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Information on EC 6.1.1.1 - tyrosine-tRNA ligase
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EC Tree
6.1.1.1 tyrosine-tRNA ligaseSpecify your search results
Word Map
- 6.1.1.1
- synthetases
- aminoacylation
-
tyrosylation
- stearothermophilus
-
amber
-
anticodon
- neurospora
- trprs
- jannaschii
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tryptophanyl-trna
-
kmsks
- methanococcus
-
aarss
-
trna-like
-
anticodon-binding
-
tyrts
- d-tyrosine
-
half-of-the-sites
- biotechnology
-
charcot-marie-tooth
- medicine
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non-cognate
- methanocaldococcus
- elr
- methionyl-trna
-
self-splicing
- phenylalanyl-trna
-
brome
-
sideroblastic
-
isoleucyl-trna
-
misacylation
- pharmacology
-
mischarging
-
fersht
- 3-iodo-l-tyrosine
- drug development
The enzyme appears in viruses and cellular organisms
Synonyms
CHOTyrRS, class I tyrosyl-tRNA synthetase, CYT-18, CYT-18 protein, dTyRS, hTyrRS, LdTyrRS, LMJF_14_1370, mini-tyrosyl-tRNA synthetase, mini-TyrRS, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
class I tyrosyl-tRNA synthetase
CYT-18
LdTyrRS
mitochondrial tyrosyl-tRNA synthetase
mtTyrRS
tRNATyr/tyrosyl-tRNA synthetase
Tyrosine translase
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Tyrosine tRNA synthetase
Tyrosine--tRNA ligase
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Tyrosine-transfer ribonucleate synthetase
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Tyrosine-transfer RNA ligase
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tyrosyl tRNA synthetase
Tyrosyl--tRNA ligase
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Tyrosyl-transfer ribonucleate synthetase
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Tyrosyl-transfer ribonucleic acid synthetase
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Tyrosyl-transfer RNA synthetase
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Tyrosyl-tRNA ligase
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Tyrosyl-tRNA synthetase
TyrRS
TyrRSs
YRS
YTS
class I tyrosyl-tRNA synthetase
Methanocaldococcus jannaschii TCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440
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CYT-18
bifunctional, aminoacylates mitochondrial tRNATyr and promotes the splicing of mitochondrial group I introns
mtTyrRS
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bifunctional mitochondrial tyrosyl-tRNA synthetase (CYT-18 protein) both aminoacylates mitochondrial tRNATyr and acts as a structure-stabilizing splicing cofactor for group I introns
mtTyrRS
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bifunctional mitochondrial tyrosyl-tRNA synthetase (CYT-18 protein) both aminoacylates mitochondrial tRNATyr and acts as a structure-stabilizing splicing cofactor for group I introns
mtTyrRS
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bifunctional mitochondrial tyrosyl-tRNA synthetase (CYT-18 protein) both aminoacylates mitochondrial tRNATyr and acts as a structure-stabilizing splicing cofactor for group I introns
Tyrosine tRNA synthetase
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Tyrosyl-tRNA synthetase
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Tyrosyl-tRNA synthetase
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Tyrosyl-tRNA synthetase
Methanocaldococcus jannaschii TCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440
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Tyrosyl-tRNA synthetase
Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1
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Tyrosyl-tRNA synthetase
Pyrococcus horikoshii ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3
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TyrRS
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TyrRS
Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr
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ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr
mechanism
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ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr
mechanism
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ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr
amino acid residues Y37 and Q195 are involved in substrate specificity determination
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ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr
mechanism, class I enzyme has a class II mode of cognate tRNA recognition
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ATP + L-tyrosine + tRNATyr = AMP + diphosphate + L-tyrosyl-tRNATyr
mechanism, residues Asp78, Tyr169, Gln173, Asp194, and Gln195 are involved in catalysis
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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
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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
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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
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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
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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
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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
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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
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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acylation
esterification
Acylation
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esterification
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
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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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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
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mutant Y43G, aminoacylation assay
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?
ATP + 3-azido-L-tyrosine + tRNATyr
AMP + 3-azido-L-Tyr-tRNATyr + diphosphate
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mutant Y43G, aminoacylation assay
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?
ATP + 3-chloro-L-tyrosine + tRNATyr
AMP + 3-chloro-L-Tyr-tRNATyr + diphosphate
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mutant Y43G, aminoacylation assay
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?
ATP + 3-iodo-L-tyrosine + tRNATyr
AMP + 3-iodo-L-Tyr-tRNATyr + diphosphate
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mutant Y43G, aminoacylation assay
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?
ATP + 3-iodo-L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
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mutant Y73V/Q195C and other mutants, no activity with the wild-type enzyme
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?
ATP + 3-methoxy-L-tyrosine + tRNATyr
AMP + 3-methoxy-L-Tyr-tRNATyr + diphosphate
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mutant Y43G, aminoacylation assay
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?
ATP + 3-nitro-L-tyrosine + tRNATyr
AMP + 3-nitro-L-Tyr-tRNATyr + diphosphate
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mutant Y43G, aminoacylation assay
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?
ATP + D-3,4-dihydroxyphenylalanine + tRNATyr
AMP + D-3,4-dihydroxyphenylalanine-tRNATyr + diphosphate
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mutant Y43G, aminoacylation assay
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?
ATP + D-tyrosine + tRNATyr
AMP + D-Tyr-tRNATyr + diphosphate
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mutant Y43G, aminoacylation assay
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?
ATP + D-tyrosine + tRNATyr
AMP + diphosphate + D-tyrosyl-tRNATyr
enzyme TyrRS has a detectable, natural activity for the D-tyrosine stereoisomer, only tenfold less than for L-Tyr
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?
ATP + L-3,4-dihydroxyphenylalanine + tRNATyr
AMP + L-3,4-dihydroxyphenylalanine-tRNATyr + diphosphate
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mutant Y43G, aminoacylation assay
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?
ATP + L-beta-(5-hydroxy-2-pyridyl)-alanine + tRNATyr
AMP + L-beta-(5-hydroxy-2-pyridyl)-alanine-tRNATyr + diphosphate
ATP + L-tyrosine + native yeast tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
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?
ATP + L-tyrosine + tRNATyrGTA
AMP + diphosphate + L-tyrosyl-tRNATyrGTA
two sequences, tRNATyr1 and tRNATyr2, substrate CHO tRNATyrGTA is recombinantly expressed. CHOTyrRS is able to attach Phe to both tRNATyr2 and CHO total tRNA containing native tRNATyr, excluding the possibility that mischarging results from the lack of post-transcriptional modifications to the in vitro-transcribed substrate
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?
ATP + m-fluoro-D,L-tyrosine + tRNATyr
AMP + m-fluoro-D,L-Tyr-tRNATyr + diphosphate
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mutant Y43G, aminoacylation assay
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?
ATP + N-acetyl-L-tyrosine + tRNATyr
AMP + N-acetyl-L-Tyr-tRNATyr + diphosphate
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wild-type and mutant Y43G, aminoacylation assay
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?
ATP + N-formyl-L-tyrosine + tRNATyr
AMP + N-formyl-L-Tyr-tRNATyr + diphosphate
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wild-type and mutant Y43G, aminoacylation assay
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?
ATP + N-o-nitrophenylsulfenyl-L-tyrosine + tRNATyr
AMP + N-o-nitrophenylsulfenyl-L-Tyr-tRNATyr + diphosphate
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wild-type and mutant Y43G, aminoacylation assay
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?
ATP + O-dansyl-L-tyrosine + tRNATyr
AMP + O-dansyl-L-Tyr-tRNATyr + diphosphate
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wild-type and mutant Y43G, aminoacylation assay
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?
ATP + O-phospho-L-tyrosine + tRNATyr
AMP + O-phospho-L-Tyr-tRNATyr + diphosphate
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wild-type and mutant Y43G, aminoacylation assay
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?
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
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-
?
ATP + p-iodophenylalanine + tRNATyr
AMP + diphosphate + p-iodophenylalanyl-tRNATyr
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a variant of the Methanococcus jannaschii tyrosyl synthetase that selectively incorporates para-iodophenylalanine in response to an amber stop codon is identified
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?
ATP + 3-(2-naphthyl)alanine + tRNATyr
AMP + diphosphate + 3-(2-naphthyl)alanyl-tRNATyr
activity of a natural mutant enzyme, NpAla TyrRS activity
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-
?
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
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?
ATP + 3-azido-L-tyrosine + tRNATyr
AMP + diphosphate + 3-azido-L-tyrosyl-tRNATyr
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-
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?
ATP + 3-azido-L-tyrosine + tRNATyr
AMP + diphosphate + 3-azido-L-tyrosyl-tRNATyr
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-
-
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?
ATP + 3-azido-L-tyrosine + tRNATyr
AMP + diphosphate + 3-azido-L-tyrosyl-tRNATyr
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?
ATP + 3-iodo-L-tyrosine + tRNATyr
AMP + diphosphate + 3-iodo-L-tyrosyl-tRNATyr
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-
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?
ATP + 3-iodo-L-tyrosine + tRNATyr
AMP + diphosphate + 3-iodo-L-tyrosyl-tRNATyr
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-
-
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?
ATP + 3-iodo-L-tyrosine + tRNATyr
AMP + diphosphate + 3-iodo-L-tyrosyl-tRNATyr
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-
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?
ATP + 4-acetylphenylalanine + tRNATyr
AMP + diphosphate + 4-acetylphenylalanyl-tRNATyr
activity of a natural mutant enzyme
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?
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
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?
ATP + 4-bromophenylalanine + tRNATyr
AMP + diphosphate + 4-bromophenylalanyl-tRNATyr
activity of a natural mutant enzyme, p-BrPhe TyrRS activity
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?
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
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?
ATP + L-beta-(5-hydroxy-2-pyridyl)-alanine + tRNATyr
AMP + L-beta-(5-hydroxy-2-pyridyl)-alanine-tRNATyr + diphosphate
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L-beta-(5-hydroxy-2-pyridyl)-alanine i.e. azatyrosine, mutant F130S, and wild-type enzyme the latter showing low activity
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?
ATP + L-beta-(5-hydroxy-2-pyridyl)-alanine + tRNATyr
AMP + L-beta-(5-hydroxy-2-pyridyl)-alanine-tRNATyr + diphosphate
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L-beta-(5-hydroxy-2-pyridyl)-alanine i.e. azatyrosine, mutant F130S shows 17fold higher activity in vivo than the wild-type enzyme
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?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
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-
-
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?
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
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-
?
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
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-
?
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
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-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
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-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
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-
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?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
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-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
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-
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?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
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-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
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-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
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-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
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-
-
-
?
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
Methanocaldococcus jannaschii TCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440
-
-
-
?
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
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
?
-
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 presence of the C-terminal EMAP II-domain has no effect on the recognition of cognate Tyr and discrimination against noncognate Phe
-
-
?
additional information
?
-
-
the presence of the C-terminal EMAP II-domain has no effect on the recognition of cognate Tyr and discrimination against noncognate Phe
-
-
?
additional information
?
-
residues Asp81, Tyr175, Gln179, and Gln201 coordinate the ammonium group of the L-Tyr ligand
-
-
?
additional information
?
-
-
residues Asp81, Tyr175, Gln179, and Gln201 coordinate the ammonium group of the L-Tyr ligand
-
-
?
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
?
-
-
recombinant hTyrRS also synthesizes kyotorphin from tyrosine, arginine, and ATP, cf. EC 6.3.2.24
-
-
?
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
?
-
enzyme TyrRS has a detectable, natural, tRNA-acylation activity for the D-tyrosine stereoisomer, being capable of charging D-Tyr onto tRNATyr to form D-Tyr-tRNA instead of the usual L-Tyr-tRNA
-
-
?
additional information
?
-
-
enzyme TyrRS has a detectable, natural, tRNA-acylation activity for the D-tyrosine stereoisomer, being capable of charging D-Tyr onto tRNATyr to form D-Tyr-tRNA instead of the usual L-Tyr-tRNA
-
-
?
additional information
?
-
Methanocaldococcus jannaschii TCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440
enzyme TyrRS has a detectable, natural, tRNA-acylation activity for the D-tyrosine stereoisomer, being capable of charging D-Tyr onto tRNATyr to form D-Tyr-tRNA instead of the usual L-Tyr-tRNA
-
-
?
additional information
?
-
enzyme MtTyrRS is incapable of cross-recognition and aminoacylation of human cytoplasmic tRNATyr
-
-
?
additional information
?
-
-
enzyme MtTyrRS is incapable of cross-recognition and aminoacylation of human cytoplasmic tRNATyr
-
-
?
additional information
?
-
enzyme MtTyrRS is incapable of cross-recognition and aminoacylation of human cytoplasmic tRNATyr
-
-
?
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
-
-
?
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
-
-
?
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NATURAL SUBSTRATE
NATURAL 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-(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
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
-
-
-
-
?
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
-
-
-
?
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
Methanocaldococcus jannaschii TCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440
-
-
-
?
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 + L-Tyr-tRNATyr + diphosphate
-
-
?
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
?
-
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
?
-
enzyme MtTyrRS is incapable of cross-recognition and aminoacylation of human cytoplasmic tRNATyr
-
-
?
additional information
?
-
-
enzyme MtTyrRS is incapable of cross-recognition and aminoacylation of human cytoplasmic tRNATyr
-
-
?
additional information
?
-
enzyme MtTyrRS is incapable of cross-recognition and aminoacylation of human cytoplasmic tRNATyr
-
-
?
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+
-
activates the wild-type enzyme and mutants S225A and K231A, no interaction with the KMSSS motif
K+
-
dependent on, required for catalysis of the tyrosine activation step, 260fold increase of the froward reaction constant
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+
-
required, shows regulatory function, binding of 1 Mg2+ per tRNA molecule for the transfer reaction, binding to the tRNA is weakened by chloride
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.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-[4-[([4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl]oxy)carbonyl]phenyl]dibroman-1-ium
-
-
-
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
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 2-bromobenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 2-chlorobenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 2-chloropyridine-3-carboxylate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 2-fluorobenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 2-methoxybenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 2-methylbenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 2-nitrobenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-(3-methylphenyl)propanoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-(4-methylphenyl)propanoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-aminobenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-bromobenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-chlorobenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-fluorobenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-hydroxybenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-methylbenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-phenylpropanoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 4-aminobenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 4-chlorobenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 4-fluorobenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 4-hydroxybenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 4-methylbenzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 6-chloropyridine-3-carboxylate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 6-hydroxypyridine-3-carboxylate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl benzoate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl pyridine-3-carboxylate
-
-
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl pyridine-4-carboxylate
-
-
5'-O-[N-(L-tyrosyl)sulfamoyl]adenosine
-
i.e. TyrSA, a tyrosyl adenylate analogue,. TyrSA is engaged in many interactions with active site residues occupying the tyrosine and adenine binding pockets. Residues making hydrogen bonds with the TyrSA tyrosyl group in the tyrosine binding pocket (YBP) are Y36, Y163, Q167, D170 and Q185. Residues G38, A72 and F75 are responsible for the hydrophobic interactions between enzyme and tyrosine moiety in the YBP
O-(adenosine-5'-O-yl) N-(L-tyrosyl)phosphoramidate
i.e. Tyr-AMPN, a non-hydrolyzable Tyr-AMP analog, binding structure, overview
resveratrol
inhibits the enzyme activity and the growth of promastigotes
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+
fisetin
inhibits the enzyme activity and the growth of promastigotes
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
natural compounds as inhibitors of tyrosyl-tRNA synthetase, effects of various polyphenols, alkaloids, and terpenes-secondary metabolites produced by higher plants, overview. Most of them act as competitive inhibitors. Structure-activity relationship shows that the most potent flavonoid inhibitors contain hydroxyl group at position 5 and 7 of A ring and a -OCH3 group at position 4' of B ring
-
additional information
-
natural compounds as inhibitors of tyrosyl-tRNA synthetase, effects of various polyphenols, alkaloids, and terpenes-secondary metabolites produced by higher plants, overview. Most of them act as competitive inhibitors. Structure-activity relationship shows that the most potent flavonoid inhibitors contain hydroxyl group at position 5 and 7 of A ring and a -OCH3 group at position 4' of B ring
-
additional information
-
LdTyrRS specific nanobodies are generated in Lama glama. Nanobodies are the variable domains of camelid heavy chain-only antibodies. The nanobody NbA makes numerous crystal contacts and in addition reduces the flexibility of a loop of LdTyrRS. NbA is cloned in the pMESy4 vector that carries the pelB sequence coding for the secretion signal peptide of PelB and is expressed as His-tagged protein in Escherichia coli for subsequent purification from the bacterial periplasm by affinity chromatography and gel filtration. 4 anti-LdTyrRS nanobodies are tested as crystallization chaperones, crystallization and structure analysis and modeling, overview
-
additional information
natural compounds as inhibitors of tyrosyl-tRNA synthetase, effects of various polyphenols, alkaloids, and terpenes-secondary metabolites produced by higher plants, overview. Most of them act as competitive inhibitors. Structure-activity relationship shows that the most potent flavonoid inhibitors contain hydroxyl group at position 5 and 7 of A ring and a -OCH3 group at position 4' of B ring
-
additional information
-
natural compounds as inhibitors of tyrosyl-tRNA synthetase, effects of various polyphenols, alkaloids, and terpenes-secondary metabolites produced by higher plants, overview. Most of them act as competitive inhibitors. Structure-activity relationship shows that the most potent flavonoid inhibitors contain hydroxyl group at position 5 and 7 of A ring and a -OCH3 group at position 4' of B ring
-
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
-
additional information
-
synthesis and evaluation of new tyrosyl-tRNA synthetase inhibitors as antibacterial agents based on a N2-(arylacetyl)glycinanilide scaffold, molecular docking study, antimicrobial activity, overview
-
additional information
-
synthesis and evaluation of a series of novel 4-hydroxy-3-(naphthalen-1-ylmethyl)thiophen-2(5H)-ones as tyrosyl-tRNA synthetase inhibitors, molecular docking, structure-activity relationships, overview
-
additional information
-
natural compounds as inhibitors of tyrosyl-tRNA synthetase, effects of various polyphenols, alkaloids, and terpenes-secondary metabolites produced by higher plants, overview. Most of them act as competitive inhibitors. Structure-activity relationship shows that the most potent flavonoid inhibitors contain hydroxyl group at position 5 and 7 of A ring and a -OCH3 group at position 4' of B ring
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Acidosis, Lactic
A novel homozygous YARS2 mutation causes severe myopathy, lactic acidosis, and sideroblastic anemia 2.
Acidosis, Lactic
A novel mutation in YARS2 causes myopathy with lactic acidosis and sideroblastic anemia.
Acidosis, Lactic
Mutation of the mitochondrial tyrosyl-tRNA synthetase gene, YARS2, causes myopathy, lactic acidosis, and sideroblastic anemia--MLASA syndrome.
Acidosis, Lactic
Phenotypic variability and identification of novel YARS2 mutations in YARS2 mitochondrial myopathy, lactic acidosis and sideroblastic anaemia.
Anemia, Sideroblastic
A novel homozygous YARS2 mutation causes severe myopathy, lactic acidosis, and sideroblastic anemia 2.
Anemia, Sideroblastic
A novel mutation in YARS2 causes myopathy with lactic acidosis and sideroblastic anemia.
Anemia, Sideroblastic
Phenotypic variability and identification of novel YARS2 mutations in YARS2 mitochondrial myopathy, lactic acidosis and sideroblastic anaemia.
Asthma
Association analysis of DTD1 gene variations with aspirin-intolerance in asthmatics.
Deafness
Contribution of a mitochondrial tyrosyl-tRNA synthetase mutation to the phenotypic expression of the deafness-associated tRNASer(UCN) 7511A>G mutation.
Extensively Drug-Resistant Tuberculosis
Identification of an anti-TB compound targeting the tyrosyl-tRNA synthetase.
Infections
Crystal structure of Staphylococcus aureus tyrosyl-tRNA synthetase in complex with a class of potent and specific inhibitors.
Leishmaniasis
Twin Attributes of Tyrosyl-tRNA Synthetase of Leishmania donovani: A HOUSEKEEPING PROTEIN TRANSLATION ENZYME AND A MIMIC OF HOST CHEMOKINE.
Malaria
Malaria parasite tyrosyl-tRNA synthetase secretion triggers pro-inflammatory responses.
Mitochondrial Diseases
A novel homozygous YARS2 mutation causes severe myopathy, lactic acidosis, and sideroblastic anemia 2.
Muscular Diseases
A novel homozygous YARS2 mutation causes severe myopathy, lactic acidosis, and sideroblastic anemia 2.
Muscular Diseases
A novel mutation in YARS2 causes myopathy with lactic acidosis and sideroblastic anemia.
Muscular Diseases
Mutation of the mitochondrial tyrosyl-tRNA synthetase gene, YARS2, causes myopathy, lactic acidosis, and sideroblastic anemia--MLASA syndrome.
Muscular Diseases
Phenotypic variability and identification of novel YARS2 mutations in YARS2 mitochondrial myopathy, lactic acidosis and sideroblastic anaemia.
Myocardial Infarction
Different angiogenesis effect of mini-TyrRS/mini-TrpRS by systemic administration of modified siRNAs in rats with acute myocardial infarction.
Myocardial Infarction
Effect of mini-tyrosyl-tRNA synthetase/mini-tryptophanyl-tRNA synthetase on ischemic angiogenesis in rats: proliferation and migration of endothelial cells.
Myocardial Infarction
Natural aminoacyl tRNA synthetase fragment enhances cardiac function after myocardial infarction.
Neoplasms
The novel fragment of tyrosyl tRNA synthetase, mini-TyrRS, is secreted to induce an angiogenic response in endothelial cells.
Parasitic Diseases
Leishmania donovani tyrosyl-tRNA synthetase structure in complex with a tyrosyl adenylate analog and comparisons with human and protozoan counterparts.
Starvation
Confirmation of the antibacterial mode of action of SB-219383, a novel tyrosyl tRNA synthetase inhibitor from a Micromonospora sp.
Thrombocytopenia
Tyrosyl-tRNA synthetase stimulates thrombopoietin-independent hematopoiesis accelerating recovery from thrombocytopenia.
Tuberculosis
Structural states of the flexible catalytic loop of M. tuberculosis tyrosyl-tRNA synthetase in different enzyme-substrate complexes.
Tuberculosis
[A model of three-dimensional structure of Mycobacterium tuberculosis tyrosyl-tRNA synthetase]
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00043
ATP
pH 7.2, 37°C, Tyr activation activity, recombinant wild-type enzyme
0.00045
ATP
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 144AcK
0.00049
ATP
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 355AcK
0.00071
ATP
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 235AcK
0.00223
ATP
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 85AcK
0.07
ATP
-
phosphate exchange reaction, pH 8.0, wild-type enzyme
0.018
L-beta-(5-hydroxy-2-pyridyl)-alanine
-
wild-type enzyme, pH 7.5, 30°C
0.0021
L-tyrosine
-
wild-type enzyme and mutant L105V, pH 7.8, 25°C
0.00669
L-tyrosine
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 355AcK
0.00678
L-tyrosine
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 85AcK
0.00713
L-tyrosine
pH 7.2, 37°C, Tyr activation activity, recombinant wild-type enzyme
0.00728
L-tyrosine
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 144AcK
0.00845
L-tyrosine
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 235AcK
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
wild type enzyme, at 55°C, in 100 mM HEPES-NaOH (pH 8.0), 10 mM MgCl2, 10 mM KCl
0.00037
tRNATyr
pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant wild-type enzyme
0.00042
tRNATyr
pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant lysine acetylated enzyme mutant 144AcK
0.00045
tRNATyr
pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant lysine acetylated enzyme mutant 85AcK
0.00048
tRNATyr
pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant lysine acetylated enzyme mutant 355AcK
0.0025
tRNATyr
-
aminoacylation reaction, pH 8.0, wild-type enzyme
0.00068
tRNATyr(G34C)
37°C, pH 7.5, mutant enzyme D268R
-
0.00035
tRNATyr(wild-type)
37°C, pH 7.5, wild-type enzyme
-
0.0014
tRNATyr(wild-type)
37°C, pH 7.5, mutant enzyme D268R
-
additional information
additional information
-
role of a mobile loop, corresponding to KMSKS signature sequence in catalytic mechanism
-
additional information
additional information
-
role of threonine 234 in catalysis
-
additional information
additional information
-
kinetic analysis of mutation
-
additional information
additional information
-
role of lysine 233 in catalysis
-
additional information
additional information
-
stoichiometry of substrate binding
-
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
-
fluorescence emission measurement for determination of steady-state kinetics for the His-tagged and the non-His-tagged recombinant enzyme
-
additional information
additional information
-
kinetics, influence of assay conditions, Km 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
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
-
additional information
additional information
kinetic parameters for anticodon mutants of tRNATyr and for for acceptor stem mutants of tRNATyr
-
additional information
additional information
calculation of the L-Tyr/D-Tyr binding free energy difference. Michaelis-Menten kinetics of wild-type and mutant enzymes
-
additional information
additional information
-
calculation of the L-Tyr/D-Tyr binding free energy difference. Michaelis-Menten kinetics of wild-type and mutant enzymes
-
additional information
additional information
Michaelis-Menten steady-state kinetics. Steady-state kinetic constants for ATP-[32P]PPi exchange for CHO cytosolic full length wild-type and variant TyrRS
-
additional information
additional information
-
Michaelis-Menten steady-state kinetics. Steady-state kinetic constants for ATP-[32P]PPi exchange for CHO cytosolic full length wild-type and variant TyrRS
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1
ATP
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 235AcK
2
ATP
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 85AcK
3.3
ATP
-
phosphate exchange reaction, pH 8.0, wild-type enzyme
5.29
ATP
-
phosphate exchange reaction, pH 8.0, wild-type enzyme
11.9
ATP
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 355AcK
12.3
ATP
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 144AcK
14.2
ATP
pH 7.2, 37°C, Tyr activation activity, recombinant wild-type enzyme
0.1
L-tyrosine
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 235AcK
2
L-tyrosine
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 85AcK
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
11.9
L-tyrosine
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 355AcK
12.3
L-tyrosine
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 144AcK
14.2
L-tyrosine
pH 7.2, 37°C, Tyr activation activity, recombinant wild-type enzyme
0.15
tRNATyr
pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant lysine acetylated enzyme mutant 85AcK
0.29
tRNATyr
wild type enzyme, at 55°C, in 100 mM HEPES-NaOH (pH 8.0), 10 mM MgCl2, 10 mM KCl
1.09
tRNATyr
pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant lysine acetylated enzyme mutant 355AcK
1.17
tRNATyr
pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant lysine acetylated enzyme mutant 144AcK
1.32
tRNATyr
pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant wild-type enzyme
0.079
tRNATyr(G34C)
37°C, pH 7.5, mutant enzyme D268R
-
0.12
tRNATyr(wild-type)
37°C, pH 7.5, mutant enzyme D268R
-
0.19
tRNATyr(wild-type)
37°C, pH 7.5, wild-type enzyme
-
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
-
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
140
ATP
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 235AcK
900
ATP
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 85AcK
24290
ATP
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 355AcK
27330
ATP
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 144AcK
33020
ATP
pH 7.2, 37°C, Tyr activation activity, recombinant wild-type enzyme
10
L-tyrosine
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 235AcK
93.75
L-tyrosine
recombinant truncated mutant enzyme, pH 7.8, 25°C
290
L-tyrosine
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 85AcK
1570
L-tyrosine
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 144AcK
1780
L-tyrosine
pH 7.2, 37°C, Tyr activation activity, recombinant lysine acetylated enzyme mutant 355AcK
1990
L-tyrosine
pH 7.2, 37°C, Tyr activation activity, recombinant wild-type enzyme
0.33
tRNATyr
pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant lysine acetylated enzyme mutant 85AcK
2.27
tRNATyr
pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant lysine acetylated enzyme mutant 355AcK
2.78
tRNATyr
pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant lysine acetylated enzyme mutant 144AcK
3.51
tRNATyr
pH 7.2, 37°C, tRNATyr aminoacylation activity, recombinant wild-type enzyme
1300
tRNATyr
wild type enzyme, at 55°C, in 100 mM HEPES-NaOH (pH 8.0), 10 mM MgCl2, 10 mM KCl
additional information
additional information
-
kinetic parameters for anticodon mutants of tRNATyr and for for acceptor stem mutants of tRNATyr
-
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.
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
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.05117
1-[4-[([4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl]oxy)carbonyl]phenyl]dibroman-1-ium
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
-
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
0.1
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 2-bromobenzoate
Staphylococcus aureus
-
above, pH 7.9, 37°C, recombinant enzyme
0.1
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 2-chlorobenzoate
Staphylococcus aureus
-
above, pH 7.9, 37°C, recombinant enzyme
0.1
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 2-chloropyridine-3-carboxylate
Staphylococcus aureus
-
above, pH 7.9, 37°C, recombinant enzyme
0.1
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 2-fluorobenzoate
Staphylococcus aureus
-
above, pH 7.9, 37°C, recombinant enzyme
0.0921
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 2-methoxybenzoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.08862
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 2-methylbenzoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.1
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 2-nitrobenzoate
Staphylococcus aureus
-
above, pH 7.9, 37°C, recombinant enzyme
0.01898
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-(3-methylphenyl)propanoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.0111
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-(4-methylphenyl)propanoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.07109
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-aminobenzoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.08313
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-bromobenzoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.08613
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-chlorobenzoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.08214
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-fluorobenzoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.07211
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-hydroxybenzoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.069
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-methylbenzoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.083
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 3-phenylpropanoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.04894
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 4-aminobenzoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.05523
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 4-chlorobenzoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.06514
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 4-fluorobenzoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.04476
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 4-hydroxybenzoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.05008
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 4-methylbenzoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.1
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 6-chloropyridine-3-carboxylate
Staphylococcus aureus
-
above, pH 7.9, 37°C, recombinant enzyme
0.1
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl 6-hydroxypyridine-3-carboxylate
Staphylococcus aureus
-
above, pH 7.9, 37°C, recombinant enzyme
0.04332
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl benzoate
Staphylococcus aureus
-
pH 7.9, 37°C, recombinant enzyme
0.1
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl pyridine-3-carboxylate
Staphylococcus aureus
-
above, pH 7.9, 37°C, recombinant enzyme
0.1
4-[(naphthalen-1-yl)methyl]-5-oxo-2,5-dihydrothiophen-3-yl pyridine-4-carboxylate
Staphylococcus aureus
-
above, pH 7.9, 37°C, recombinant enzyme
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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 - 9
7.6
7.8
7.9
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
25
30
37