古菌域中无叶酸或修饰叶酸时的嘌呤生物合成。
Purine biosynthesis in the domain Archaea without folates or modified folates.
作者信息
White R H
机构信息
Department of Biochemistry, Virginia Polytechnic Institute and State University, Blacksburg 24061-0308, USA.
出版信息
J Bacteriol. 1997 May;179(10):3374-7. doi: 10.1128/jb.179.10.3374-3377.1997.
Abstract
The established pathway for the last two steps in purine biosynthesis, the conversion of 5-aminoimidazole-4-carboxamide ribonucleotide (ZMP) to IMP, is known to utilize 10-formyl-tetrahydrofolate as the required C1 donor cofactor. The biosynthetic conversion of ZMP to IMP in three members of the domain Archaea, Methanobacterium thermoautotrophicum deltaH, M. thermoautotrophicum Marburg, and Sulfolobus solfataricus, however, has been demonstrated to occur with only formate and ATP serving as cofactors. Thus, in these archaea, which use methanopterin (MPT) or another modified folate in place of folate as the C1 carrier coenzyme, neither folate nor a modified folate serves as a cofactor for this biosynthetic transformation. It is concluded that archaea, which function with modified folates such as MPT, are able to carry out purine biosynthesis without the involvement of folates or modified folates.
摘要
嘌呤生物合成最后两步的既定途径，即5-氨基咪唑-4-甲酰胺核糖核苷酸（ZMP）转化为肌苷一磷酸（IMP），已知利用10-甲酰四氢叶酸作为所需的C1供体辅因子。然而，在古菌域的三个成员，即嗜热自养甲烷杆菌δH、嗜热自养甲烷杆菌马尔堡菌株和嗜热栖热菌中，ZMP到IMP的生物合成转化已被证明仅以甲酸和ATP作为辅因子发生。因此，在这些使用甲烷蝶呤（MPT）或另一种修饰叶酸替代叶酸作为C1载体辅酶的古菌中，叶酸和修饰叶酸均不作为这种生物合成转化的辅因子。得出的结论是，利用MPT等修饰叶酸发挥功能的古菌能够在不涉及叶酸或修饰叶酸的情况下进行嘌呤生物合成。
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