Kyle Symonds, Milena A. Smith, Oona Esme, William C. Plaxton, Wayne A. Snedden
{"title":"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。","authors":"Kyle Symonds, Milena A. Smith, Oona Esme, William C. Plaxton, Wayne A. Snedden","doi":"10.1002/1873-3468.14979","DOIUrl":null,"url":null,"abstract":"<p>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 <i>Arabidopsis</i> 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 Ca<sup>2+</sup>-dependent manner with high specificity and affinity (<i>K</i><sub>D</sub> ~ 190 n<span>m</span>) and enhanced its stability. AtFBA4 and AtFBA5 exhibited Michaelis–Menten kinetics with <i>K</i><sub>m</sub> and <i>V</i><sub>max</sub> values of 180 μ<span>m</span> and 4.9 U·mg<sup>−1</sup> for AtFBA4, and 6.0 μ<span>m</span> and 0.30 U·mg<sup>−1</sup> for AtFBA5, respectively. The flavonoid morin inhibited both isozymes. Our study suggests that Ca<sup>2+</sup> signaling and flavanols may influence plant glycolysis/gluconeogenesis.</p>","PeriodicalId":12142,"journal":{"name":"FEBS Letters","volume":"598 15","pages":"1864-1876"},"PeriodicalIF":3.5000,"publicationDate":"2024-07-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/1873-3468.14979","citationCount":"0","resultStr":"{\"title\":\"Characterization of Arabidopsis aldolases AtFBA4, AtFBA5, and their inhibition by morin and interaction with calmodulin\",\"authors\":\"Kyle Symonds, Milena A. Smith, Oona Esme, William C. Plaxton, Wayne A. Snedden\",\"doi\":\"10.1002/1873-3468.14979\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p>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 <i>Arabidopsis</i> 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 Ca<sup>2+</sup>-dependent manner with high specificity and affinity (<i>K</i><sub>D</sub> ~ 190 n<span>m</span>) and enhanced its stability. AtFBA4 and AtFBA5 exhibited Michaelis–Menten kinetics with <i>K</i><sub>m</sub> and <i>V</i><sub>max</sub> values of 180 μ<span>m</span> and 4.9 U·mg<sup>−1</sup> for AtFBA4, and 6.0 μ<span>m</span> and 0.30 U·mg<sup>−1</sup> for AtFBA5, respectively. The flavonoid morin inhibited both isozymes. Our study suggests that Ca<sup>2+</sup> signaling and flavanols may influence plant glycolysis/gluconeogenesis.</p>\",\"PeriodicalId\":12142,\"journal\":{\"name\":\"FEBS Letters\",\"volume\":\"598 15\",\"pages\":\"1864-1876\"},\"PeriodicalIF\":3.5000,\"publicationDate\":\"2024-07-12\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://onlinelibrary.wiley.com/doi/epdf/10.1002/1873-3468.14979\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"FEBS Letters\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://onlinelibrary.wiley.com/doi/10.1002/1873-3468.14979\",\"RegionNum\":4,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"Biochemistry, Genetics and Molecular Biology\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"FEBS Letters","FirstCategoryId":"99","ListUrlMain":"https://onlinelibrary.wiley.com/doi/10.1002/1873-3468.14979","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"Biochemistry, Genetics and Molecular Biology","Score":null,"Total":0}
Characterization of Arabidopsis aldolases AtFBA4, AtFBA5, and their inhibition by morin and interaction with calmodulin
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 (KD ~ 190 nm) and enhanced its stability. AtFBA4 and AtFBA5 exhibited Michaelis–Menten kinetics with Km and Vmax 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.
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.
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