Replacement of serine 373 by phenylalanine in the alpha subunit of Escherichia coli F1-ATPase results in loss of steady-state catalysis by the enzyme.
Replacement of serine 373 by phenylalanine in the alpha subunit of Escherichia coli F1-ATPase results in loss of steady-state catalysis by the enzyme.
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在大肠杆菌 F1-ATP 酶的 α 亚基中，丝氨酸 373 被苯丙氨酸取代，导致该酶失去稳态催化作用。
DOI：
10.1016/s0021-9258(18)90930-0
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发表时间：
1984
期刊：
影响因子：
--
通讯作者：
H. Kanazawa
中科院分区：
文献类型：
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作者：
T. Noumi;M. Futai;H. Kanazawa
在杂交质粒pAN 120上，从突变体AN 120的总DNA中克隆大肠杆菌F1-ATP酶α亚基基因的突变等位基因（uncA 401）。测定pAN 120 α亚基基因的DNA序列，发现核苷酸残基1118处的胞嘧啶变为胸腺嘧啶，并表明丝氨酸373被苯丙氨酸取代。据报道，突变体F1在稳态催化步骤中有缺陷，而其单一周转过程是正常的（金泽，H.，Noumi，T.，松冈岛Hirata T.，和Futai，M.（1984）Arch. Biochem. Biophys. 228，258-269）。因此，我们得出结论，丝氨酸373 α亚基是必不可少的稳态催化F1-ATP酶。
The mutant allele (uncA401) of the gene for the alpha subunit of Escherichia coli F1-ATPase was cloned from the total DNA of the mutant AN120 on a hybrid plasmid pAN120. Determination of the DNA sequence of the alpha subunit gene from pAN120 revealed a single base change of cytosine at nucleotide residue 1118 to thymine and indicated that serine 373 was replaced by phenylalanine. It has been reported that the mutant F1 is defective in a step of steady-state catalysis, whereas its single turnover process is normal (Kanazawa, H., Noumi, T., Matsuoka, I., Hirata T., and Futai, M. (1984) Arch. Biochem. Biophys. 228, 258-269). Thus, we concluded that serine 373 in the alpha subunit is essential for steady-state catalysis by F1-ATPase.
大肠杆菌 uncA 突变体的质子 ATP 酶缺陷。
DOI：
--
发表时间：
1981
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Wise,JG;Latchney,LR;Senior,AE
通讯作者：
Senior,AE