Characterization of Arabidopsis aldolases AtFBA4, AtFBA5, and their inhibition by morin and interaction with calmodulin

IF 3.5 4区生物学 Q1 Biochemistry, Genetics and Molecular Biology FEBS Letters Pub Date : 2024-07-12 DOI:10.1002/1873-3468.14979

Kyle Symonds, Milena A. Smith, Oona Esme, William C. Plaxton, Wayne A. Snedden

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Abstract

Fructose bisphosphate aldolases (FBAs) catalyze the reversible cleavage of fructose 1,6-bisphosphate into dihydroxyacetone phosphate and glyceraldehyde 3-phosphate. We analyzed two previously uncharacterized cytosolic Arabidopsis FBAs, AtFBA4 and AtFBA5. Based on a recent report, we examined the interaction of AtFBA4 with calmodulin (CaM)-like protein 11 (AtCML11). AtFBA4 did not bind AtCML11; however, we found that CaM bound AtFBA5 in a Ca²⁺-dependent manner with high specificity and affinity (K_D ~ 190 nm) and enhanced its stability. AtFBA4 and AtFBA5 exhibited Michaelis–Menten kinetics with K_m and V_max values of 180 μm and 4.9 U·mg⁻¹ for AtFBA4, and 6.0 μm and 0.30 U·mg⁻¹ for AtFBA5, respectively. The flavonoid morin inhibited both isozymes. Our study suggests that Ca²⁺ signaling and flavanols may influence plant glycolysis/gluconeogenesis.

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拟南芥醛缩酶 AtFBA4 和 AtFBA5 的特征及其受吗啉的抑制作用和与钙调素的相互作用。

果糖二磷酸醛缩酶（FBAs）催化 1,6-二磷酸果糖可逆裂解为磷酸二羟丙酮和 3-磷酸甘油醛。我们分析了两种以前未表征的拟南芥细胞质 FBA，即 AtFBA4 和 AtFBA5。根据最近的一份报告，我们研究了 AtFBA4 与钙调蛋白（CaM）样蛋白 11（AtCML11）的相互作用。AtFBA4 与 AtCML11 没有结合；但是，我们发现 CaM 以 Ca2+ 依赖性方式与 AtFBA5 结合，具有高度特异性和亲和性（KD ~ 190 nm），并增强了其稳定性。AtFBA4 和 AtFBA5 的 Km 和 Vmax 值分别为 180 μm 和 4.9 U-mg-1，以及 6.0 μm 和 0.30 U-mg-1。黄酮类物质吗啉对这两种同工酶都有抑制作用。我们的研究表明，Ca2+ 信号传导和黄烷醇可能会影响植物的糖酵解/糖酮生成。

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来源期刊

FEBS Letters 生物-生化与分子生物学

CiteScore

7.00

自引率

2.90%

发文量

303

审稿时长

1.0 months

期刊介绍： FEBS Letters is one of the world''s leading journals in molecular biology and is renowned both for its quality of content and speed of production. Bringing together the most important developments in the molecular biosciences, FEBS Letters provides an international forum for Minireviews, Research Letters and Hypotheses that merit urgent publication.