Purification and properties of methionyl-tRNA synthetase fromE. coliK 12 carrying the F32 episome
نویسندگان
چکیده
منابع مشابه
Methionyl-tRNA Synthetase from Phaseolus aureus: Purification and Properties.
l-Methionyl-tRNA synthetase (EC 6.1.1.10) from seeds of Phaseolus aureus has been purified approximately 290-fold. Optimum assay conditions were determined by using the ATP-pyrophosphate exchange assay and the aminoacylation assay. The enzyme catalyzes both selenomethionine- and selenoethionine-dependent ATP-pyrophosphate exchange in addition to catalyzing the formation of selenomethionyl-tRNA ...
متن کاملMethionyl-tRNA synthetase.
Methionyl-tRNA synthetase (MetRS) belongs to the family of 20 enzymes essential for protein biosynthesis. It links covalently methionine with its cognate tRNA. Crystal structures solved for bacterial MetRSs have given a number of interesting insights into enzyme architecture and methionylation catalysis. A comparison of sequences of MetRSs belonging to all kingdoms of life, as well as numerous ...
متن کاملCytoplasmic Methionyl - tRNA Synthetase from Bakers ’ Yeast
Methionyl-tRNA synthetase has been purified from a yeast strain carrying the MESl structural gene on a high copy number plasmid (pFL1). The purified enzyme is a monomer of M, = 85,000 in contrast to its counterpart from Escherichia coli which is a dimer made up of identical subunits (M, = 76,000; Dardel, F., Fayat, G., and Blanquet, S . (1984) J. Bucteriol. 160,1115-1122). The yeast enzyme was ...
متن کاملVariable sensitivity to bacterial methionyl-tRNA synthetase inhibitors reveals subpopulations of Streptococcus pneumoniae with two distinct methionyl-tRNA synthetase genes.
As reported previously (J. R. Jarvest et al., J. Med. Chem. 45:1952-1962, 2002), potent inhibitors (at nanomolar concentrations) of Staphylococcus aureus methionyl-tRNA synthetase (MetS; encoded by metS1) have been derived from a high-throughput screening assay hit. Optimized compounds showed excellent activities against staphylococcal and enterococcal pathogens. We report on the bimodal suscep...
متن کاملSelectivity and specificity of substrate binding in methionyl-tRNA synthetase.
The accuracy of in vivo incorporation of amino acids during protein biosynthesis is controlled to a significant extent by aminoacyl-tRNA synthetases (aaRS). This paper describes the application of the HierDock computational method to study the molecular basis of amino acid binding to the Escherichia coli methionyl tRNA synthetase (MetRS). Starting with the protein structure from the MetRS cocry...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: FEBS Letters
سال: 1971
ISSN: 0014-5793
DOI: 10.1016/0014-5793(71)80002-9