Enzymes of an alternative pathway of glucose metabolism in obligate methanotrophs

Rozova, Olga N.; Ekimova, Galina A.; Molochkov, Nikolai V.; Reshetnikov, A. S.; Khmelenina, V. N.; Mustakhimov, Ildar I.

doi:10.1038/s41598-021-88202-x

Cited by 6 publications

(1 citation statement)

References 41 publications

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“…561 The LUCA has been predicted/proposed to be an anaerobe. 562−564 Several strict anaerobes are known to produce glycogen, 565,566 while glycogen metabolism enzymes were identified in anaerobic hyperthermophile bacteria from the genera Thermotogales and Aquifex. 567,568 The reconstruction of the tree of life also suggests that the LUCA was a thermophile, 569 which is consistent with the hypothesis of the origin of life at hydrothermal vents.…”

Section: Considerations On the Origin Of Glycogen Metabolism In Bacteriamentioning

confidence: 99%

Architecture, Function, Regulation, and Evolution of α-Glucans Metabolic Enzymes in Prokaryotes

Cifuente,

Colleoni,

Kalscheuer

et al. 2024

Chem. Rev.

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Bacteria have acquired sophisticated mechanisms for assembling and disassembling polysaccharides of different chemistry. α-D-Glucose homopolysaccharides, so-called α-glucans, are the most widespread polymers in nature being key components of microorganisms. Glycogen functions as an intracellular energy storage while some bacteria also produce extracellular assorted α-glucans. The classical bacterial glycogen metabolic pathway comprises the action of ADP-glucose pyrophosphorylase and glycogen synthase, whereas extracellular α-glucans are mostly related to peripheral enzymes dependent on sucrose. An alternative pathway of glycogen biosynthesis, operating via a maltose 1phosphate polymerizing enzyme, displays an essential wiring with the trehalose metabolism to interconvert disaccharides into polysaccharides. Furthermore, some bacteria show a connection of intracellular glycogen metabolism with the genesis of extracellular capsular α-glucans, revealing a relationship between the storage and structural function of these compounds. Altogether, the current picture shows that bacteria have evolved an intricate α-glucan metabolism that ultimately relies on the evolution of a specific enzymatic machinery. The structural landscape of these enzymes exposes a limited number of core catalytic folds handling many different chemical reactions. In this Review, we present a rationale to explain how the chemical diversity of α-glucans emerged from these systems, highlighting the underlying structural evolution of the enzymes driving α-glucan bacterial metabolism.

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