The effect of protein phosphorylation and acetylation on phosphofructokinase in lamb

文献类型： 外文期刊

第一作者： Ren, Chi

作者： Ren, Chi;Zhao, Xinran;Li, Xin;Hou, Chengli;Wang, Zhenyu;Zhang, Dequan;Ren, Chi;Schroyen, Martine

作者机构：

关键词： Phosphofructokinase; Protein phosphorylation; Protein acetylation; Enzyme activity

期刊名称：FOOD BIOSCIENCE （ 影响因子：5.9； 五年影响因子：6.1 ）

ISSN： 2212-4292

年卷期： 2025 年 64 卷

页码：

收录情况： SCI

摘要： Phosphofructokinase (PFK) is a key glycolytic rate-limiting enzyme that affects final meat quality through glycolysis regulation. PFK occurs protein phosphorylation and acetylation in postmortem meat, but how they affect PFK activity has not been well studied. Phosphorylation and acetylation of PFK were adjusted in an in vitro system by adding protein kinase A (PKA) and P300/CBP-associated factor (PCAF), respectively. PFK activity significantly decreased after increasing its phosphorylation level by PKA (P < 0.05). PCAF increased PFK acetylation level, but did not significantly change its activity (P > 0.05). Five PFK variants including wtPFK (wild type), PFK_T704D (T704 phosphorylation), PFK_T704A (T704 dephosphorylation), PFK_K678Q (K678 acetylation) and PFK_K678R (K678 acetylation) were constructed to investigated the effect of T704 and K678 on enzyme activity. Kinetic analysis showed a higher Km, lower Vmax, and lower catalytic efficiency of PFK_T704D on fructose 6-phosphate (F6P), suggesting that T704 phosphorylation decreased PFK activity, possibly by weakening the affinity between F6P and PFK. The changes of PFK variants on ATP were slightly lower than those of PFK variants on F6P. The present study identifies T704 as a possibly vital site for PFK activity regulation and provides theoretical support for the development of meat quality preservation technology.

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