl aminoacyl-tRNA synthetase
-
-
tyrosyl synthetase
-
-
tyrosyl tRNA synthetase
-
-
tyrosyl tRNA synthetase
-
-
Tyrosyl--tRNA ligase
-
-
-
-
Tyrosyl-transfer ribonucleate synthetase
-
-
-
-
Tyrosyl-transfer ribonucleic acid synthetase
-
-
-
-
Tyrosyl-transfer RNA synthetase
-
-
-
-
Tyrosyl-tRNA ligase
-
-
-
-
Tyrosyl-tRNA synthetase
-
-
-
-
Tyrosyl-tRNA synthetase
-
-
Tyrosyl-tRNA synthetase
-
-
Tyrosyl-tRNA synthetase
-
-
Tyrosyl-tRNA synthetase
-
-
Tyrosyl-tRNA synthetase
-
-
Tyrosyl-tRNA synthetase
-
-
Tyrosyl-tRNA synthetase
Q57834
-
Tyrosyl-tRNA synthetase
-
-
Tyrosyl-tRNA synthetase
-
-
Tyrosyl-tRNA synthetase
P12063
-
Tyrosyl-tRNA synthetase
-
-
Tyrosyl-tRNA synthetase
-
-
Tyrosyl-tRNA synthetase
-
-
Tyrosyl-tRNA synthetase
-
-
tyrosyltRNA synthetase
-
-
TyrRS
-
-
-
-
TyrRS
-
-
TyrRS
-
-
TyrRS
P12063
-
TyrRS
Staphylococcus aureus ATCC 25923
-
-
-
YARS
-
-
CAS REGISTRY NUMBER
COMMENTARY
9023-45-4
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
a model for human dominant-intermediate Charcot-Marie-Tooth neuropathy type C is established
-
-
Manually annotated by BRENDA team
C6, purified enzyme
-
-
Manually annotated by BRENDA team
mechanism of evolution
-
-
Manually annotated by BRENDA team
strain ATCC 12980
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
gene TyrS
-
-
Manually annotated by BRENDA team
the enzyme's C-terminal domain is a endothelial monocyte activating polypeptide II-like, i.e. an EMAP II-like, protein with cytokine activity
-
-
Manually annotated by BRENDA team
Staphylococcus aureus ATCC 25923
-
-
-
Manually annotated by BRENDA team
strain HB27, purified recombinant enzyme
-
-
Manually annotated by BRENDA team
wheat
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
evolution
-
phylogenetic relationship of TyrRS sequences, schematic overview
additional information
-
dissociating quaternary structures regulating novel functions of other tRNA synthetases
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
AMP + diphosphate
ATP
show the reaction diagram
-
-
-
-
AMP + diphosphate
ATP
show the reaction diagram
-
-
-
-
AMP + diphosphate
ATP
show the reaction diagram
-
-
1
-
-
-
AMP + diphosphate
ATP
show the reaction diagram
-
-
-
-
AMP + diphosphate
ATP
show the reaction diagram
-
-
-
-
ATP + 3-(2-naphthyl)alanine + tRNATyr
AMP + diphosphate + 3-(2-naphthyl)alanyl-tRNATyr
show the reaction diagram
-
activity of a natural mutant enzyme, NpAla TyrRS activity, 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-amino-L-tyrosine + tRNATyr
AMP + 3-amino-L-Tyr-tRNATyr + diphosphate
show the reaction diagram
-
mutant Y43G, aminoacylation assay
-
?
ATP + 3-azido-L-tyrosine + tRNATyr
AMP + 3-azido-L-Tyr-tRNATyr + diphosphate
show the reaction diagram
-
mutant Y43G, aminoacylation assay
-
?
ATP + 3-azido-L-tyrosine + tRNATyr
AMP + diphosphate + 3-azido-L-tyrosyl-tRNATyr
show the reaction diagram
-
-
-
-
?
ATP + 3-chloro-L-tyrosine + tRNATyr
AMP + 3-chloro-L-Tyr-tRNATyr + diphosphate
show the reaction diagram
-
mutant Y43G, aminoacylation assay
-
?
ATP + 3-iodo-L-tyrosine + tRNATyr
AMP + 3-iodo-L-Tyr-tRNATyr + diphosphate
show the reaction diagram
-
mutant Y43G, aminoacylation assay
-
?
ATP + 3-iodo-L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
show the reaction diagram
-
mutant Y73V/Q195C and other mutants, no activity with the wild-type enzyme
-
?
ATP + 3-iodo-L-tyrosine + tRNATyr
AMP + diphosphate + 3-iodo-L-tyrosyl-tRNATyr
show the reaction diagram
-
-
-
-
?
ATP + 3-methoxy-L-tyrosine + tRNATyr
AMP + 3-methoxy-L-Tyr-tRNATyr + diphosphate
show the reaction diagram
-
mutant Y43G, aminoacylation assay
-
?
ATP + 3-nitro-L-tyrosine + tRNATyr
AMP + 3-nitro-L-Tyr-tRNATyr + diphosphate
show the reaction diagram
-
mutant Y43G, aminoacylation assay
-
?
ATP + 4-acetylphenylalanine + tRNATyr
AMP + diphosphate + 4-acetylphenylalanyl-tRNATyr
show the reaction diagram
-
activity of a natural mutant enzyme, 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
show the reaction diagram
-
activity of a natural mutant enzyme, p-BrPhe TyrRS activity, 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 + D-3,4-dihydroxyphenylalanine + tRNATyr
AMP + D-3,4-dihydroxyphenylalanine-tRNATyr + diphosphate
show the reaction diagram
-
mutant Y43G, aminoacylation assay
-
?
ATP + D-tyrosine + tRNATyr
AMP + D-Tyr-tRNATyr + diphosphate
show the reaction diagram
-
mutant Y43G, aminoacylation assay
-
?
ATP + L-3,4-dihydroxyphenylalanine + tRNATyr
AMP + L-3,4-dihydroxyphenylalanine-tRNATyr + diphosphate
show the reaction diagram
-
mutant Y43G, aminoacylation assay
-
?
ATP + L-beta-(5-hydroxy-2-pyridyl)-alanine + tRNATyr
AMP + L-beta-(5-hydroxy-2-pyridyl)-alanine-tRNATyr + diphosphate
show the reaction diagram
-
L-beta-(5-hydroxy-2-pyridyl)-alanine i.e. azatyrosine, mutant F130S, and wild-type enzyme the latter showing low activity, 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 + L-Tyr-tRNATyr + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
show the reaction diagram
-
-
-
r
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
show the reaction diagram
-, Q57834
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
wild-type and mutant Y43G, aminoacylation assay
-
?
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
show the reaction diagram
Q9Y2Z4
the enzyme aminoacylates Escherichia coli tRNA as well as in vitro transcribed human mitochondrial tRNAs
-
-
?
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
-
-
-
-
?
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
P54577
-
-
-
?
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
-
-
1
-
-
-
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
P36421
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
show the reaction diagram
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
show the reaction diagram
-
wild-type activity
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
show the reaction diagram
Q5UPJ7
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
show the reaction diagram
P36421
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 + m-fluoro-D,L-tyrosine + tRNATyr
AMP + m-fluoro-D,L-Tyr-tRNATyr + diphosphate
show the reaction diagram
-
mutant Y43G, aminoacylation assay
-
?
ATP + N-acetyl-L-tyrosine + tRNATyr
AMP + N-acetyl-L-Tyr-tRNATyr + diphosphate
show the reaction diagram
-
wild-type and mutant Y43G, aminoacylation assay
-
?
ATP + N-formyl-L-tyrosine + tRNATyr
AMP + N-formyl-L-Tyr-tRNATyr + diphosphate
show the reaction diagram
-
wild-type and mutant Y43G, aminoacylation assay
-
?
ATP + N-o-nitrophenylsulfenyl-L-tyrosine + tRNATyr
AMP + N-o-nitrophenylsulfenyl-L-Tyr-tRNATyr + diphosphate
show the reaction diagram
-
wild-type and mutant Y43G, aminoacylation assay
-
?
ATP + O-dansyl-L-tyrosine + tRNATyr
AMP + O-dansyl-L-Tyr-tRNATyr + diphosphate
show the reaction diagram
-
wild-type and mutant Y43G, aminoacylation assay
-
?
ATP + O-methyl-L-tyrosine + tRNATyr
AMP + O-methyl-L-Tyr-tRNATyr + diphosphate
show the reaction diagram
-, Q57834
-
-
?
ATP + O-methyl-L-tyrosine + tRNATyr
AMP + O-methyl-L-Tyr-tRNATyr + diphosphate
show the reaction diagram
-
wild-type and mutant Y43G, aminoacylation assay
-
?
ATP + O-phospho-L-tyrosine + tRNATyr
AMP + O-phospho-L-Tyr-tRNATyr + diphosphate
show the reaction diagram
-
wild-type and mutant Y43G, aminoacylation assay
-
?
ATP + p-acetyl-L-phenylalanine + tRNATyr
AMP + diphosphate + p-acetyl-L-phenylalanyl-tRNATyr
show the reaction diagram
-
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
show the reaction diagram
-
a variant of the Methanococcus jannaschii tyrosyl synthetase that selectively incorporates para-iodophenylalanine in response to an amber stop codon is identified
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
show the reaction diagram
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
show the reaction diagram
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
show the reaction diagram
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
show the reaction diagram
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
show the reaction diagram
-
-
-
-
-
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
show the reaction diagram
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
show the reaction diagram
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
show the reaction diagram
-
-
-
r
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
show the reaction diagram
-
-
-
-
-
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
show the reaction diagram
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
show the reaction diagram
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
show the reaction diagram
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
show the reaction diagram
-
-
-
r
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
show the reaction diagram
-
-
-
r
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
show the reaction diagram
-
-
-
-
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
show the reaction diagram
-
-
-
-
-
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
show the reaction diagram
-
r
-
-
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
show the reaction diagram
-
same affinity for tRNA or tRNA acylated with tyrosine
-
-
-
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
show the reaction diagram
-
K2ATP2- or Na2ATP2-
-
-
-
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
show the reaction diagram
-
Na2ATP2-, specific for tyrosine as amino acid
-
-
-
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
show the reaction diagram
-
phosphorothioate analogs of ATP
-
-
-
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
extreme high fidelity in charging the tRNA with an amino acid
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
tRNATyr substrate from Escherichia coli
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
show the reaction diagram
-
enzyme plays a key role in protein biosynthesis
-
?
ATP + tyrosine + tRNATyr
?
show the reaction diagram
-
-
-
-
-
additional information
?
-
-
no activity with tRNAAsp and tRNAPhe
-
?
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
?
-
-
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
?
-
Q5UPJ7
mimivirus aminoacyl-tRNA synthetases function as regular translation enzymes in infected amoebas
-
-
-
additional information
?
-
-
TyrRS deficiency is involved in the autosomal dominant intermediate Charcot-Marie-Tooth neuropathy type C disorder, overview
-
-
-
additional information
?
-
-
conformational flexibility of cytokine-like C-module of the enzyme
-
-
-
additional information
?
-
-
high degree of structural plasticity that is observed in these aminoacyl-tRNA synthetases, overview
-
-
-
additional information
?
-
P36421
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
-
-
-
additional information
?
-
-
two distinct conformational states of the active site in the three Leishmania major TyrRS structures
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + 3-(2-naphthyl)alanine + tRNATyr
AMP + diphosphate + 3-(2-naphthyl)alanyl-tRNATyr
show the reaction diagram
-
activity of a natural mutant enzyme, NpAla TyrRS activity
-
-
?
ATP + 4-acetylphenylalanine + tRNATyr
AMP + diphosphate + 4-acetylphenylalanyl-tRNATyr
show the reaction diagram
-
activity of a natural mutant enzyme
-
-
?
ATP + 4-bromophenylalanine + tRNATyr
AMP + diphosphate + 4-bromophenylalanyl-tRNATyr
show the reaction diagram
-
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
show the reaction diagram
-
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 + L-Tyr-tRNATyr + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
show the reaction diagram
-
-
-
r
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
show the reaction diagram
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
show the reaction diagram
-, Q57834
-
-
?
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
-
-
-
-
?
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
P54577
-
-
-
?
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
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
show the reaction diagram
P36421
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
show the reaction diagram
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
show the reaction diagram
-
wild-type activity
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
show the reaction diagram
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
show the reaction diagram
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
show the reaction diagram
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
show the reaction diagram
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
show the reaction diagram
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
show the reaction diagram
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
show the reaction diagram
-
-
-
r
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
show the reaction diagram
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
show the reaction diagram
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
show the reaction diagram
-
-
-
?
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
show the reaction diagram
-
-
-
r
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
show the reaction diagram
-
-
-
r
ATP + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
show the reaction diagram
-
enzyme plays a key role in protein biosynthesis
-
?
ATP + tyrosine + tRNATyr
?
show the reaction diagram
-
-
-
-
-
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
?
-
-
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
?
-
Q5UPJ7
mimivirus aminoacyl-tRNA synthetases function as regular translation enzymes in infected amoebas
-
-
-
additional information
?
-
-
TyrRS deficiency is involved in the autosomal dominant intermediate Charcot-Marie-Tooth neuropathy type C disorder, overview
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
K+
-
activation up to a concentration of 200 mM, sharp decrease above
K+
-
0.15 M activates 12fold
K+
-
absolute requirement, Km: 10 mM
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+
-
optimum at 6 mM
Mg2+
-
no requirement if spermine is present
Mg2+
-
10 mM, can be replaced by Mn2+ with equal efficiency and by Ca2+, Co2+, Sr2+, Ba2+, spermine with reduced efficiency
Mg2+
-
Km: 1 mM
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, shows regulatory function
Mg2+
-
required
Mg2+
-
required
Mg2+
-
required, MgATP2-
Mg2+
-
required
Mg2+
-
required
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
8
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3-(3,4-dichlorophenyl)-4-(2-(4-methylpiperazin-1-yl)ethoxy)furan-2(5H)-one
-
-
3-(3,4-difluorophenyl)-4-(2-(piperidin-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-(3-bromophenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
-
-
3-(3-chlorophenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
-
-
3-(3-hydroxyphenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
-
-
3-(3-methoxyphenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
-
-
3-(4-bromophenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
-
-
3-(4-chlorophenyl)-4-(2-morpholinoethoxy)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
3-(4-methoxyphenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
-
-
3-phenyl-4-(2-(piperidin-1-yl)ethoxy)furan-2(5H)-one
-
-
3-phenyl-4-(2-(propylamino)ethoxy)furan-2(5H)-one
-
-
3-phenyl-4-(2-(pyrrolidin-1-yl)ethoxy)furan-2(5H)-one
-
-
4-(2-(2-(4-nitrophenyl)hydrazinyl)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(4-methylpiperazin-1-yl)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(benzylamino)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(butylamino)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-(cyclohexylamino)ethoxy)-3-(3,4-dimethoxyphenyl)furan-2(5H)-one
-
-
4-(2-(cyclohexylamino)ethoxy)-3-phenylfuran-2(5H)-one
-
-
4-(2-morpholinoethoxy)-3-phenylfuran-2(5H)-one
-
-
-
6-Aminomethyladenosine triphosphate
-
-
AMP
-
inhibition is weakened by chloride
chloride
-
inhibition in presence of 1 mM free Mg2+, no inhibition in presence of 10 mM free Mg2+
diphosphate
-
inhibition is strengthened by chloride
fisetin
-
binding structure, overview
L-tyrosinyl 1,4-anhydro-D-ribitol-5-O-phosphate
-
-
L-tyrosinyl 1-beta-naphthyl-1,4-anhydro-D-ribitol-5-O-phosphate
-
-
L-tyrosinyl N6-benzoyl adenylate
-
-
L-tyrosinyl uridine-5'-O-phosphate
-
25% inhibition at 0.1 mM
L-tyrosinyl uridine-5'-O-phosphate
-
-
L-tyrosinyl-2',3'-O-isopropylidene adenylate
-
-
N-ethylmaleimide
-
-
O-(adenosine-5'-O-yl) N-(L-tyrosyl)phosphoramidate
P36421
i.e. Tyr-AMPN, a non-hydrolyzable Tyr-AMP analog, binding structure, overview
sulfate
-
inhibition in presence of 1 mM free Mg2+
tyrosinol
-
binding structure, overview
-
tyrosyl aryl dipeptides
-
inhibitor interacts with and occupies the key catalytic residues in the tyrosyl binding pocket of the catalytic site
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
-
enzyme-inhibitor complexes
-
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
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2.04
-
3-chloro-L-tyrosine
-
pH 7.6, 30C, wild-type enzyme
2.43
-
3-chloro-L-tyrosine
-
pH 7.6, 30C, mutant Y43G
0.625
-
3-fluoro-D,L-tyrosine
-
pH 7.6, 30C, wild-type enzyme
1.3
-
3-fluoro-D,L-tyrosine
-
pH 7.6, 30C, mutant Y43G
0.13
-
3-iodo-L-tyrosine
-
pH 7.6, 37C, mutant Y73V/Q195C
1.15
-
3-iodo-L-tyrosine
-
pH 7.6, 30C, mutant Y43G
1.6
-
A22G mutated tRNATyr transcript
-
-
-
0.04
-
ATP
-
-
0.049
-
ATP
-
cytoplasm
0.07
-
ATP
-
phosphate exchange reaction, pH 8.0, wild-type enzyme
0.13
-
ATP
-
aminoacylation reaction, pH 8.0, wild-type enzyme
0.21
-
ATP
-
chloroplasts
0.217
-
ATP
-
ATP-diphosphate exchange reaction
1
0.5
-
ATP
-
ATP-diphosphate exchange reaction
1.7
-
ATP
-
ATP-diphosphate exchange reaction
1
2
-
ATP
-
mutant M55L, pH 7.8, 25C
2.1
-
ATP
-
wild-type enzyme, pH 7.8, 25C
2.4
-
ATP
-
mutant I52L, pH 7.8, 25C
2.7
-
ATP
-
mutant L105V, pH 7.8, 25C
3
-
ATP
-
pH 7.5, 25C, mutant S225A and mutant K231A
4
-
ATP
-
pH 7.5, 25C, wild-type enzyme and mutant S224A
4.1
-
ATP
-
pH 7.5, 25C, mutant S226A
0.46
-
D-tyrosine
-
pH 7.6, 30C, wild-type enzyme
14
-
D-tyrosine
-
pH 7.6, 30C, mutant Y43G
0.8
-
G15A mutated tRNATyr transcript
-
-
-
22
-
K+
-
pH 7.5, 25C, mutant S226A
24
-
K+
-
pH 7.5, 25C, mutant S224A
30
-
K+
-
pH 7.5, 25C, mutant S225A
32
-
K+
-
pH 7.5, 25C, wild-type enzyme
0.56
-
L-3,4-dihydroxyphenylalanine
-
pH 7.6, 30C, mutant Y43G
1.84
-
L-3,4-dihydroxyphenylalanine
-
pH 7.6, 30C, wild-type enzyme
0.018
-
L-beta-(5-hydroxy-2-pyridyl)-alanine
-
wild-type enzyme, pH 7.5, 30C
0.038
-
L-beta-(5-hydroxy-2-pyridyl)-alanine
-
mutant F130S, pH 7.5, 30C
0.0003
-
L-tyrosine
-
30C, purified recombinant His-tagged enzyme
0.0014
-
L-tyrosine
-
mutant M55L, pH 7.8, 25C
0.0015
-
L-tyrosine
-
mutant TyrRS, KMGCA
0.0018
-
L-tyrosine
-
mutant I52L, pH 7.8, 25C
0.0021
-
L-tyrosine
-
wild-type enzyme and mutant L105V, pH 7.8, 25C
0.0033
-
L-tyrosine
-
wild-type enzyme, pH 7.5, 30C
0.0043
-
L-tyrosine
-
mutant TyrRS, RMSSS; wild-type TyrRS, KMSSS
0.0044
-
L-tyrosine
-
mutant TyrRS, AMSSS
0.0049
-
L-tyrosine
-
chloroplasts
0.0053
-
L-tyrosine
-
pH 7.6, 37C, wild-type enzyme
0.0068
-
L-tyrosine
-
cytoplasm
0.012
-
L-tyrosine
-
pH 7.6, 30C, wild-type enzyme, radioisotopic assay
0.014
-
L-tyrosine
-
pH 7.6, 30C, wild-type enzyme, spectrophotometric assay
0.021
-
L-tyrosine
-
phosphate exchange reaction, pH 8.0, wild-type enzyme
0.021
-
L-tyrosine
-
pH 7.5, 25C, mutant S225A
0.027
-
L-tyrosine
-
aminoacylation reaction, pH 8.0, wild-type enzyme
0.03
-
L-tyrosine
-
pH 7.5, 25C, mutant K231A
0.034
-
L-tyrosine
-
pH 7.5, 25C, wild-type enzyme
0.042
-
L-tyrosine
-
pH 7.5, 25C, mutant S226A
0.05
-
L-tyrosine
-
pH 7.5, 25C, mutant S224A
0.066
-
L-tyrosine
-
mutant F130S, pH 7.5, 30C
0.14
-
L-tyrosine
-
pH 7.6, 37C, mutant Y73V/Q195C
0.002
-
native yeast tRNATyr
-
pH 7.5, 30C
-
2.2e-05
-
tRNATyr
-
chloroplasts
2.2e-05
-
tRNATyr
-
in absence of KCl, pH 7.4, 30C
3.7e-05
-
tRNATyr
-
in presence of 50 mM KCl, pH 7.4, 30C
8.98e-05
-
tRNATyr
-
cytoplasm
9.3e-05
-
tRNATyr
-
in presence of 100 mM KCl, pH 7.4, 30C
0.00014
-
tRNATyr
-
-
1
0.00024
-
tRNATyr
-
in presence of 150 mM KCl, pH 7.4, 30C
0.0003
-
tRNATyr
-
-
0.00035
-
tRNATyr
-
-
0.00052
-
tRNATyr
-
acylation
0.00052
-
tRNATyr
Q9Y2Z4
pH 7.6, 37C, native Escherichia coli tRNATyr
0.0009
-
tRNATyr
-
30C, purified recombinant His-tagged enzyme
0.0025
-
tRNATyr
-
aminoacylation reaction, pH 8.0, wild-type enzyme
0.0048
-
tRNATyr
Q9Y2Z4
pH 7.6, 37C, human mitochondrial tRNATyr
4.8
-
tRNATyr
-
-
0.0015
-
tRNYTyr
-
-
-
0.002
-
tyrosine
-
-
0.0033
-
tyrosine
-
-
0.008
-
tyrosine
-
acylation
0.012
-
tyrosine
-
ATP-diphosphate exchange reaction
0.013
-
tyrosine
-
ATP-diphosphate exchange reaction and aminoacylation
1
0.0002
-
tyrosyl-tRNATyr
-
deacylation
-
2.2
-
U54C mutated tRNATyr transcript
-
-
-
1.19
-
L-tyrosine
-
pH 7.6, 30C, mutant Y43G
additional information
-
additional information
-
kinetics
-
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
-
kinetics
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
role of a mobile loop, corresponding to KMSKS signature sequence in catalytic mechanism
-
additional information
-
additional information
-
values for mutant strains
-
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
-
kinetics
-
additional information
-
additional information
-
mutants
-
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
Q5UPJ7
kinetics with Escherichia coli tRNATyr, Plasmodium falciparum tRNATyr, and diverse wild-type and mutant Saccharomyces cerevisiae tRNATyrs, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.13
-
3-chloro-L-tyrosine
-
pH 7.6, 30C, wild-type enzyme
1.46
-
3-chloro-L-tyrosine
-
pH 7.6, 30C, mutant Y43G
6.08
-
3-chloro-L-tyrosine
-
pH 7.6, 30C, mutant Y43G
0.62
-
3-fluoro-D,L-tyrosine
-
pH 7.6, 30C, mutant Y43G
3.3
-
3-fluoro-D,L-tyrosine
-
pH 7.6, 30C, wild-type enzyme
4.96
-
3-fluoro-D,L-tyrosine
-
pH 7.6, 30C, wild-type enzyme
6.08
-
3-fluoro-D,L-tyrosine
-
pH 7.6, 30C, mutant Y43G
0.43
-
3-iodo-L-tyrosine
-
pH 7.6, 37C, mutant Y73V/Q195C
0.48
-
3-iodo-L-tyrosine
-
pH 7.6, 30C, mutant Y43G
3e-05
-
A22G mutated tRNATyr transcript
-
-
-
3.3
-
ATP
-
phosphate exchange reaction, pH 8.0, wild-type enzyme
4.6
-
ATP
-
mutant M55L, pH 7.8, 25C
5.29
-
ATP
-
phosphate exchange reaction, pH 8.0, wild-type enzyme
6.8
-
ATP
-
mutant I52L, pH 7.8, 25C
7.7
-
ATP
-
aminoacylation reaction, pH 8.0, wild-type enzyme
7.7
-
ATP
-
wild-type enzyme, pH 7.8, 25C
12
-
ATP
-
mutant L105V, pH 7.8, 25C
0.37
-
D-tyrosine
-
pH 7.6, 30C, mutant Y43G
1.2
-
D-tyrosine
-
pH 7.6, 30C, wild-type enzyme
0.0002
-
G15A mutated tRNATyr transcript
-
-
-
0.67
-
L-3,4-dihydroxyphenylalanine
-
pH 7.6, 30C, mutant Y43G
1.65
-
L-3,4-dihydroxyphenylalanine
-
pH 7.6, 30C, wild-type enzyme
6.08
-
L-3,4-dihydroxyphenylalanine
-
pH 7.6, 30C, mutant Y43G
0.042
-
L-beta-(5-hydroxy-2-pyridyl)-alanine
-
mutant F130S, pH 7.5, 30C
0.11
-
L-beta-(5-hydroxy-2-pyridyl)-alanine
-
wild-type enzyme, pH 7.5, 30C
0.01
-
L-tyrosine
-
mutant TyrRS, RMSSS
0.012
-
L-tyrosine
-
mutant TyrRS, AMSSS
0.025
-
L-tyrosine
-
mutant TyrRS, KMGCA
0.045
-
L-tyrosine
-
pH 7.6, 37C, mutant Y73V/Q195C
0.53
-
L-tyrosine
-
wild-type TyrRS, KMSSS
0.74
-
L-tyrosine
-
wild-type enzyme, pH 7.5, 30C
0.78
-
L-tyrosine
-
pH 7.5, 25C, mutant S226A
0.95
-
L-tyrosine
-
pH 7.6, 30C, mutant Y43G
1.4
-
L-tyrosine
-
mutant F130S, pH 7.5, 30C
1.49
-
L-tyrosine
-
30C, purified recombinant His-tagged enzyme
2.5
-
L-tyrosine
-
mutant M55L, pH 7.8, 25C
3.3
-
L-tyrosine
-
phosphate exchange reaction, pH 8.0, wild-type enzyme
3.6
-
L-tyrosine
-
mutant I52L, pH 7.8, 25C
4.4
-
L-tyrosine
-
pH 7.6, 30C, wild-type enzyme, radioisotopic assay
4.6
-
L-tyrosine
-
pH 7.6, 30C, wild-type enzyme, spectrophotometric assay
4.9
-
L-tyrosine
-
mutant L105V, pH 7.8, 25C
5.29
-
L-tyrosine
-
phosphate exchange reaction, pH 8.0, wild-type enzyme
5.4
-
L-tyrosine
-
wild-type enzyme, pH 7.8, 25C
6
-
L-tyrosine
-
pH 7.5, 25C, mutant S224A
6.08
-
L-tyrosine
-
wild-type enzyme, pH 7.5, 30C
6.08
-
L-tyrosine
-
pH 7.5, 25C, mutant S226A
6.08
-
L-tyrosine
-
30C, purified recombinant His-tagged enzyme
7.7
-
L-tyrosine
-
aminoacylation reaction, pH 8.0, wild-type enzyme
12
-
L-tyrosine
-
pH 7.6, 37C, wild-type enzyme
30
-
L-tyrosine
-
pH 7.5, 25C, mutant K231A
31
-
L-tyrosine
-
pH 7.5, 25C, mutant S225A
1.5
-
native yeast tRNATyr
-
pH 7.5, 30C
-
0.046
-
tRNATyr
-
-
6.08
-
tRNATyr
-
-
0.012
-
U54C mutated tRNATyr transcript
-
-
-
45
-
L-tyrosine
-
pH 7.5, 25C, wild-type enzyme
additional information
-
additional information
-
influence of assay conditions, kcat for diverse tRNA variants, overview
-
additional information
-
additional information
-
mutants
-
additional information
-
additional information
-
the C-terminal His-tag of the recombinant enzyme has little effect on the catalytic activity
-
additional information
-
additional information
Q9Y2Z4
-
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.32
-
AMP
-
in absence of KCl, and in presence of 1 mM free Mg2+, pH 7.4, 30C
0.35
-
AMP
-
in absence of KCl, pH 7.4, 30C
0.5
-
AMP
-
in presence of 0.5 mM KCl, pH 7.4, 30C
0.5
-
AMP
-
in presence of 50 mM KCl, and in presence of 1 mM free Mg2+, pH 7.4, 30C
0.9
-
AMP
-
in presence of 0.9 mM KCl, pH 7.4, 30C
2.15
-
AMP
-
in presence of 150 mM KCl, and in presence of 1 mM free Mg2+, pH 7.4, 30C
0.048
-
diphosphate
-
in presence of 150 mM KCl, and in presence of 1 mM free Mg2+, pH 7.4, 30C
0.056
-
diphosphate
-
in presence of 0.9 mM KCl, pH 7.4, 30C
0.1
-
diphosphate
-
in presence of 50 mM KCl, and in presence of 1 mM free Mg2+, pH 7.4, 30C
0.12
-
diphosphate
-
in presence of 0.5 mM KCl, pH 7.4, 30C
0.14
-
diphosphate
-
in absence of KCl, pH 7.4, 30C
0.23
-
diphosphate
-
in absence of KCl, and in presence of 1 mM free Mg2+, pH 7.4, 30C
0.076
-
L-tyrosinyl 1,4-anhydro-D-ribitol-5-O-phosphate
-
pH 7.9, 37C
0.42
-
L-tyrosinyl 1,4-anhydro-D-ribitol-5-O-phosphate
-
pH 7.9, 37C
0.0057
-
L-tyrosinyl 1-beta-naphthyl-1,4-anhydro-D-ribitol-5-O-phosphate
-
pH 7.9, 37C
0.15
-
L-tyrosinyl 1-beta-naphthyl-1,4-anhydro-D-ribitol-5-O-phosphate
-
pH 7.9, 37C
1.1e-05
-
L-tyrosinyl adenylate
-
pH 7.9, 37C
0.00068
-
L-tyrosinyl N6-benzoyl adenylate
-
pH 7.9, 37C
0.00021
-
L-tyrosinyl uridine-5'-O-phosphate
-
pH 7.9, 37C
9.3e-06
-
L-tyrosinyl-2',3'-O-isopropylidene adenylate
-
pH 7.9, 37C
2.6e-05
-
L-tyrosinyl-2',3'-O-isopropylidene adenylate
-
pH 7.9, 37C
0.018
-
L-tyrosinyl-2'-deoxy adenylate
-
pH 7.9, 37C
0.1
-
L-tyrosinyl-2'-deoxy adenylate
-
pH 7.9, 37C
0.036
-
L-tyrosinyl-3'-deoxy adenylate
-
pH 7.9, 37C
6.3e-06
-
tyrosinyl adenylate
-
pH 7.9, 37C
0.14
-
L-tyrosinyl-3'-deoxy adenylate
-
pH 7.9, 37C
additional information
-
additional information
-
inhibition kinetics
-
additional information
-
additional information
-
-
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.1
-
3-(3,4-dichlorophenyl)-4-(2-(4-methylpiperazin-1-yl)ethoxy)furan-2(5H)-one
-
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
-
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
-
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
-
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
-
pH not specified in the publication, temperature not specified in the publication
0.0205
-
3-(3-chlorophenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
-
pH not specified in the publication, temperature not specified in the publication
0.0256
-
3-(3-hydroxyphenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
-
pH not specified in the publication, temperature not specified in the publication
0.0375
-
3-(3-methoxyphenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
-
pH not specified in the publication, temperature not specified in the publication
0.0024
-
3-(4-bromophenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
-
pH not specified in the publication, temperature not specified in the publication
0.00062
-
3-(4-chlorophenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
-
pH not specified in the publication, temperature not specified in the publication
0.0001
-
3-(4-hydroxyphenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
-
pH not specified in the publication, temperature not specified in the publication
0.0328
-
3-(4-methoxyphenyl)-4-(2-morpholinoethoxy)furan-2(5H)-one
-
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
-
pH not specified in the publication, temperature not specified in the publication
0.0291
-
3-phenyl-4-(2-(propylamino)ethoxy)furan-2(5H)-one
-
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
-
pH not specified in the publication, temperature not specified in the publication
0.1
-
4-(2-(2-(4-nitrophenyl)hydrazinyl)ethoxy)-3-phenylfuran-2(5H)-one
-
above, pH not specified in the publication, temperature not specified in the publication
0.0086
-
4-(2-(4-methylpiperazin-1-yl)ethoxy)-3-phenylfuran-2(5H)-one
-
pH not specified in the publication, temperature not specified in the publication
0.1
-
4-(2-(benzylamino)ethoxy)-3-phenylfuran-2(5H)-one
-
above, pH not specified in the publication, temperature not specified in the publication
0.0719
-
4-(2-(butylamino)ethoxy)-3-phenylfuran-2(5H)-one
-
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
-
above, pH not specified in the publication, temperature not specified in the publication
0.0874
-
4-(2-(cyclohexylamino)ethoxy)-3-phenylfuran-2(5H)-one
-
pH not specified in the publication, temperature not specified in the publication
0.0062
-
4-(2-morpholinoethoxy)-3-phenylfuran-2(5H)-one
-
pH not specified in the publication, temperature not specified in the publication
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.6e-06
-
-
purified recombinant His-tagged enzyme
1.8
-
-
purified enzyme
18.35
-
-
-
1
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
Q5UPJ7
activity with Escherichia coli tRNATyr, Plasmodium falciparum tRNATyr, and diverse wild-type and mutant Saccharomyces cerevisiae tRNATyrs, overview
additional information
-
-
enzymatic activity is shown
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)
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.7
-
-
aminoacylation
1
7.5
9
-
ATP-diphosphate exchange reaction
1
7.5
9
-
-
7.5
-
-
assay at
7.5
-
-
assay at
7.5
-
P54577
aminoacylation assay
7.5
-
-
tyrosylation assay
7.6
-
-
assay at
7.6
-
-
assay at
7.6
-
-
assay at
7.7
8
-
kinetic assays
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.2
8.5
-
less than 50% of maximal activity above and below
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
-
P54577
aminoacylation assay at room temperature
25
-
-
assay at
30
-
-
assay at
30
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
tyrosylation assay
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
a model is proposed, in which the KMSKS signature sequence is conformationally constrained and unable to participate in catalysis below 25C
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.8
-
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
lung cancer giant-cell strain
Manually annotated by BRENDA team
-
bovine aortic endothelial cells
Manually annotated by BRENDA team
-
mini-TyrRS is reduced in extracts of ischemic calf muscle and in thoracic aorta explants exposed to hypoxia or VEGF
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
e.g. primary embryonic motor neurons
Manually annotated by BRENDA team
additional information
-
YARS is expressed ubiquitously, in neuronal cells making extensions, the enzyme is located at outgrowth behaving like an early polarity maker, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
axonal termini in differentiating primary motor neuron and neuroblastoma cultures
Manually annotated by BRENDA team
Q9Y2Z4
human mitochondrial and cytosolic enzymes are encoded by two different sets of genes
Manually annotated by BRENDA team
-
the mt-TyrRS is strictly mitochondrial, mitochondrial idiosyncrasies
Manually annotated by BRENDA team
additional information
-
the C-terminal EMAP II-like protein domain of the enzyme is probably responsible for mediation of enzyme export
-
Manually annotated by BRENDA team
additional information
-
subcellular localization of wild-type and mutant YARS, overview
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
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)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
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)
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)
Staphylococcus aureus (strain Newman)
Staphylococcus aureus (strain Newman)
Staphylococcus aureus (strain Newman)
Staphylococcus aureus (strain Newman)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
38000
-
-
calculation from sequence of tyrZ gene
38800
40300
-
sedimentation equilibrium centrifugation
43000
46500
-
sedimentation equilibrium centrifugation
43000
-
-
Western blot
50000
-
-
synthetase T1, gel filtration
70000
-
-
synthetase T2, gel filtration
90000
-
-
sucrose density gradient centrifugation
95000
-
-
gel filtration
97000
-
-
PAGE
100000
-
-
gel filtration
105000
-
-
recombinant His-tagged enzyme, gel filtration
110000
-
-
gel filtration
120000
-
-
gel filtration
130000
-
Q9Y2Z4
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
-
2 * 55000, SDS-PAGE
dimer
-
2 * 47000, SDS-PAGE
dimer
-
2 * 40000-45000, identical, sequence of tryptic peptides, SDS-PAGE
dimer
-
1 * 62000 + 1 * 62000, nonidentical, Factor A, role unclear + Factor B, responsible for the activation of tyrosine, SDS-PAGE
dimer
-
2 * 48000, recombinant His-tagged enzyme, SDS-PAGE
dimer
-
2 * 58000, SDS-PAGE
dimer
Q9Y2Z4
2 * 51302, calculation from amino acid sequence
dimer
Q5UPJ7
dimer interface structure from crystal structure analysis, modeling, overview
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
-
three-dimensional structures of subunits A and B, modelling, overview
dimer
-
binding of substrates alters the structure of the subunits
6, 7
monomer
-
1 * 40000, SDS-PAGE
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
-
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
-
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
P36421
structural comparison of TyrRS of different origin, overview
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
-
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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
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
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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, 25C, 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
Q5UPJ7
crystal of SeMet-substituted TyrRS is obtained by the microbatch method, using an automatic crystallization robot. The crystals are grown at 20C 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
-, Q9YA64
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
-, O29482
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
-
electron density map, X-ray structure
-
3
quarternary structure
-
4
X-ray diffraction, at 2.7 A resolution, structure analysis of the enzyme-ligand complex, e.g. with specific synthetic inhibitors, molecular modeling
-
-
P54577
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 20C or 4C, 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
-
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
O58739, -
crystal structure at 2.3 A resolution
-
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 100mM Tris buffer at pH 7.5, X-ray diffraction structure determination and analysis at 2.4 A resolution
P36421
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
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
68.5
-
-
wild-type enzyme shows 50% inactivation after 27 min
additional information
-
-
effects of mutations and of coupling of mutations on thermal parameters and stability, overview
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
stable to immediate freezing and thawing, but not for longer periods, no stabilization by potassium borohydrite, MgCl2, ATP, Vitamin B12
-
Tyrosine and/or ATP stabilize
-
dilution has denaturing effect
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-15C, rapid loss of activity, 0.05 M GSH plus 0.005 M EDTA stabilizes
-
-20C, 4 months stable
-
-20C, 0.025 M potassium phosphate buffer, pH 6.7, 0.01 M 2-mercaptoethanol, 50% glycerol, no loss of activity in 6 months
-
4C, 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
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant HIs-tagged enzyme from overexpression in Escherichia coli strain JM105
-
using Ni-NTA chromatography
-
recombinant TyrRSfrom Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
using Ni-NTA chromatography
-
synthetase 1-3
-
recombinant C-terminal domain from Escherichia coli strain BL21(DE3) by cation exchange chromatography and gel filtration
-
using Ni-NTA chromatography
-
catalytic domain (residues 1-322)
-
recombinant His-tagged wild-type and mutant enzymes from strain BL21(DE3)
-
recombinant HIs-tagged wild-type and mutant F130S from strain JM109
-
on a Source 15Q-Sepharose anion-exchange column
-
wild-type and mutant enzymes
-
-
Q9Y2Z4
by utilizing the His-tag
-
recombinant His-Tagged enzyme form Escherichia coli strain BL21(DE3), removal of the N-terminal His-tag
-
recombinant His-tagged enzyme from Escherichia coli strain BL21, 4.2fold
-
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
-
recombinant wild-type and mutant His-tagged enzymes
-
by chromatography on Ni-nitrilotriacetic acid agarose
-
recombinant C-terminally His6-tagged tyrosyl aminoacyl-tRNA synthetase from Escherichia coli by nickel affinity and ion exchange chromatography to homogeneity
-
by ammonium sulfate precipitation and on a heparin-Sepharose column
-
mutant DELTA424-669
-
synthetase T1 and T2
-
recombinant His-tagged wild-type and mutant Y43G enzyme from Escherichia coli Y43G
-
recombinant truncated enzyme SceTyrRS comprising residues 1-364
P36421
recombinant enzyme to near homogeneity
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
Q5UPJ7
gene tyrZ, overexpression of the HIs-tagged enzyme in Escherichia coli strain JM105
-
expressed in Escherichia coli as a His-tagged fusion protein
-
expression in Escherichia coli strain BL21(DE3)
-
expressed in Escherichia coli as a His-tagged fusion protein
-
into the pUAST transformation vector
-
expressed in Escherichia coli as a His-tagged fusion protein
-
expression of C-terminal domain of TyrRS in Escherichia coli strain BL21(DE3)
-
catalytic domain (residues 1-322)
-
gene tyrS, expression of wild-type and mutant enzymes as His-tagged proteins in strain JM109
-
into the vectors pACYC184 and pAp102
-
overexpression of His-tagged wild-type and mutants in strain BL21(DE3)
-
for expression in Escherichia coli TG2 cells
-
gene tyrS, overexpression of wild-type and mutant enzymes from phage M13-BY(DELTA1) in Escherichia coli strains RZ1032 and TG2
-
wild-type and mutants into the phagemid pYTS5-WT
-
DNA and amino acid sequence determination of wild-type and mutant enzymes, localization of the gene encoding the enzyme on chromosome 1p34-p35, functional complementation of a Saccharomyces cerevisiae TYS1 mutant strain, overview, transient expression of EGFP-tagged wild-type and mutant enzymes in murine neuroblastoma N2a cells
-
expression of His-tagged full-length wild-type and truncated mutant enzymes in Escherichia coli
-
expression of the enzyme as His-tagged protein in Escherichia coli strain BL21(DE3)
-
expression of wild-type and mutant enzymes as His-tagged proteins in Escherichia coli
-
gene TyrS, DNA sequence determination, overexpression as His-tagged enzyme in Escherichia coli BL21
-
mutant human mini-TyrRS constructs are generated using QuikChange site-directed mutagenesis kit and using a plasmid encoding the gene for wild-type human mini-TyrRS as the template for PCR mutagenesis reactions, all proteins are expressed with a C-terminal His-tag to facilitate purification
P54577
overexpression in Escherichia coli
Q9Y2Z4
gene structure and motifs in double-length TyrRS homologues, phylogenetic comparison
-
a library of more than 200 mutants substituting the ATP binding motif KMSSS, Lys204-Met205-Ser206-Ser207-Ser208, is built, mutants and wild-type of MjYRS are cloned into the vector pET41a+
-
DNA and amino acid sequence determination and analysis of two enzymes types, expression of tyrosyl aminoacyl-tRNA synthetase as C-terminally His6-tagged enzyme in Escherichia coli
-
expressed in Escherichia coli
-
into the vectors pACYC184 and pAp102
-
CYT-18 is expressed from the plasmid pEX560 in the Escherichia coli strain HMS174DE3
-
into the TOPO TA cloning vector for sequencing
-
expression of truncated enzyme SceTyrRS comprising residues 1-364
P36421
into the single copy plasmid YCplac111
-
into the vectors pACYC184 and pAp102
-
overexpression of His-tagged wild-type and mutant Y43G enzyme in Escherichia coli BL21(DE3)
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
high glucose significantly decreases mRNA expression of tyrosyl-tRNA synthetase
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
H306A
-
no complementation of the thermosensitive Escherichia coli tyrS mutant HB2109, 3fold decrease in kcat for amino acid activation
H306D
-
no complementation of the thermosensitive Escherichia coli tyrS mutant HB2109
H53A
-
no complementation of the thermosensitive Escherichia coli tyrS mutant HB2109, inactive
K395N
-
slight complementation of the thermosensitive Escherichia coli tyrS mutant HB2109, 17fold increase in Km for Escherichia coli tRNATyr, reduced activity
S356A
-
no complementation of the thermosensitive Escherichia coli tyrS mutant HB2109, 7fold increase in Km for Escherichia coli tRNATyr, reduced activity
E91N
-
mutation of the ELR motif: mutant protein does not induce phosphorylation of VEGFR2, suggesting that the ELR motif in mini-TyrRS has an important role in transactivation of VEGFR2
L92Y
-
mutation of the ELR motif: mutant protein does not induce phosphorylation of VEGFR2, suggesting that the ELR motif in mini-TyrRS has an important role in transactivation of VEGFR2
F130S
-
construction of a plasmid library of randomly mutated gene tyrS by PCR, isolation of a mutant R-6-A-7 which incorporates L-beta-(5-hydroxy-2-pyridyl)-alanine in transformed Escherichia coli cells in vivo, increased temperature instability
Q179A
-
site-directed mutagenesis, reduced activity with L-tyrosine, no activity with 3-iodo-L-tyrosine
Q179E
-
inactive mutant
Q179N
-
site-directed mutagenesis, reduced activity with L-tyrosine, no activity with 3-iodo-L-tyrosine
Q179S
-
site-directed mutagenesis, reduced activity with L-tyrosine, no activity with 3-iodo-L-tyrosine
Q179Y
-
inactive mutant
Q195A
-
site-directed mutagenesis, active with L-tyrosine, low activity with 3-iodo-L-tyrosine
Q195C
-
site-directed mutagenesis, reduced activity with L-tyrosine, low activity with 3-iodo-L-tyrosine
Q195D
-
site-directed mutagenesis, highly reduced activity with L-tyrosine, low activity with 3-iodo-L-tyrosine
Q195E
-
site-directed mutagenesis, active with L-tyrosine, no activity with 3-iodo-L-tyrosine
Q195F
-
inactive mutant
Q195G
-
site-directed mutagenesis, reduced activity with L-tyrosine, no activity with 3-iodo-L-tyrosine
Q195H
-
site-directed mutagenesis, active with L-tyrosine, no activity with 3-iodo-L-tyrosine
Q195I
-
site-directed mutagenesis, highly reduced activity with L-tyrosine, no activity with 3-iodo-L-tyrosine
Q195K
-
inactive mutant
Q195L
-
site-directed mutagenesis, reduced activity with L-tyrosine, no activity with 3-iodo-L-tyrosine
Q195M
-
site-directed mutagenesis, highly reduced activity with L-tyrosine, no activity with 3-iodo-L-tyrosine
Q195N
-
site-directed mutagenesis, reduced activity with L-tyrosine, low activity with 3-iodo-L-tyrosine
Q195R
-
inactive mutant
Q195S
-
site-directed mutagenesis, active with L-tyrosine, low activity with 3-iodo-L-tyrosine
Q195T
-
site-directed mutagenesis, active with L-tyrosine, no activity with 3-iodo-L-tyrosine
Q195V
-
site-directed mutagenesis, reduced activity with L-tyrosine, no activity with 3-iodo-L-tyrosine
Q195W
-
inactive mutant
Q195Y
-
site-directed mutagenesis, reduced activity with L-tyrosine, no activity with 3-iodo-L-tyrosine
Y37A/Q195A
-
inactive mutant
Y37A/Q195C
-
site-directed mutagenesis, active with L-tyrosine and 3-iodo-L-tyrosine, preference for the latter, reduced overall activity
Y37A/Q195N
-
inactive mutant
Y37A/Q195S
-
site-directed mutagenesis, equally low activity with L-tyrosine and 3-iodo-L-tyrosine
Y37I/Q195A
-
site-directed mutagenesis, equally low activity with L-tyrosine and 3-iodo-L-tyrosine
Y37I/Q195C
-
inactive mutant
Y37I/Q195N
-
inactive mutant
Y37I/Q195S
-
inactive mutant
Y37L/Q195A
-
site-directed mutagenesis, highly reduced activity with L-tyrosine, no activity with 3-iodo-L-tyrosine
Y37L/Q195C
-
site-directed mutagenesis, equally low activity with L-tyrosine and 3-iodo-L-tyrosine
Y37L/Q195N
-
site-directed mutagenesis, highly reduced activity with L-tyrosine, no activity with 3-iodo-L-tyrosine
Y37L/Q195S
-
inactive mutant
Y37V/Q195N
-
site-directed mutagenesis, active with L-tyrosine and 3-iodo-L-tyrosine, preference for the latter, reduced overall activity
Y37V/Q195S
-
site-directed mutagenesis, reduced activity with L-tyrosine and 3-iodo-L-tyrosine
Y73A
-
site-directed mutagenesis, equally active with L-tyrosine and 3-iodo-L-tyrosine
Y73F
-
site-directed mutagenesis, active with L-tyrosine, no activity with 3-iodo-L-tyrosine
Y73G
-
site-directed mutagenesis, equally active with L-tyrosine and 3-iodo-L-tyrosine, reduced overall activity
Y73H
-
site-directed mutagenesis, active with L-tyrosine, and slightly active with 3-iodo-L-tyrosine
Y73I
-
site-directed mutagenesis, active with L-tyrosine and 3-iodo-L-tyrosine, preference for the latter
Y73L
-
site-directed mutagenesis, equally active with L-tyrosine and 3-iodo-L-tyrosine
Y73M
-
site-directed mutagenesis, equally active with L-tyrosine and 3-iodo-L-tyrosine
Y73S
-
site-directed mutagenesis, active with L-tyrosine and 3-iodo-L-tyrosine, preference for the first
Y73V
-
site-directed mutagenesis, equally active with L-tyrosine and 3-iodo-L-tyrosine
Y73V/Q195A
-
site-directed mutagenesis, active with L-tyrosine and 3-iodo-L-tyrosine, preference for the latter, reduced overall activity
Y73V/Q195C
-
site-directed mutagenesis, 10fold more active with 3-iodo-L-tyrosine than with L-tyrosine, reduced overall activity
C35G
-
crystal structure of mutants Cys to Gly35 and Tyr to Phe34
D194A
-
site-directed mutagenesis, mutation does not affect the initial binding of the tRNATyr substrate, it does not destabilize the transition state complex for the second reaction step
D78A
-
site-directed mutagenesis, mutation does not affect the initial binding of the tRNATyr substrate, it does not destabilize the transition state complex for the second reaction step
I52L
-
unaltered enzyme activity in the diphosphate exchange reaction, decreased kinetic stability at 68.5C compared to the wild-type, compensates mutation L105V partially, destabilized association between subunits
K233A
-
mutant shows a reduced affinity for ATP
L105V
-
unaltered enzyme activity in the diphosphate exchange reaction, decreased kinetic stability at 68.5C compared to the wild-type, destabilization of the monomeric intermediate of unfolding, mutation can be partially compensated by mutation I52L
Q173A
-
site-directed mutagenesis, mutation does not affect the initial binding of the tRNATyr substrate, it destabilizes the transition state complex for the second reaction step
Q195A
-
site-directed mutagenesis, mutation does not affect the initial binding of the tRNATyr substrate, it does not destabilize the transition state complex for the second reaction step
T234A
-
decrease of the forward rate constant by 540fold, 3fold increase in affinity of the enzyme for ATP
T34F
-
crystal structure of mutants Cys to Gly35 and Tyr to Phe34
T51P
-
increased enzyme activity in the diphosphate exchange reaction, decreased kinetic stability at 68.5C compared to the wild-type, slightly destalized mutant
Y169A
-
site-directed mutagenesis, mutation does not affect the initial binding of the tRNATyr substrate, it does not destabilize the transition state complex for the second reaction step
E196K
-
naturally occuring mutation in the autosomal dominant intermediate Charcot-Marie-Tooth neuropathy type C disorder, the mutant enzyme shows reduced activity and specific distribution in the cell compared to the wild-type enzyme, no functional complementation of a Saccharomyces cerevisiae TYS1 mutant strain, the mutant shows altered distribution in neuronal cells compared to the wild-type enzyme when recombinantly expressed
G41R
-
naturally occuring mutation in the autosomal dominant intermediate Charcot-Marie-Tooth neuropathy type C disorder, the mutant enzyme shows reduced activity and specific distribution in the cell compared to the wild-type enzyme, partial functional complementation of a Saccharomyces cerevisiae TYS1 mutant strain, the mutant shows altered distribution in neuronal cells compared to the wild-type enzyme when recombinantly expressed
K231A
-
site-directed mutagenesis, no effect on the catalytic activity of the enzyme
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
mini-TyrRS_D173A
P54577
binding pocket variant, retains cytokine function
mini-TyrRS_TyrRS(ELQ)
P54577
the surface helix encodes an ELR motif that functions like the ELR tripeptide in CXC cytokines, substitution of Arg93 to generate ELQ
mini-TyrRS_TyrRS(EYR)
P54577
the surface helix encodes an ELR motif that functions like the ELR tripeptide in CXC cytokines, substitution of Leu92 to generate EYR
mini-TyrRS_TyrRS(NLR)
P54577
the surface helix encodes an ELR motif that functions like the ELR tripeptide in CXC cytokines, substitution of Glu91 to generate NLR
mini-TyrRS_Y39A
P54577
binding pocket variant, retains cytokine function
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
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
S224A
-
site-directed mutagenesis, 7.5fold decrease of the forward rate constant
S225A
-
site-directed mutagenesis, no effect on the catalytic activity of the enzyme
S226A
-
site-directed mutagenesis, 60fold decrease of the forward rate constant
TyrRS_153-156delVKQV
-
dominant-intermediate Charcot-Marie-Tooth neuropathy associated mutation
TyrRS_E196K
-
dominant-intermediate Charcot-Marie-Tooth neuropathy associated mutation
TyrRS_G41R
-
dominant-intermediate Charcot-Marie-Tooth neuropathy associated mutation
AMSSS
-
TyrRS mutant, a library of more than 200 mutants substituting the ATP binding motif KMSSS is built
RMSSS
-
TyrRS mutant, a library of more than 200 mutants substituting the ATP binding motif KMSSS is built
Y32Q/D158A
-
site-directed mutagenesis, enzyme mutant discriminates between L-tyrosine and O-methyl-L-tyrosine, with a high activity only with the latter
Y43G
-
broadened amino acid substrate specificity
YARS_153-156delVKQV
-
dominant-intermediate Charcot-Marie-Tooth neuropathy associated mutation
YARS_E196K
-
dominant-intermediate Charcot-Marie-Tooth neuropathy associated mutation
YARS_G41R
-
dominant-intermediate Charcot-Marie-Tooth neuropathy associated mutation
R93Q
-
mutation of the ELR motif: mutant protein does not induce phosphorylation of VEGFR2, suggesting that the ELR motif in mini-TyrRS has an important role in transactivation of VEGFR2
additional information
-
interaction analysis of deletion and truncation mutants, overview
M55L
-
increase in kinetic stability at 68.5C compared to the wild-type, mutation is not coupled to others in its effects, slightly increased kinetic stability at 68.5C
additional information
-
kinetic properties ATP-diphosphate exchange reacion of engineered mutants
additional information
-
altered specificity for amino acid
additional information
-
effects of coupling of mutations on thermal stability
mini-TyrRS_Y39A/D173A
P54577
binding pocket variant, retains cytokine function
additional information
-
disrupted function and axonal distribution of the mutant enzyme in autosomal dominant intermediate Charcot-Marie-Tooth neuropathy type C, a common disorder of the peripheral nervous system, caused by demyelination or axonal degeneration or a combination of both, mutant families analysis, mutation analysis, phenotype, overview
KMGCA
-
TyrRS mutant, a library of more than 200 mutants substituting the ATP binding motif KMSSS is built
additional information
-
computational design of possible mutants with altered substrate specificity by prediction of the binding structure and calculation of binding energies of mutants to amino acids, overview
additional information
-
structural comparison of wild-type enzye and naturally occuring mutant variant p-BrPhe TyrRSs, the latter shows an altered substrate specificity charging 4-bromophenylalanine, 3-(2-naphthyl)alanine, or 4-acetylphenylalanine, overview
additional information
-
60 aminoacyl-tRNA synthetases are modeled using the conformation of Methanococcus jannaschii tRNATyr/tyrosyl-tRNA synthetase as template
additional information
-
the Escherichia coli TyrRS-tRNATyr pair is functionally replaced by the Methanocaldococcus jannaschii tyrosine pair
additional information
-
development of a one-plasmid expression system encoding an inducible modified tyrosyl-tRNA synthetase, the orthogonal cognate suppressor tRNA, and eGFPUAG in an individually regulatable fashion, overview. Assessment of the system for the incorporation of a non-natural amino acid yielding a fluorescent readout. Mutant library construction by random mutagenesis, and selection for O-methyl-L-tyrosine-specific mutant variants
Y32Q/D158A/L162P/D286R
-
The engineered enzyme is improved with specificity for O-methyl-L-tyrosine and 10fold improved incorporation. The optimized synthetase is used for the preparative expression of a modified uvGFP carrying MeTyr at position 66 as part of its fluorophore. This biosynthetic protein shows quantitative incorporation of the non-natural amino acid, The Asp286Arg mutation serves for improved recognition of the CUA anticodon
additional information
-
mutation of the ELR-motif to EYR abolishes the effect on ischemic angiogenesis, leukocyte recruitment, and vascular permeability
additional information
-
construction of diverse tRNA variants of the native tRNATyr from yeast by heterologous in vitro translation, transplantation and point mutations
additional information
P36421
construction of a chemically truncated enzyme comprising residues 1-364, termed SceTyrRS
additional information
-
the Escherichia coli TyrRS-tRNATyr pair is functionally replaced by the Saccharomyces cerevisiae tyrosine pair
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
it is shown that mini-TyrRS is exported from endothelial cells when they are treated with tumor necrosis factor-alpha. Mini-TyrRS binds to vascular endothelial cells and activates an array of angiogenic signal transduction pathways. Mini-TyrRS-induces angiogenesis requires the activation of VEGF receptor-2. Mini-TyrRS stimulates VEGFR2 phosphorylation in a VEGF-independent manner, suggesting VEGFR2 transactivation
medicine
-
dominant-intermediate Charcot-Marie-Tooth neuropathy, DI-CMT, is characterized by axonal degeneration and demyelination of peripheral motor and sensory neurons, three dominant mutations in the YARS gene, encoding tyrosyl-tRNA synthetase, have so far been associated with DI-CMT type C
biotechnology
-
site-specific incorporation of 3-iodo-L-tyrosine into proteins in a cell-free system for use in specialized in vitro translation systems
biotechnology
-
the present engineering allows Escherichia coli TyrRS variants for non-natural amino acids to be developed in Escherichia coli, for use in both eukaryotic and bacterial cells for genetic code expansion
medicine
-
enzyme inhibitors can be used as antibacterial agents
medicine
P54577
some mammalian synthetases develop cytokine functions possibly linked to disease-causing mutations in tRNA synthetases
medicine
-
dominant-intermediate Charcot-Marie-Tooth neuropathy, DI-CMT, is characterized by axonal degeneration and demyelination of peripheral motor and sensory neurons, three dominant mutations in the YARS gene, encoding tyrosyl-tRNA synthetase, have so far been associated with DI-CMT type C
pharmacology
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design of antimicrobials that target the bacterial enzyme of Bacillus stearothermophilus making use of the differences between the actives sites of the 2 enzymes
biotechnology
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incorporation of unusual specific amino acids into proteins in in vitro translation systems by mutant enzyme with altered substrate specificity. e.g. mutant Y32Q/D158A
biotechnology
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Escherichia coli-based cell-free system for the production of proteins with a non-natural amino acid incorporated site-specifically is described. A mutant Methanococcus jannaschii tyrosyl-tRNA synthetase (mTyrRS) and tRNATyr pair are used as orthogonal elements. The mTyrRS experienced proteolysis and modified protein yields improves with higher synthetase addition (200-300 mg/mL)
biotechnology
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a mutant Methanococcus jannaschii tyrosyl amber suppressor tRNA, Tyr MjtRNA CUR/tyrosyl-tRNA synthetase (MjTyrRS) pair is developed to uniquely incorporate phenylselenocysteine in response to the amber TAG codon in Escherichia coli. After being efficiently converted into dehydroalanine under mild conditions, Michael addition reactions with the corresponding thiols can be used to synthesize N-methyl- and N-acetyl-lysine analogues
biotechnology
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a rapid, straightforward, one plasmid dual positive/negative selection system for the evolution of aminoacyl-tRNA synthetases with altered specifities in Escherichia coli is developed
biotechnology
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the present engineering allows Escherichia coli TyrRS variants for non-natural amino acids to be developed in Escherichia coli, for use in both eukaryotic and bacterial cells for genetic code expansion
medicine
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high-dose mini-TyrRS (600 microgram/kg/day) augments while low-dose mini-TyrRS (3 microgram/kg/day), inhibits angiogenesis in the ischemic mouse ear. Enhanced angiogenesis is associated with increased CD45- and CD4-positive leukocyte accumulation. Mini-TyrRS also has biphasic actions on both basal and mustard oil-evoked and VEGF-evoked leakage of Evan's blue dye-albumin in nonischemic ear and in endothelial cell monolayers, that is, low-dose inhibited and high-dose augmented leakage. Mini-TyrRS has dose-dependent biphasic effects on ischemic angiogenesis and vascular permeability in vivo, that is, antiangiogenic and antipermeability activities at low concentration and proangiogenic, propermeability activities at high concentrations
medicine
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it has been suggested that bone metabolism disorders are one of the major complications of diabetes mellitus, glucose could affect bone metabolism by regulating the expression of tyrosyl-tRNA synthetase genes
biotechnology
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use of mutant Y43G for specialized protein synthesis as a carrier for additional amino acids and derivatives for use in e.g. crystal structure determination by X-ray diffraction
biotechnology
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the present engineering allows Escherichia coli TyrRS variants for non-natural amino acids to be developed in Escherichia coli, for use in both eukaryotic and bacterial cells for genetic code expansion
medicine
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enzyme inhibitors can be used as antibacterial agents
pharmacology
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design of antimicrobial agents against Staphylococcus aureus, largely responsible for hospital-acquired infections, on the basis of knowledge of the crystal structure and the revealed catalytic mechanism