Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + L-tyrosine + tRNATyr
AMP + diphosphate + L-tyrosyl-tRNATyr
AMP + diphosphate
ATP
-
-
-
?
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 + L-tyrosine + tRNATyr
AMP + L-Tyr-tRNATyr + diphosphate
ATP + m-fluoro-D,L-tyrosine + tRNATyr
AMP + m-fluoro-D,L-Tyr-tRNATyr + diphosphate
-
mutant Y43G, aminoacylation assay
-
?
ATP + N-acetyl-L-tyrosine + tRNATyr
AMP + N-acetyl-L-Tyr-tRNATyr + diphosphate
-
wild-type and mutant Y43G, aminoacylation assay
-
?
ATP + N-formyl-L-tyrosine + tRNATyr
AMP + N-formyl-L-Tyr-tRNATyr + diphosphate
-
wild-type and mutant Y43G, aminoacylation assay
-
?
ATP + N-o-nitrophenylsulfenyl-L-tyrosine + tRNATyr
AMP + N-o-nitrophenylsulfenyl-L-Tyr-tRNATyr + diphosphate
-
wild-type and mutant Y43G, aminoacylation assay
-
?
ATP + O-dansyl-L-tyrosine + tRNATyr
AMP + O-dansyl-L-Tyr-tRNATyr + diphosphate
-
wild-type and mutant Y43G, aminoacylation assay
-
?
ATP + O-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 + tyrosine + tRNATyr
AMP + Tyr-tRNATyr + diphosphate
additional information
?
-
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
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2.04 - 2.43
3-chloro-L-tyrosine
0.625 - 1.3
3-fluoro-D,L-tyrosine
1.15
3-iodo-L-tyrosine
-
pH 7.6, 30°C, mutant Y43G
0.56 - 1.84
L-3,4-dihydroxyphenylalanine
0.002
native yeast tRNATyr
-
pH 7.5, 30°C
-
additional information
additional information
-
kinetics, influence of assay conditions, Km for diverse tRNA variants, overview
-
2.04
3-chloro-L-tyrosine
-
pH 7.6, 30°C, wild-type enzyme
2.43
3-chloro-L-tyrosine
-
pH 7.6, 30°C, mutant Y43G
0.625
3-fluoro-D,L-tyrosine
-
pH 7.6, 30°C, wild-type enzyme
1.3
3-fluoro-D,L-tyrosine
-
pH 7.6, 30°C, mutant Y43G
0.46
D-tyrosine
-
pH 7.6, 30°C, wild-type enzyme
14
D-tyrosine
-
pH 7.6, 30°C, mutant Y43G
0.56
L-3,4-dihydroxyphenylalanine
-
pH 7.6, 30°C, mutant Y43G
1.84
L-3,4-dihydroxyphenylalanine
-
pH 7.6, 30°C, wild-type enzyme
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
1.19
L-tyrosine
-
pH 7.6, 30°C, mutant Y43G
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.13 - 6.08
3-chloro-L-tyrosine
0.62 - 6.08
3-fluoro-D,L-tyrosine
0.48
3-iodo-L-tyrosine
-
pH 7.6, 30°C, mutant Y43G
0.67 - 6.08
L-3,4-dihydroxyphenylalanine
1.5
native yeast tRNATyr
-
pH 7.5, 30°C
-
additional information
additional information
-
influence of assay conditions, kcat for diverse tRNA variants, overview
-
0.13
3-chloro-L-tyrosine
-
pH 7.6, 30°C, wild-type enzyme
1.46
3-chloro-L-tyrosine
-
pH 7.6, 30°C, mutant Y43G
6.08
3-chloro-L-tyrosine
-
pH 7.6, 30°C, mutant Y43G
0.62
3-fluoro-D,L-tyrosine
-
pH 7.6, 30°C, mutant Y43G
3.3
3-fluoro-D,L-tyrosine
-
pH 7.6, 30°C, wild-type enzyme
4.96
3-fluoro-D,L-tyrosine
-
pH 7.6, 30°C, wild-type enzyme
6.08
3-fluoro-D,L-tyrosine
-
pH 7.6, 30°C, mutant Y43G
0.37
D-tyrosine
-
pH 7.6, 30°C, mutant Y43G
1.2
D-tyrosine
-
pH 7.6, 30°C, wild-type enzyme
0.67
L-3,4-dihydroxyphenylalanine
-
pH 7.6, 30°C, mutant Y43G
1.65
L-3,4-dihydroxyphenylalanine
-
pH 7.6, 30°C, wild-type enzyme
6.08
L-3,4-dihydroxyphenylalanine
-
pH 7.6, 30°C, mutant Y43G
0.95
L-tyrosine
-
pH 7.6, 30°C, mutant Y43G
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Beikirch, H.; v.d.Haar, F.; Cramer, F.
Tyrosyl-tRNA synthetase
Methods Enzymol.
34B
503-506
1974
Saccharomyces cerevisiae
-
brenda
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
-
brenda
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
brenda
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
brenda
Beikirch, H.; Haar, F.; Cramer, F.
Tyrosyl-tRNA synthetase from baker's yeast
Eur. J. Biochem.
26
182-190
1972
Saccharomyces cerevisiae
brenda
Kucan, Z.; Chambers, R.W.
Purification of tyrosine: tRNA ligase from Saccharomyces cerevisiae
J. Biochem.
73
811-819
1973
Saccharomyces cerevisiae
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda