Any feedback?
Information on EC 6.1.1.1 - tyrosine-tRNA ligase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P36421
for references in articles please use BRENDA:EC6.1.1.1Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
6.1.1.1 tyrosine-tRNA ligaseSpecify your search results
Word Map
- 6.1.1.1
- synthetases
- aminoacylation
-
tyrosylation
- stearothermophilus
-
anticodon
-
amber
- jannaschii
- trprs
-
aarss
- methanococcus
-
kmsks
-
tryptophanyl-trna
-
charcot-marie-tooth
-
mischarging
-
trna-like
- d-tyrosine
-
self-splicing
- methanocaldococcus
-
half-of-the-sites
- elr
-
non-cognate
- methionyl-trna
-
isoleucyl-trna
- medicine
- biotechnology
-
sideroblastic
-
anticodon-binding
-
tyrts
- 3-iodo-l-tyrosine
- glycyl-trna
- drug development
- pharmacology
- leurs
-
misacylation
- phenylalanyl-trna
-
fersht
-
brome
- hisrs
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
tyrosyl-trna synthetase, tyrrs, cyt-18, mitochondrial tyrosyl-trna synthetase, mini-tyrrs, tyrrss, cyt-18 protein, tyrosyl trna synthetase, ldtyrrs, mttyrrs, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Tyrosine translase
-
-
-
-
Tyrosine tRNA synthetase
Tyrosine--tRNA ligase
-
-
-
-
Tyrosine-transfer ribonucleate synthetase
-
-
-
-
Tyrosine-transfer RNA ligase
-
-
-
-
Tyrosyl--tRNA ligase
-
-
-
-
Tyrosyl-transfer ribonucleate synthetase
-
-
-
-
Tyrosyl-transfer ribonucleic acid synthetase
-
-
-
-
Tyrosyl-transfer RNA synthetase
-
-
-
-
Tyrosyl-tRNA ligase
-
-
-
-
Tyrosyl-tRNA synthetase
TyrRS
Tyrosine tRNA synthetase
-
-
-
-
Tyrosyl-tRNA synthetase
-
-
-
-
TyrRS
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
esterification
Acylation
esterification
-
-
-
-
Acylation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-tyrosine:tRNATyr ligase (AMP-forming)
-
CAS REGISTRY NUMBER
COMMENTARY
9023-45-4
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 3-amino-L-tyrosine + tRNATyr
AMP + 3-amino-L-Tyr-tRNATyr + diphosphate
-
mutant Y43G, aminoacylation assay
-
?
ATP + 3-azido-L-tyrosine + tRNATyr
AMP + 3-azido-L-Tyr-tRNATyr + diphosphate
-
mutant Y43G, aminoacylation assay
-
?
ATP + 3-azido-L-tyrosine + tRNATyr
AMP + diphosphate + 3-azido-L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + 3-chloro-L-tyrosine + tRNATyr
AMP + 3-chloro-L-Tyr-tRNATyr + diphosphate
-
mutant Y43G, aminoacylation assay
-
?
ATP + 3-iodo-L-tyrosine + tRNATyr
AMP + 3-iodo-L-Tyr-tRNATyr + diphosphate
-
mutant Y43G, aminoacylation assay
-
?
ATP + 3-iodo-L-tyrosine + tRNATyr
AMP + diphosphate + 3-iodo-L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + 3-methoxy-L-tyrosine + tRNATyr
AMP + 3-methoxy-L-Tyr-tRNATyr + diphosphate
-
mutant Y43G, aminoacylation assay
-
?
ATP + 3-nitro-L-tyrosine + tRNATyr
AMP + 3-nitro-L-Tyr-tRNATyr + diphosphate
-
mutant Y43G, aminoacylation assay
-
?
ATP + D-3,4-dihydroxyphenylalanine + tRNATyr
AMP + D-3,4-dihydroxyphenylalanine-tRNATyr + diphosphate
-
mutant Y43G, aminoacylation assay
-
?
ATP + D-tyrosine + tRNATyr
AMP + D-Tyr-tRNATyr + diphosphate
-
mutant Y43G, aminoacylation assay
-
?
ATP + L-3,4-dihydroxyphenylalanine + tRNATyr
AMP + L-3,4-dihydroxyphenylalanine-tRNATyr + diphosphate
-
mutant Y43G, aminoacylation assay
-
?
ATP + L-tyrosine + native yeast tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
-
-
-
-
?
ATP + m-fluoro-D,L-tyrosine + tRNATyr
AMP + m-fluoro-D,L-Tyr-tRNATyr + diphosphate
-
mutant Y43G, aminoacylation assay
-
?
ATP + N-acetyl-L-tyrosine + tRNATyr
AMP + N-acetyl-L-Tyr-tRNATyr + diphosphate
-
wild-type and mutant Y43G, aminoacylation assay
-
?
ATP + N-formyl-L-tyrosine + tRNATyr
AMP + N-formyl-L-Tyr-tRNATyr + diphosphate
-
wild-type and mutant Y43G, aminoacylation assay
-
?
ATP + N-o-nitrophenylsulfenyl-L-tyrosine + tRNATyr
AMP + N-o-nitrophenylsulfenyl-L-Tyr-tRNATyr + diphosphate
-
wild-type and mutant Y43G, aminoacylation assay
-
?
ATP + O-dansyl-L-tyrosine + tRNATyr
AMP + O-dansyl-L-Tyr-tRNATyr + diphosphate
-
wild-type and mutant Y43G, aminoacylation assay
-
?
ATP + O-methyl-L-tyrosine + tRNATyr
AMP + O-methyl-L-Tyr-tRNATyr + diphosphate
-
wild-type and mutant Y43G, aminoacylation assay
-
?
ATP + O-phospho-L-tyrosine + tRNATyr
AMP + O-phospho-L-Tyr-tRNATyr + diphosphate
-
wild-type and mutant Y43G, aminoacylation assay
-
?
ATP + 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 + L-Tyr-tRNATyr + diphosphate
-
-
-
?
ATP + L-tyrosine + tRNATyr
AMP + 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
-
-
-
?
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
-
?
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
-
-
?
additional information
?
-
-
no activity with tRNAAsp and tRNAPhe
-
?
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 + 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 + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
-
10 mM, can be replaced by Mn2+ with equal efficiency and by Ca2+, Co2+, Sr2+, Ba2+, spermine with reduced efficiency
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
O-(adenosine-5'-O-yl) N-(L-tyrosyl)phosphoramidate
i.e. Tyr-AMPN, a non-hydrolyzable Tyr-AMP analog, binding structure, overview
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetics, influence of assay conditions, Km for diverse tRNA variants, overview
-
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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
influence of assay conditions, kcat for diverse tRNA variants, overview
-
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
structural comparison of TyrRS of different origin, overview
additional information
-
structural comparison of TyrRS of different origin, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant modified enzyme, SceTyrRS comprising residues 1-364, as ternary complex with cognate tRNATyr and Tyr-AMP analog O-(adenosine-5'-O-yl) N-(L-tyrosyl)phosphoramidate, i.e. Tyr-AMPN, hanging-drop vapor diffusion method, mixing of equal volumes of protein solution containing ca. 0.2 mM SceTyrRS, 5 mM Tyr-AMPN, ca. 0.2 mM tRNATyr, 40 mM KCl in 20 mM Tris buffer at pH 7.5, with reservoir solution containing 25% v/v PEG 400 and 100 mM CaCl2 in 100 mM Tris buffer at pH 7.5, X-ray diffraction structure determination and analysis at 2.4 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
additional information
additional information
construction of a chemically truncated enzyme comprising residues 1-364, termed SceTyrRS
additional information
-
construction of a chemically truncated enzyme comprising residues 1-364, termed SceTyrRS
additional information
-
construction of diverse tRNA variants of the native tRNATyr from yeast by heterologous in vitro translation, transplantation and point mutations
additional information
-
the Escherichia coli TyrRS-tRNATyr pair is functionally replaced by the Saccharomyces cerevisiae tyrosine pair
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant truncated enzyme SceTyrRS comprising residues 1-364
recombinant His-tagged wild-type and mutant Y43G enzyme from Escherichia coli Y43G
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of truncated enzyme SceTyrRS comprising residues 1-364
overexpression of His-tagged wild-type and mutant Y43G enzyme in Escherichia coli BL21(DE3)
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
biotechnology
-
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
-
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Beikirch, H.; v.d.Haar, F.; Cramer, F.
Tyrosyl-tRNA synthetase
Methods Enzymol.
34B
503-506
1974
Saccharomyces cerevisiae
-
Bhanot, O.S.; Kucan, Z.; Aoyagi, S.; Lee, F.C.; Chambers, R.W.
Purification of tyrosine:tRNA ligase, valine:tRNA ligase, alanine:tRNA ligase, and isoleucine:tRNA ligase from Saccharomyces cerevisiae alphaS288C
Methods Enzymol.
29E
547-576
1974
Saccharomyces cerevisiae
-
Brick, P.; Bhat, T.N.; Blow, D.M.
Structure of tyrosyl-tRNA synthetase refined at 2.3 A resolution
J. Mol. Biol.
208
83-98
1988
Saccharomyces cerevisiae
Freist, W.; Sternbach, H.
Tyrosyl-tRNA synthetase from bakers yeast. Order of substrate addition, discrimination of 20 amino acids in aminoacylation of tRNATyr-C-C-A and tRNATyr-C-C-A(3'NH2)
Eur. J. Biochem.
177
425-433
1988
Saccharomyces cerevisiae
Beikirch, H.; Haar, F.; Cramer, F.
Tyrosyl-tRNA synthetase from baker's yeast
Eur. J. Biochem.
26
182-190
1972
Saccharomyces cerevisiae
Kucan, Z.; Chambers, R.W.
Purification of tyrosine: tRNA ligase from Saccharomyces cerevisiae
J. Biochem.
73
811-819
1973
Saccharomyces cerevisiae
Faulhammer, G.H.; Cramer, F.
Tyrosyl-tRNA synthetase from baker's yeast. Rapid isolation by affinity elution, molecular weight of the enzyme and determination of essential sulfhydryl groups
Eur. J. Biochem.
75
561-570
1977
Saccharomyces cerevisiae
Freist, W.; von der Haar, F.; Faulhammer, H.; Cramer, F.
Valyl-tRNA, isoleucyl-tRNA and tyrosyl-tRNA synthetase from baker's yeast. Substrate specificity with regard to ATP analogs and mechanism of the aminoacylation reaction
Eur. J. Biochem.
66
493-497
1976
Saccharomyces cerevisiae
Fechter, P.; Rudinger-Thirion, J.; Theobald-Dietrich, A.; Giege, R.
Identity of tRNA for yeast tyrosyl-tRNA synthetase: tyrosylation is more sensitive to identity nucleotides than to structural features
Biochemistry
39
1725-1733
2000
Saccharomyces cerevisiae
Ohno, S.; Yokogawa, T.; Nishikawa, K.
Changing the amino acid specificity of yeast tyrosyl-tRNA synthetase by genetic engineering
J. Biochem.
130
417-423
2001
Saccharomyces cerevisiae
Tsunoda, M.; Kusakabe, Y.; Tanaka, N.; Ohno, S.; Nakamura, M.; Senda, T.; Moriguchi, T.; Asai, N.; Sekine, M.; Yokogawa, T.; Nishikawa, K.; Nakamura, K.T.
Structural basis for recognition of cognate tRNA by tyrosyl-tRNA synthetase from three kingdoms
Nucleic Acids Res.
35
4289-4300
2007
Saccharomyces cerevisiae (P36421), Saccharomyces cerevisiae
Iraha, F.; Oki, K.; Kobayashi, T.; Ohno, S.; Yokogawa, T.; Nishikawa, K.; Yokoyama, S.; Sakamoto, K.
Functional replacement of the endogenous tyrosyl-tRNA synthetase-tRNATyr pair by the archaeal tyrosine pair in Escherichia coli for genetic code expansion
Nucleic Acids Res.
38
3682-3691
2010
Saccharomyces cerevisiae, Methanocaldococcus jannaschii, Escherichia coli (P0AGJ9), Escherichia coli
Storkebaum, E.; Leitao-Goncalves, R.; Godenschwege, T.; Nangle, L.; Mejia, M.; Bosmans, I.; Ooms, T.; Jacobs, A.; Van Dijck, P.; Yang, X.L.; Schimmel, P.; Norga, K.; Timmerman, V.; Callaerts, P.; Jordanova, A.
Dominant mutations in the tyrosyl-tRNA synthetase gene recapitulate in Drosophila features of human Charcot-Marie-Tooth neuropathy
Proc. Natl. Acad. Sci. USA
106
11782-11787
2009
Saccharomyces cerevisiae, Drosophila melanogaster, Homo sapiens
EXTERNAL LINKS (specific for EC-Number 6.1.1.1)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
