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Literature summary 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)

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

Protein Variants

EC Number Protein Variants Comment Organism
6.1.1.1 D172H mutant enzyme shows a significant reductions in tyrosylation activity Aeropyrum pernix
6.1.1.1 D172N mutant enzyme shows a significant reductions in tyrosylation activity Aeropyrum pernix
6.1.1.1 D172P mutant enzyme shows a significant reductions in tyrosylation activity Aeropyrum pernix
6.1.1.1 D172P the mutation completely abolishes tyrosylation activity Aeropyrum pernix
6.1.1.1 additional information Asp172 mutants shows completely abolished tyrosylation activity, whereas mutation at Tyr39 has no effect on activity Aeropyrum pernix
6.1.1.1 Y39E mutant enzyme maintains tyrosylation activity Aeropyrum pernix
6.1.1.1 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
6.1.1.1 Y39G the mutant exhibits near identical aminoacylation activity of both L-tyrosine and 4-azide-L-phenylalanine Aeropyrum pernix
6.1.1.1 Y39G/D172P reduction in tyrosylation activity, the mutant shows specific aminoacylation activity for 4-azide-L-phenylalanine Aeropyrum pernix
6.1.1.1 Y39G/D172P the double mutant shows a reduction in tyrosylation activity Aeropyrum pernix
6.1.1.1 Y39K mutant enzyme maintains tyrosylation activity Aeropyrum pernix

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.1.1.1 additional information
-
 additional information kinetic parameters for anticodon mutants of tRNATyr and for for acceptor stem mutants of tRNATyr Aeropyrum pernix
6.1.1.1 0.00022
-
 tRNATyr 55°C, pH 8.0 Aeropyrum pernix
6.1.1.1 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)

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

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.1 Aeropyrum pernix
-
-
-
6.1.1.1 Aeropyrum pernix Q9YA64
-
-
6.1.1.1 Aeropyrum pernix DSM 11879 Q9YA64
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.1 ATP + 3-(5-hydroxypyridin-2-yl)-L-alanine + tRNATyr
-
 Aeropyrum pernix ?
-
 ?
6.1.1.1 ATP + L-tyrosine + tRNATyr
-
 Aeropyrum pernix AMP + diphosphate + L-tyrosyl-tRNATyr
-
 ?
6.1.1.1 ATP + L-tyrosine + tRNATyr
-
 Aeropyrum pernix DSM 11879 AMP + diphosphate + L-tyrosyl-tRNATyr
-
 ?
6.1.1.1 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

EC Number Synonyms Comment Organism
6.1.1.1 Tyrosyl-tRNA synthetase
-
 Aeropyrum pernix
6.1.1.1 TyrRS
-
 Aeropyrum pernix
6.1.1.1 TyrRSs
-
 Aeropyrum pernix

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.1.1.1 55
-
 assay at Aeropyrum pernix

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.1.1.1 additional information
-
 additional information kinetic parameters for anticodon mutants of tRNATyr and for for acceptor stem mutants of tRNATyr Aeropyrum pernix
6.1.1.1 0.29
-
 tRNATyr 55°C, pH 8.0 Aeropyrum pernix
6.1.1.1 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

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.1.1.1 8
-
 assay at Aeropyrum pernix

Cofactor

EC Number Cofactor Comment Organism Structure
6.1.1.1 ATP
-
 Aeropyrum pernix

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
6.1.1.1 additional information
-
 additional information kinetic parameters for anticodon mutants of tRNATyr and for for acceptor stem mutants of tRNATyr Aeropyrum pernix
6.1.1.1 1300
-
 tRNATyr wild type enzyme, at 55°C, in 100 mM HEPES-NaOH (pH 8.0), 10 mM MgCl2, 10 mM KCl Aeropyrum pernix
6.1.1.1 1318
-
 tRNATyr 55°C, pH 8.0 Aeropyrum pernix