Pickl Andreas, Schönheit Peter
Institut für Allgemeine Mikrobiologie, Christian-Albrechts-Universität Kiel, Am Botanischen Garten 1-9, D-24118 Kiel, Germany.
Institut für Allgemeine Mikrobiologie, Christian-Albrechts-Universität Kiel, Am Botanischen Garten 1-9, D-24118 Kiel, Germany.
FEBS Lett. 2015 Apr 28;589(10):1105-11. doi: 10.1016/j.febslet.2015.03.026. Epub 2015 Mar 31.
The oxidative pentose phosphate pathway (OPPP), catalyzing the oxidation of glucose-6-phosphate to ribulose-5-phosphate is ubiquitous in eukarya and bacteria but has not yet been reported in archaea. In haloarchaea a putative 6-phosphogluconate dehydrogenase (6PGDH) is annotated, whereas a gene coding for glucose-6-phosphate dehydrogenase (Glc6PDH) could not be identified. Here we report the purification and characterization of a novel type of Glc6PDH in Haloferax volcanii that is not related to bacterial and eukaryal Glc6PDHs and the encoding gene is designated as azf (archaeal zwischenferment). Further, recombinant H. volcanii 6PGDH was characterized. Deletion mutant analyses indicate that both, Glc6PDH and 6PGDH, are functionally involved in pentose phosphate formation in vivo. This is the first report on the operation of the OPPP in the domain of archaea.
氧化戊糖磷酸途径（OPPP）催化6-磷酸葡萄糖氧化为5-磷酸核酮糖，在真核生物和细菌中普遍存在，但在古细菌中尚未见报道。在嗜盐古菌中，注释了一个假定的6-磷酸葡萄糖酸脱氢酶（6PGDH），而未鉴定到编码6-磷酸葡萄糖脱氢酶（Glc6PDH）的基因。在此，我们报道了在沃氏嗜盐富球菌中一种新型Glc6PDH的纯化和特性，它与细菌和真核生物的Glc6PDH无关，其编码基因被命名为azf（古菌中间发酵酶）。此外，还对重组沃氏嗜盐富球菌6PGDH进行了特性分析。缺失突变分析表明，Glc6PDH和6PGDH在体内戊糖磷酸形成过程中均发挥功能作用。这是关于古菌域中OPPP运作的首次报道。
