N Azim, E Deery, M J Warren, P Erskine, J B Cooper, S P Wood, M Akhtar
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引用次数: 0
摘要
卟啉原脱氨酶(PBGD;羟甲基比兰合成酶;EC 2.5.1.61)催化四吡咯生物合成途径的早期步骤,在该步骤中,四分子单吡咯卟啉原缩合成线性四吡咯。该酶具有一个二吡咯烷辅助因子,该辅助因子通过硫醚桥与一个不变的半胱氨酸残基共价连接。在大肠杆菌中表达 His 标记形式的巨型芽孢杆菌 PBGD 使该物种的酶得以结晶并进行了初步的高分辨率 X 射线分析。
Crystallization and preliminary X-ray characterization of the tetrapyrrole-biosynthetic enzyme porphobilinogen deaminase from Bacillus megaterium.
The enzyme porphobilinogen deaminase (PBGD; hydroxymethylbilane synthase; EC 2.5.1.61) catalyses an early step of the tetrapyrrole-biosynthesis pathway in which four molecules of the monopyrrole porphobilinogen are condensed to form a linear tetrapyrrole. The enzyme possesses a dipyrromethane cofactor which is covalently linked by a thioether bridge to an invariant cysteine residue. Expression in Escherichia coli of a His-tagged form of Bacillus megaterium PBGD permitted the crystallization and preliminary X-ray analysis of the enzyme from this species at high resolution.
期刊介绍:
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