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Crystal Structure of Transketolase in complex with TPP_V and fructose-6-phosphate from Pichia StipitisCrystal Structure of Transketolase in complex with TPP_V and fructose-6-phosphate from Pichia Stipitis
Structural highlights
Function[TKT_PICST] Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate. Publication Abstract from PubMedTransketolase (TK) catalyzes a reversible transfer of a two-carbon (C2 ) unit between phosphoketose donors and phosphoaldose acceptors, for which the group-transfer reaction that follows a one- or two-electron mechanism and the force that breaks the C2"-C3" bond of the ketose donors remain unresolved. Herein, we report ultrahigh-resolution crystal structures of a TK (TKps) from Pichia stipitis in previously undiscovered intermediate states and support a diradical mechanism for a reversible group-transfer reaction. In conjunction with MS, NMR spectroscopy, EPR and computational analyses, it is concluded that the enzyme-catalyzed non-Kekule diradical cofactor brings about the C2"-C3" bond cleavage/formation for the C2 -unit transfer reaction, for which suppression of activation energy and activation and destabilization of enzymatic intermediates are facilitated. Evidence of Diradicals Involved in the Yeast Transketolase Catalyzed Keto-Transferring Reactions.,Hsu NS, Wang YL, Lin KH, Chang CF, Ke SC, Lyu SY, Hsu LJ, Li YS, Chen SC, Wang KC, Li TL Chembiochem. 2018 Nov 16;19(22):2395-2402. doi: 10.1002/cbic.201800378. Epub 2018, Oct 18. PMID:30155962[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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