Histidine-272 of isopenicillin N synthase of Cephalosporium acremonium, which is possibly involved in iron binding, is essential for its catalytic activity.
Histidine-272 of isopenicillin N synthase of Cephalosporium acremonium, which is possibly involved in iron binding, is essential for its catalytic activity.
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顶头孢霉异青霉素 N 合酶的组氨酸 272 可能参与铁结合，对其催化活性至关重要。
DOI：
10.1111/j.1574-6968.1994.tb07040.x
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发表时间：
1994
影响因子：
2.1
通讯作者：
D. Tan
中科院分区：
文献类型：
--
作者：
S. Tiow;D. Tan
顶头孢霉异青霉素N合酶（cIPNS）与来自28种不同来源（细菌、真菌、植物和动物）的类似非血红素Fe（2+）含酶的氨基酸序列比对揭示了cIPNS中在位置272处含有不变的组氨酸残基的高度序列保守的同源区域。通过用亮氨酸替换组氨酸残基的定点诱变研究了cIPNS中该组氨酸残基的重要性。通过DNA序列分析证实了突变基因的正确性，并在大肠杆菌中表达。当通过变性凝胶电泳和免疫印迹分析时，突变体cIPNS具有与野生型酶相同的迁移率。对突变酶的酶研究显示酶活性的丧失，表明His272对于cIPNS的催化功能是必需的，可能作为铁结合的配体。
Amino acid sequence alignment of the Cephalosporium acremonium isopenicillin N synthase (cIPNS) to similar non-heme Fe(2+)-containing enzymes from 28 different sources (bacterial, fungal, plant and animals) revealed a homologous region of high sequence conservation containing an invariant histidine residue at position 272 in cIPNS. The importance of this histidine residue in cIPNS was investigated through site-directed mutagenesis by replacing the histidine residue with leucine. The mutated gene was verified by DNA sequence analysis and expressed in Escherichia coli. When analyzed by denaturing gel electrophoresis and immunoblotting, the mutant cIPNS had identical mobility as that of the wild-type enzyme. Enzyme studies on the mutant enzyme showed loss of enzymatic activity indicating that His272 is essential for the catalytic function of cIPNS, possibly as a ligand for iron binding.
异青霉素 N 合酶 Cu(II) 取代衍生物的电子自旋回波包络调制研究：结构和光谱模型。
影响因子：
2.9
作者：
Jiang,F;Peisach,J;Ming,LJ;QueJr,L;Chen,VJ
通讯作者：
Chen,VJ
通过 NMR、EPR 和穆斯堡尔光谱研究血红素电子结构。
DOI：
--
发表时间：
2010
期刊：
影响因子：
--
作者：
Mikio Nakamura;Yoshiki Ohgo;Akira Ikezaki;Masashi Takahashi
通讯作者：
Masashi Takahashi