Publications by authors named "Antonela E Cereijo"

Article Synopsis
  • The study focuses on two enzymes, GlgAb and GlgAc, from a bacterial genus that play a crucial role in glycogen synthesis and biofuel production through oleaginous behaviors when carbon and nitrogen ratios are optimized.
  • Both enzymes were produced in cells and characterized for their activity, showing that GlgAc is more efficient in using glucose-1P as a substrate compared to GlgAb.
  • Interestingly, GlgAb has a unique structure with a super-oligomeric conformation and displays similar efficiencies in synthesizing oligosaccharides, suggesting a complex relationship between enzyme structure and function in polysaccharide biosynthesis.
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We explored the ability of ADP-glucose pyrophosphorylase (ADP-Glc PPase) from different bacteria to use glucosamine (GlcN) metabolites as a substrate or allosteric effectors. The enzyme from the actinobacteria exhibited marked and distinctive sensitivity to allosteric activation by GlcN-6P when producing ADP-Glc from glucose-1-phosphate (Glc-1P) and ATP. This behavior is also seen in the enzyme from spp.

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Sugar alcohols are major photosynthetic products in plant species from the Apiaceae and Plantaginaceae families. Mannose-6-phosphate reductase (Man6PRase) and aldose-6-phosphate reductase (Ald6PRase) are key enzymes for synthesizing mannitol and glucitol in celery (Apium graveolens) and peach (Prunus persica), respectively. In this work, we report the first crystal structures of dimeric plant aldo/keto reductases (AKRs), celery Man6PRase (solved in the presence of mannonic acid and NADP+) and peach Ald6PRase (obtained in the apo form).

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Glycogen was described as a temporal storage molecule in rhodococci, interconnecting lipids and carbon availability. The Rhodococcus jostii ADP-glucose pyrophosphorylase (ADP-GlcPPase) kinetic and regulatory properties support this role. Curiously, the enzyme uses glucosamine-1P as alternative substrate.

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ADP-glucose pyrophosphorylase from is encoded by two genes ( and ) leading to a heterotetrameric protein structure, unlike those in other bacterial phyla. The enzymes from two groups of , and , present dissimilar kinetic and regulatory properties. Nevertheless, no ADP-glucose pyrophosphorylase from , the third group in , has been characterized.

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Rhodococcus spp. are oleaginous bacteria that accumulate glycogen during exponential growth. Despite the importance of these microorganisms in biotechnology, little is known about the regulation of carbon and energy storage, mainly the relationship between glycogen and triacylglycerols metabolisms.

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