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首页> 外文期刊>febs open bio >Crystal structure of a novel homodimeric l-ribulose 3-epimerase from Methylomonus sp.
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Crystal structure of a novel homodimeric l-ribulose 3-epimerase from Methylomonus sp.

机译：Crystal structure of a novel homodimeric l-ribulose 3-epimerase from Methylomonus sp.

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d -Allulose has potential as a low-calorie sweetener which can suppress fat accumulation. Several enzymes capable of d -allulose production have been isolated, including d -tagatose 3-epimerases. Here, we report the isolation of a novel protein from Methylomonas sp. expected to be a putative enzyme based on sequence similarity to ketose 3-epimerase. The synthesized gene encoding the deduced ketose 3-epimerase was expressed as a recombinant enzyme in Escherichia coli , and it exhibited the highest enzymatic activity toward l -ribulose, followed by d -ribulose and d -allulose. The X-ray structure analysis of l -ribulose 3-epimerase from Methylomonas sp. (MetLRE) revealed a homodimeric enzyme, the first reported structure of dimeric l -ribulose 3-epimerase. The monomeric structure of MetLRE is similar to that of homotetrameric l -ribulose 3-epimerases, but the short C-terminal α-helix of MetLRE is unique and different from those of known l -ribulose 3 epimerases. The length of the C-terminal α-helix was thought to be involved in tetramerization and increasing stability; however, the addition of residues to MetLRE at the C terminus did not lead to tetramer formation. MetLRE is the first dimeric l -ribulose 3-epimerase identified to exhibit high relative activity toward d -allulose.

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