Aminoacylation of tRNATrpfrom beef liver, yeast and E. coli by beef pancreas tryptopban-tRNA ligase. Stoichiometry of tRNATrpbinding | Zendy

Mireille Dorizzi | Zendy; G. Mérault | Zendy; Michel Fournier | Zendy; Julie Labouesse | Zendy; Gérard Keith | Zendy; G. Dirheimer | Zendy; Richard H. Buckingham | Zendy

Open Access

Aminoacylation of tRNA^Trpfrom beef liver, yeast and E. coli by beef pancreas tryptopban-tRNA ligase. Stoichiometry of tRNA^Trpbinding

Author(s) -

Mireille Dorizzi,

G. Mérault,

Michel Fournier,

Julie Labouesse,

Gérard Keith,

G. Dirheimer,

Richard H. Buckingham

Publication year - 1977

Publication title -

nucleic acids research

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 9.008

H-Index - 537

eISSN - 1362-4954

pISSN - 0305-1048

DOI - 10.1093/nar/4.1.31

Subject(s) - biology , aminoacylation , transfer rna , yeast , biochemistry , escherichia coli , microbiology and biotechnology , dna ligase , enzyme , rna , gene

The Michaelis constants and the maximum velocities in the aminoacylation reaction of tRNATrp from beef liver, yeast and E. coli by pure beef pancreas tryptophan-tRNA ligase show that this mammalian enzyme recognizes and charges the two eucaryotic tRNAs with the same efficiency. The rate of aminoacylation of the procaryotic tRNATrp by the enzyme is three orders of magnitude lower. The pH optimum of aminoacylation is 8 for both eucaryotic tRNAs. The optimum magnesium concentration is different. The rate is maximum when magnesium concentration is stoichiometric to ATP concentration for tRNATrp from beef liver and 10 mM above ATP concentration for tRNATrp from yeast. The number of binding sites on the enzyme for the two eucaryotic tRNAs has been measured by equilibrium filtration on Sephadex G-100 and found equal to two.

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