巨大芽孢杆菌四吡咯生物合成酶胆色素原脱氨酶的结晶及X射线初步表征
Crystallization and preliminary X-ray characterization of the tetrapyrrole-biosynthetic enzyme porphobilinogen deaminase from Bacillus megaterium.
作者信息
Azim N, Deery E, Warren M J, Erskine P, Cooper J B, Wood S P, Akhtar M
机构信息
School of Biological Sciences, University of Punjab, New Campus, Lahore 54590, Pakistan.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Aug;69(Pt 8):906-8. doi: 10.1107/S1744309113018526. Epub 2013 Jul 27.
Abstract
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.
摘要
胆色素原脱氨酶（PBGD；羟甲基胆色素原合酶；EC 2.5.1.61）催化四吡咯生物合成途径的早期步骤，在此步骤中，四个单吡咯胆色素原分子缩合形成线性四吡咯。该酶具有一个二吡咯甲烷辅因子，它通过硫醚桥与一个不变的半胱氨酸残基共价连接。在大肠杆菌中表达巨大芽孢杆菌PBGD的His标签形式，使得能够对该物种的酶进行高分辨率结晶和初步X射线分析。
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