结核分枝杆菌ribose-5-phosphate异构酶有一个已知的褶皱,但小说活性部位。
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鲁斯AK,安德森CE、Bergfors T,路上,M, Karlen, Unge T,琼斯助教,莫布雷SL
结核分枝杆菌ribose-5-phosphate异构酶有一个已知的褶皱,但小说活性部位。
J杂志。2004年1月16日,335 (3):799 - 809。
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14687575 (在PubMed]
- 文摘
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Ribose-5-phosphate异构酶(EC 5.3.1.6) inter-convert Ribose-5-phosphate ribulose-5-phosphate。这个反应可以合成核糖与其他糖,也意味着打捞核苷酸分解后的碳水化合物。两个不相关的已知类型的酶催化异构化。最常见的一种,RpiA,存在于几乎所有的生物。RpiB,第二种类型是发现在许多细菌物种。在这里,我们表明,结核分枝杆菌的RpiB (Rv2465c)催化性质非常类似于之前报道的大肠杆菌RpiB酶。进一步,我们报告分枝杆菌酶的结构,解决了分子置换和精炼到1.88一项决议。比较与E。杆菌结构表明,重要的差异有两个活跃的网站,包括位置和催化性质的变化。序列比较表明,M。结核病和E。coli RpiB enzymes are in fact representative of two distinct sub-families. The mycobacterial enzyme represents a type found only in actinobacteria, while the enzyme from E.coli is typical of that seen in many other bacterial proteomes. Both RpiBs are very different from RpiA in structure as well as in the construction of the active site. Docking studies allow additional insights into the reactions of all three enzymes, and show that many features of the mechanism are preserved despite the different catalytic components.