Izumoring: A Novel and Complete Strategy for Bioproduction of Rare Sugars

Granström, Tom; Takata, Goro; Tokuda, Masaaki; Izumori, Ken

doi:10.1263/jbb.97.89

Cited by 132 publications

(170 citation statements)

References 34 publications

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“…43 However, rare sugars are very demanded in the preparation of antiviral drugs, anti-inflammatory agents, and as chiral building blocks. 44 Most of the synthesis processes of rare sugars from abundant ones involve biochemical processes, where different enzymes are used (epimerases).…”

Section: 2-sugar Epimerization To Synthesize Rare Sugarsmentioning

confidence: 99%

State of the art of Lewis acid-containing zeolites: lessons from fine chemistry to new biomass transformation processes

2014

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Section: 2-sugar Epimerization To Synthesize Rare Sugarsmentioning

confidence: 99%

State of the art of Lewis acid-containing zeolites: lessons from fine chemistry to new biomass transformation processes

2014

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“…It constitutes the central enzyme for biocatalytic access to rare monosaccharides, which have recently attracted great interest as low calorie sweeteners, chiral building blocks or as active pharmaceutical ingredients [7] . By combining DTE with maximally two additional isomerases, the whole set of 24 hexoses can be generated in a short cascade reaction from only 4 starting materials that are cheaply available (D-glucose, D-fructose, D-galactose, L-sorbose) [8] . D-Tagatose epimerases from various organisms are known to date [9] , however none of them exhibits catalytic rates on the respective substrates that would make them attractive for application in an industrial context.…”

Section: Introductionmentioning

confidence: 99%

Directed Divergent Evolution of a Thermostable D‐Tagatose Epimerase towards Improved Activity for Two Hexose Substrates

et al. 2015

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Abstract:We exploit the functional promiscuity of an engineered thermostable variant of a promiscuous D-tagatose epimerase (DTE Var8) to morph it into two efficient catalysts for the C3 epimerization of D-fructose to D-psicose and of L-sorbose to L-tagatose. Iterative single-site randomization and screening of 48 residues in the first and second shell around the substrate binding site of Var8 yielded 8-sites mutant IDF8 with an 9-fold improved kcat for the epimerization of D-fructose, and the 6-sites mutant ILS6 with an 14-fold improved epimerization of L-sorbose compared to Var8. Structure analysis of IDF8 revealed a charged patch at the entrance of its active site that supposedly facilitates the entry of the polar substrate, whereas the improvement in variant ILS6 is thought to relate to subtle changes in the hydration of the bound substrate. The structures will inform future engineering efforts of these and other isomerizing enzymes for the production of rare.

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“…It is therefore hoped that d-TE family enzymes can serve as useful catalysts for the commercially viable production of rare sugars (Granströ m et al, 2004;Izumori, 2006). d-TE from Pseudomonas cichorii efficiently converts not only d-tagatose to d-sorbose but also d-fructose to d-psicose (Itoh et al, 1994).…”

Section: Introductionmentioning

confidence: 99%

Structure ofD-tagatose 3-epimerase-like protein fromMethanocaldococcus jannaschii

et al. 2014

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PDB reference: D-tagatose 3-epimerase-like protein, 3wqoThe crystal structure of a d-tagatose 3-epimerase-like protein (MJ1311p) encoded by a hypothetical open reading frame, MJ1311, in the genome of the hyperthermophilic archaeon Methanocaldococcus jannaschii was determined at a resolution of 2.64 Å . The asymmetric unit contained two homologous subunits, and the dimer was generated by twofold symmetry. The overall fold of the subunit proved to be similar to those of the d-tagatose 3-epimerase from Pseudomonas cichorii and the d-psicose 3-epimerases from Agrobacterium tumefaciens and Clostridium cellulolyticum. However, the situation at the subunit-subunit interface differed substantially from that in d-tagatose 3-epimerase family enzymes. In MJ1311p, Glu125, Leu126 and Trp127 from one subunit were found to be located over the metal-ion-binding site of the other subunit and appeared to contribute to the active site, narrowing the substratebinding cleft. Moreover, the nine residues comprising a trinuclear zinc centre in endonuclease IV were found to be strictly conserved in MJ1311p, although a distinct groove involved in DNA binding was not present. These findings indicate that the active-site architecture of MJ1311p is quite unique and is substantially different from those of d-tagatose 3-epimerase family enzymes and endonuclease IV.

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Izumoring: A Novel and Complete Strategy for Bioproduction of Rare Sugars

Cited by 132 publications

References 34 publications

State of the art of Lewis acid-containing zeolites: lessons from fine chemistry to new biomass transformation processes

State of the art of Lewis acid-containing zeolites: lessons from fine chemistry to new biomass transformation processes

Directed Divergent Evolution of a Thermostable D‐Tagatose Epimerase towards Improved Activity for Two Hexose Substrates

Structure ofD-tagatose 3-epimerase-like protein fromMethanocaldococcus jannaschii

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