当前位置: X-MOL 学术Biochem. Cell Biol. › 论文详情
Our official English website, www.x-mol.net, welcomes your feedback! (Note: you will need to create a separate account there.)
Activity of fructose-1,6-bisphosphatase from Campylobacter jejuni.
Biochemistry and Cell Biology ( IF 2.9 ) Pub Date : 2020-03-03 , DOI: 10.1139/bcb-2020-0021
Adnan Ayna 1 , Peter C E Moody 2
Affiliation  

The glycolytic pathway of the enteric pathogen Campylobacter jejuni is incomplete; the absence of phosphofructokinase means that the suppression of futile cycling at this point in the glycolytic-gluconeogenic pathway might not be required, and therefore the mechanism for controlling pathway flux is likely to be quite different or absent. In this study, the characteristics of fructose-1,6-bisphosphatase (FBPase) of C. jejuni are described and the regulation of this enzyme is compared with the equivalent enzymes from organisms capable of glycolysis. The enzyme is insensitive to AMP inhibition, unlike other type I FBPases. Campylobacter jejuni FBPase also shows limited sensitivity to other glycolytic and gluconeogenic intermediates. The allosteric cooperative control of the enzyme's activity found in type I FBPases appears to have been lost.

中文翻译:

空肠弯曲杆菌果糖-1,6-双磷酸酶的活性。

空肠弯曲菌空肠弯曲杆菌的糖酵解途径不完整;缺少磷酸果糖激酶意味着在糖酵解-糖异生途径中此时不需要抑制无效循环,因此控制途径通量的机制可能完全不同或不存在。在这项研究中,描述了空肠弯曲菌果糖-1,6-双磷酸酶(FBPase)的特性,并将该酶的调节作用与能够进行糖酵解的生物等效酶进行了比较。与其他I型FBPase不同,该酶对AMP抑制不敏感。空肠弯曲杆菌FBPase对其他糖酵解和糖异生中间体的敏感性也有限。在I型FBPase中发现的酶活性的变构协同控制似乎已经丢失。
更新日期:2020-03-03
down
wechat
bug