8j5d

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Current revision (06:13, 23 July 2025) (edit) (undo)
 
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== Function ==
== Function ==
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[https://www.uniprot.org/uniprot/MDHP_ARATH MDHP_ARATH] Catalyzes a reversible NAD-dependent dehydrogenase reaction involved in central metabolism and redox homeostasis between organelle compartments (Probable). Plays a key role in the metabolism of dark chloroplasts and non-green plastids. Essential for embryo viability (PubMed:24198233, PubMed:24453164). Plays an essential role in heterotrophic metabolism in embryos, and autotrophic metabolism in photosynthetic tissues as well (PubMed:24453164).<ref>PMID:24198233</ref> <ref>PMID:24453164</ref> <ref>PMID:20876337</ref>
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[https://www.uniprot.org/uniprot/BAM1_ARATH BAM1_ARATH] Beta-amylase activity. Can use p-nitrophenyl maltopentaoside (PNPG5) as substrate only in reduced form. Can play a minor role in the starch degradation and maltose metabolism in chloroplasts during the night. More active on phosphorylated glucan. Interacts directly with starch or other alpha-1,4-glucan.<ref>PMID:17631522</ref> <ref>PMID:18390594</ref> <ref>PMID:19664588</ref>
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== Publication Abstract from PubMed ==
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In plant leaves, starch is composed of glucan polymers that accumulate in chloroplasts as the products of photosynthesis during the day; starch is mobilized at night to continuously provide sugars to sustain plant growth and development. Efficient starch degradation requires the involvement of several enzymes, including beta-amylase and glucan phosphatase. However, how these enzymes cooperate remains largely unclear. Here, we show that the glucan phosphatase LIKE SEX FOUR 1 (LSF1) interacts with plastid NAD-dependent malate dehydrogenase (MDH) to recruit beta-amylase (BAM1), thus reconstituting the BAM1-LSF1-MDH complex. The starch hydrolysis activity of BAM1 drastically increased in the presence of LSF1-MDH in vitro. We determined the structure of the BAM1-LSF1-MDH complex by a combination of cryo-electron microscopy, crosslinking mass spectrometry, and molecular docking. The starch-binding domain of the dual-specificity phosphatase and carbohydrate-binding module of LSF1 was docked in proximity to BAM1, thus facilitating BAM1 access to and hydrolysis of the polyglucans of starch, thus revealing the molecular mechanism by which the LSF1-MDH complex improves the starch degradation activity of BAM1. Moreover, LSF1 is phosphatase inactive, and the enzymatic activity of MDH was dispensable for starch degradation, suggesting nonenzymatic scaffold functions for LSF1-MDH in starch degradation. These findings provide important insights into the precise regulation of starch degradation.
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The LIKE SEX FOUR 1-malate dehydrogenase complex functions as a scaffold to recruit beta-amylase to promote starch degradation.,Liu J, Wang X, Guan Z, Wu M, Wang X, Fan R, Zhang F, Yan J, Liu Y, Zhang D, Yin P, Yan J Plant Cell. 2023 Dec 21;36(1):194-212. doi: 10.1093/plcell/koad259. PMID:37804098<ref>PMID:37804098</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
== References ==
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Current revision

Cryo-EM structure of starch degradation complex of BAM1-LSF1-MDH

PDB ID 8j5d

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