氨酰-tRNA合成酶：2',3'-核糖氧化型ATP对ATP结合位点的亲和标记
Aminoacyl-tRNA synthetases: affinity labeling of the ATP binding site by 2', 3' -ribose oxidized ATP.
作者信息
Fayat G, Fromant M, Blanquet S
出版信息
Proc Natl Acad Sci U S A. 1978 May;75(5):2088-92. doi: 10.1073/pnas.75.5.2088.
Abstract
Homogeneous Escherichia coli methionyl-, isoleucyl-, tryptophanyl-, and phenylalanyl-tRNA synthetases and Bacillus stearothermophilus methionyl- and tyrosyl-tRNA synthetases are irreversibly inactivated by reaction of their active ATP sites with the 2',3'-dialdehyde derivative of ATP obtained by periodate oxidation. In each case, the amount of 14C-labeled dialdehyde derivative incorporated per molecule of inactivated enzyme appears consistent with the expected active stoichiometry of the synthetase. These results strongly support the presence, at the active site of the studied aminoacyl-tRNA synthetases, of a common residue, probably a lysine whose epsilon-NH2 group is known, from the work of others, to form a Schiff's base specifically with the 2',3'-dialdehyde derivatives of ribonucleotides.
摘要
同源的大肠杆菌甲硫氨酰 - 、异亮氨酰 - 、色氨酰 - 和苯丙氨酰 - tRNA合成酶以及嗜热脂肪芽孢杆菌甲硫氨酰 - 和酪氨酰 - tRNA合成酶，通过其活性ATP位点与经高碘酸盐氧化得到的ATP的2',3'-二醛衍生物反应而被不可逆地失活。在每种情况下，每分子失活酶掺入的14C标记二醛衍生物的量似乎与合成酶预期的活性化学计量一致。这些结果有力地支持了在所研究的氨酰 - tRNA合成酶的活性位点存在一个共同残基，可能是一个赖氨酸，根据其他人的研究，其ε - NH2基团已知会与核糖核苷酸的2',3'-二醛衍生物特异性形成席夫碱。
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本文引用的文献
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Level of methionyl-tRNA synthetase in merodiploids of Escherichia coli K12.大肠杆菌K12部分二倍体中甲硫氨酰 - tRNA合成酶的水平。
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