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- W2007364517 abstract "Earlier studies have shown that native phenylalanyl-tRNA synthetase from baker's yeast contains two different kinds of subunits, alpha of molecular weight 73000 and beta of molecular weight 63000. The enzyme is an asymmetric tetramer alpha-2beta-2, which binds two moles of each ligand per mole. Incubation of the purified enzyme with trypsin results in an irreversible conversion: the alpha-subunit remains apparently unchanged but beta is rapidly degraded and yields a lighter species beta of molecular weight 41000. The trypsin-modified enzyme is an alpha-2beta-2 molecule which can still activate phenylalanine but cannot transfer it to tRNA-Phe; furthermore it does not bind tRNA-Phe but its kinetic parameters are identical to those of the native enzyme with respect to ATP and phenylalanine. Therefore the two beta subunits play a critical part in tRNA binding. Isolated alpha or beta subunits exhibit no significant activity and both types of subunit seem to be required for phenylalanine activation." @default.
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- W2007364517 date "1975-05-01" @default.
- W2007364517 modified "2023-09-23" @default.
- W2007364517 title "Modification of Phenylalanyl-tRNA Synthetase from Baker's Yeast by Proteolytic Cleavage and Properties of the Trypsin-Modified Enzyme" @default.
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- W2007364517 doi "https://doi.org/10.1111/j.1432-1033.1975.tb04090.x" @default.
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