ArticlebioRxiv : the preprint server for biology2025
Functional Characterization of Arabidopsis α-Amylase3 (AMY3): Amylose Specificity and Structural Insights into Its Duplex Carbohydrate-Binding Module.
Article in bioRxiv : the preprint server for biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Flowering plants contain a plastid-localized ɑ-amylase (AMY3) with several recognized domains: two N-terminal carbohydrate-binding modules, an alpha-alpha hairpin that binds the catalytically inactive activator β-amylase9, and a C-terminal catalytic domain. Despite considerable research on leaf starch metabolism in Arabidopsis, little is known about the function of AMY3. Starch is composed of two glucose polymers: highly branched amylopectin (70-90%) and largely unbranched amylose (10-30%). Because ɑ-amylases are endo-amylases, we predicted that AMY3 might prefer to hydrolyze amylose, in contrast to the exo-amylase β-amylase1 (BAM1), which we predicted would prefer amylopectin. Using iodine spectroscopy, we observed that AMY3 caused the percent amylose of corn starch to decrease, whereas BAM1 caused the percent amylose to increase before a gradual decrease. Enzyme assays revealed that AMY3 has a higher affinity for amylose compared to amylopectin, whereas BAM1 has a higher affinity for amylopectin. Furthermore, we found that the starch in
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