Conformational changes in ketohexokinase are conserved across isozymes and species.

ABSTRACT: Ketohexokinase (KHK) catalyses the initial step in fructose metabolism, converting the furanose form of D-fructose to fructose 1-phosphate in an ATP-dependent reaction. Given its central role in metabolic pathways, KHK has emerged as a target for pharmacological intervention in the treatment of non-alcoholic fatty liver disease, metabolic syndrome, type 2 diabetes and obesity. KHK exists as two isoforms, A and C, which arise from alternative splicing of exon 3, resulting in a differing 45-amino-acid sequence within the 298-amino-acid primary structure of the enzyme. KHK is a biological homodimer, with each subunit adopting an α/β-fold architecture that interlocks with a β-clasp domain. In the case of KHK-C at least two distinct conformations of the β-clasp domain have been identified, wher

SUBMITTER: Bae SY 

PROVIDER: S-EPMC12576689 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature