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依赖ADP的蓝藻磷酸果糖激酶的结构功能分析揭示了PFK-A家族中的新系统发育分组。

Structure function analysis of ADP-dependent cyanobacterial phosphofructokinase reveals new phylogenetic grouping in the PFK-A family.

作者信息

Shen Lu, Peraglie Carmen, Podlesainski David, Stracke Christina, Ojha Ravi Shankar, Caliebe Frauke, Kaiser Markus, Forchhammer Karl, Hagemann Martin, Gutekunst Kirstin, Snoep Jacky L, Bräsen Christopher, Siebers Bettina

机构信息

Molecular Enzyme Technology and Biochemistry (MEB), Environmental Microbiology and Biotechnology (EMB), Centre for Water and Environmental Research (CWE), Faculty of Chemistry, University of Duisburg-Essen, Essen, Germany.

Chemical Biology, Centre of Medical Biotechnology (ZMB), Faculty of Biology, University of Duisburg-Essen, Essen, Germany.

出版信息

J Biol Chem. 2024 Nov;300(11):107868. doi: 10.1016/j.jbc.2024.107868. Epub 2024 Oct 10.

DOI:10.1016/j.jbc.2024.107868
PMID:39393572
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11609450/
Abstract

Depending on the light conditions, photosynthetic organisms switch between carbohydrate synthesis or breakdown, for which the reversibility of carbohydrate metabolism, including glycolysis, is essential. Kinetic regulation of phosphofructokinase (PFK), a key-control point in glycolysis, was studied in the cyanobacterium Synechocystis sp. PCC 6803. The two PFK iso-enzymes (PFK- A1, PFK-A2), were found to use ADP instead of ATP, and have similar kinetic characteristics, but differ in their allosteric regulation. PFK-A1 is inhibited by 3-phosphoglycerate, a product of the Calvin-Benson-Bassham cycle, while PFK-A2 is inhibited by ATP, which is provided by photosynthesis. This regulation enables cyanobacteria to switch PFK off in light, and on in darkness. ADP dependence has not been reported before for the PFK-A enzyme family and was thought to be restricted to the PFK-B ribokinase superfamily. Phosphate donor specificity within the PFK-A family could be related to specific binding motifs in ATP-, ADP-, and PPi-dependent PFK-As. Phylogenetic analysis revealed a distribution of ADP-PFK-As in cyanobacteria and in a few alphaproteobacteria, which was confirmed in enzymatic studies.

摘要

根据光照条件，光合生物在碳水化合物合成或分解之间进行切换，为此碳水化合物代谢（包括糖酵解）的可逆性至关重要。在蓝藻集胞藻PCC 6803中研究了糖酵解的关键控制点磷酸果糖激酶（PFK）的动力学调节。发现两种PFK同工酶（PFK-A1、PFK-A2）使用ADP而非ATP，且具有相似的动力学特征，但在别构调节方面存在差异。PFK-A1受卡尔文-本森-巴斯姆循环的产物3-磷酸甘油酸抑制，而PFK-A2受光合作用提供的ATP抑制。这种调节使蓝藻能够在光照下关闭PFK，在黑暗中开启PFK。此前尚未有关于PFK-A酶家族依赖ADP的报道，且认为这仅限于PFK-B核糖激酶超家族。PFK-A家族内的磷酸供体特异性可能与ATP、ADP和PPi依赖性PFK-A中的特定结合基序有关。系统发育分析揭示了ADP-PFK-A在蓝藻和一些α-变形菌中的分布，这在酶学研究中得到了证实。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eef0/11609450/9e9518fc7479/gr6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eef0/11609450/a4117fa77eb1/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eef0/11609450/fd7bfa7f1e3d/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eef0/11609450/74bdcfadd1a5/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eef0/11609450/fa76ddfabb82/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eef0/11609450/d2706cf08fa0/gr5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eef0/11609450/9e9518fc7479/gr6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eef0/11609450/a4117fa77eb1/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eef0/11609450/fd7bfa7f1e3d/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eef0/11609450/74bdcfadd1a5/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eef0/11609450/fa76ddfabb82/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eef0/11609450/d2706cf08fa0/gr5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/eef0/11609450/9e9518fc7479/gr6.jpg

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