ROLE OF SULFHYDRYL GROUPS IN ACTIVATING ENZYMES - PROPERTIES OF ESCHERICHIA COLI LYSINE-TRANSFER RIBONUCLEIC ACID SYNTHETASE
ROLE OF SULFHYDRYL GROUPS IN ACTIVATING ENZYMES - PROPERTIES OF ESCHERICHIA COLI LYSINE-TRANSFER RIBONUCLEIC ACID SYNTHETASE
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DOI:
10.1021/bi00865a016
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发表时间:
1966-01-01
期刊:
影响因子:
2.9
通讯作者:
MCELROY, WD
中科院分区:
文献类型:
--
作者:
STERN, R;DELUCA, M;MCELROY, WD
The role of the SH groups in the lysine-transfer ribonucleic-acid (t-RNA) synthetase from E. coli has been investigated. The native enzyme contains two reactive SH groups per mole, and one additional SH group is exposed in 6 [image] urea. Sulfhydryl reagents do not inhibit the pyrophosphate-adenosine tri-phosphate exchange activity of the enzyme. This enzyme is shown to be the only amino-acid activating enzyme from E. coli that is not inhibited by p-mercuribenzoate (PMB); PMB and HgCl2 inhibit the transfer of lysine from the enzyme to the RNA; HgCl2 causes a marked shift in the absorption maxima of the RNA, which apparently reflects disruption of structure.