VAS1/YGR094W Literature Guide Help

Other names published for VAS1: valine--tRNA ligase, YGR094W

VAS1 - Substrates/Ligands/Cofactors (11)

ReferenceOther Genes Addressed
Chiu WC, et al.  (2009) Evolutionary Basis of Converting a Bacterial tRNA Synthetase into a Yeast Cytoplasmic or Mitochondrial Enzyme. J Biol Chem 284(36):23954-60
Wientges J, et al.  (2000) Selection of viral RNA-derived tRNA-like structures with improved valylation activities. Biochemistry 39(20):6207-18
Florentz C, et al.  (1990) Stimulatory effect of ammonium sulfate at high concentrations on the aminoacylation of tRNA and tRNA-like molecules. FEBS Lett 261(2):335-8
Black S  (1983) A novel thiol-dependent arsenite-sensitive valyl-tRNA synthetase activity from yeast. J Biol Chem 258(4):2112-4
Vlassov VV, et al.  (1983) Interaction of tRNAPhe and tRNAVal with aminoacyl-tRNA synthetases. A chemical modification study. Eur J Biochem 132(3):537-44
Kern D and Giege R  (1979) The 32PPi--ATP isotope-exchange reaction catalyzed by the yeast valyl-tRNA synthetase: order of substrate binding and effect of tRNA. FEBS Lett 103(2):274-81
Freist W, et al.  (1976) 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(3):493-7
Hecht SM and Chinualt AC  (1976) Position of aminoacylation of individual Escherichia coli and yeast tRNAs. Proc Natl Acad Sci U S A 73(2):405-9
Rymo L, et al.  (1972) Subunit structure and binding properties of three amino acid transfer ribonucleic acid ligases. J Biol Chem 247(12):3888-97
Lagerkvist U and Waldenstrom J  (1967) Purification and some properties of valyl ribonucleic acid synthetase from yeast. J Biol Chem 242(13):3021-5
Lagerkvist U, et al.  (1966) Structure and function of transfer ribonucleic acid. II. Enzyme-substrate complexes with valyl ribonucleic acid synthetase from yeast. J Biol Chem 241(22):5391-400