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Structural elements of cyanobacterial co-factor-independent phosphoglycerate mutase that mediate regulation by PirC
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Structural elements of cyanobacterial co-factor-independent phosphoglycerate mutase that mediate regulation by PirC
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Journal Article
Structural elements of cyanobacterial co-factor-independent phosphoglycerate mutase that mediate regulation by PirC
2025
Overview
The primordial cyanobacteria were responsible for developing oxygenic photosynthesis early in evolution. In the pathways of fixed carbon allocation, the co-factor-independent phosphoglycerate mutase (iPGAM) plays a crucial role by directing the first CO 2 fixation product, 3-phosphoglycerate, toward central anabolic glycolytic-derived pathways. This work reveals a distinct evolution of iPGAM within oxygenic photosynthetic organisms. We have identified two specific segments in cyanobacterial iPGAMs that affect the control of iPGAM activity through its specific interactor protein PirC. This understanding of iPGAM has allowed us to engineer cyanobacterial strains with altered carbon fluxes. Since cyanobacteria can directly convert CO 2 into valuable products, our results demonstrate a novel approach for developing a chassis for biotechnical use.
Publisher
American Society for Microbiology
Subject
/ Bacterial Proteins - chemistry
/ Bacterial Proteins - genetics
/ Bacterial Proteins - metabolism
/ Enzymes
/ Gene Expression Regulation, Bacterial
/ iPGAM
/ Kinases
/ Nitrogen
/ Phosphoglycerate Mutase - chemistry
/ Phosphoglycerate Mutase - genetics
/ Phosphoglycerate Mutase - metabolism
/ PII
/ PirC
/ Proteins
