Journal
FEBS OPEN BIO
Volume 11, Issue 6, Pages 1621-1637Publisher
WILEY
DOI: 10.1002/2211-5463.13159
Keywords
D-allulose; D-allulose 3-epimerase; L-ribulose 3 epimerase; rare sugar; X-ray structure; beta/alpha-barrel
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Funding
- Seeds Development Research Fund (Emergence type) of Kagawa University Research Promotion Program 2019 (KURPP)
- grant for rare sugar research and development for 20172019 from Kagawa Prefecture
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d-Allulose has been identified as a potential low-calorie sweetener with the ability to suppress fat accumulation. A novel protein from Methylomonas sp. has been isolated and identified as a putative enzyme with high relative activity towards d-allulose. Structural analysis of the enzyme reveals unique features and differences compared to known enzymes.
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 alpha-helix of MetLRE is unique and different from those of known l-ribulose 3 epimerases. The length of the C-terminal alpha-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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