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Literature summary for 6.1.1.1 extracted from

  • Iwaki, J.; Endo, K.; Ichikawa, T.; Suzuki, R.; Fujimoto, Z.; Momma, M.; Kuno, A.; Nishimura, S.; Hasegawa, T.
    Studies on crenarchaeal tyrosylation accuracy with mutational analyses of tyrosyl-tRNA synthetase and tyrosine tRNA from Aeropyrum pernix (2012), J. Biochem., 152, 539-548.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21-CodonPlus (DE3)-RIL cells Aeropyrum pernix
expression in Escherichia coli Aeropyrum pernix

Protein Variants

Protein Variants Comment Organism
D172H mutant enzyme shows a significant reductions in tyrosylation activity Aeropyrum pernix
D172N mutant enzyme shows a significant reductions in tyrosylation activity Aeropyrum pernix
D172P mutant enzyme shows a significant reductions in tyrosylation activity Aeropyrum pernix
D172P the mutation completely abolishes tyrosylation activity Aeropyrum pernix
additional information Asp172 mutants shows completely abolished tyrosylation activity, whereas mutation at Tyr39 has no effect on activity Aeropyrum pernix
Y39E mutant enzyme maintains tyrosylation activity Aeropyrum pernix
Y39G mutant enzyme maintains tyrosylation activity. Although the wild-type enzyme shows specific tyrosylation activity but not aminoacylation activity for 4-azido-L-phenylalanine, the Y39G mutant exhibits near identical aminoacylation activity of both tyrosine and 4-azido-L-phenylalanine Aeropyrum pernix
Y39G the mutant exhibits near identical aminoacylation activity of both L-tyrosine and 4-azide-L-phenylalanine Aeropyrum pernix
Y39G/D172P reduction in tyrosylation activity, the mutant shows specific aminoacylation activity for 4-azide-L-phenylalanine Aeropyrum pernix
Y39G/D172P the double mutant shows a reduction in tyrosylation activity Aeropyrum pernix
Y39K mutant enzyme maintains tyrosylation activity Aeropyrum pernix

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetic parameters for anticodon mutants of tRNATyr and for for acceptor stem mutants of tRNATyr Aeropyrum pernix
0.00022
-
tRNATyr 55°C, pH 8.0 Aeropyrum pernix
0.00022
-
tRNATyr wild type enzyme, at 55°C, in 100 mM HEPES-NaOH (pH 8.0), 10 mM MgCl2, 10 mM KCl Aeropyrum pernix

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-tyrosine + tRNATyr Aeropyrum pernix
-
AMP + diphosphate + L-tyrosyl-tRNATyr
-
?
ATP + L-tyrosine + tRNATyr Aeropyrum pernix DSM 11879
-
AMP + diphosphate + L-tyrosyl-tRNATyr
-
?

Organism

Organism UniProt Comment Textmining
Aeropyrum pernix
-
-
-
Aeropyrum pernix Q9YA64
-
-
Aeropyrum pernix DSM 11879 Q9YA64
-
-

Purification (Commentary)

Purification (Comment) Organism
Cibacron Blue 3GA column chromatography Aeropyrum pernix

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 3-(5-hydroxypyridin-2-yl)-L-alanine + tRNATyr
-
Aeropyrum pernix ?
-
?
ATP + L-tyrosine + tRNATyr
-
Aeropyrum pernix AMP + diphosphate + L-tyrosyl-tRNATyr
-
?
ATP + L-tyrosine + tRNATyr
-
Aeropyrum pernix DSM 11879 AMP + diphosphate + L-tyrosyl-tRNATyr
-
?
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 Aeropyrum pernix ?
-
?

Synonyms

Synonyms Comment Organism
Tyrosyl-tRNA synthetase
-
Aeropyrum pernix
TyrRS
-
Aeropyrum pernix
TyrRSs
-
Aeropyrum pernix

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
55
-
assay at Aeropyrum pernix

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information kinetic parameters for anticodon mutants of tRNATyr and for for acceptor stem mutants of tRNATyr Aeropyrum pernix
0.29
-
tRNATyr 55°C, pH 8.0 Aeropyrum pernix
0.29
-
tRNATyr wild type enzyme, at 55°C, in 100 mM HEPES-NaOH (pH 8.0), 10 mM MgCl2, 10 mM KCl Aeropyrum pernix

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Aeropyrum pernix

Cofactor

Cofactor Comment Organism Structure
ATP
-
Aeropyrum pernix

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
additional information
-
additional information kinetic parameters for anticodon mutants of tRNATyr and for for acceptor stem mutants of tRNATyr Aeropyrum pernix
1300
-
tRNATyr wild type enzyme, at 55°C, in 100 mM HEPES-NaOH (pH 8.0), 10 mM MgCl2, 10 mM KCl Aeropyrum pernix
1318
-
tRNATyr 55°C, pH 8.0 Aeropyrum pernix