ArticleThe Journal of biological chemistry2010
Structure and activity of the metal-independent fructose-1,6-bisphosphatase YK23 from Saccharomyces cerevisiae.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Investigating Overflow Metabolism in Heterotrophic Cultures of the Green AlgabioRxiv : the preprint server for biology · 2025Article
- The bloodstream form of Trypanosoma brucei displays non-canonical gluconeogenesis.PLoS neglected tropical diseases · 2024Article
- A novel gluconeogenic route enables efficient use of erythritol in zoonoticFrontiers in veterinary science · 2024Article
- Fructose-1,6-bisphosphatase 1 dephosphorylates IκBα and suppresses colorectal tumorigenesis.Cell research · 2023Article
- Fructose 1,6-Bioscience reports · 2019Article
- Gluconeogenesis is essential for trypanosome development in the tsetse fly vector.PLoS pathogens · 2018Article
- Discovery and Functional Characterization of a Yeast Sugar Alcohol Phosphatase.ACS chemical biology · 2018Article
- Two enzymes with redundant fructose bisphosphatase activity sustain gluconeogenesis and virulence in Mycobacterium tuberculosis.Nature communications · 2015Article
- Functional Diversity of Haloacid Dehalogenase Superfamily Phosphatases from Saccharomyces cerevisiae: BIOCHEMICAL, STRUCTURAL, AND EVOLUTIONARY INSIGHTS.The Journal of biological chemistry · 2015Article
- Functional characterization of two members of histidine phosphatase superfamily in Mycobacterium tuberculosis.BMC microbiology · 2013Article
- Biochemical characterization and functional analysis of fructose-1,6-bisphosphatase from Clonorchis sinensis.Molecular biology reports · 2013Article
- Nucleotide degradation and ribose salvage in yeast.Molecular systems biology · 2013Article
- Crystallization and preliminary X-ray diffraction analysis of the invertase from Saccharomyces cerevisiae.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
- Proteomic analysis of excretory secretory products from Clonorchis sinensis adult worms: molecular characterization and serological reactivity of a excretory-secretory antigen-fructose-1,6-bisphosphatase.Parasitology research · 2011Article
- Structure and activity of the Saccharomyces cerevisiae dUTP pyrophosphatase DUT1, an essential housekeeping enzyme.The Biochemical journal · 2011Article
- Riboneogenesis in yeast.Cell · 2011Article
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Authors and funding
11 authors.
Funding
Abstract
Fructose-1,6-bisphosphatase (FBPase), a key enzyme of gluconeogenesis and photosynthetic CO(2) fixation, catalyzes the hydrolysis of fructose 1,6-bisphosphate (FBP) to produce fructose 6-phosphate, an important precursor in various biosynthetic pathways. All known FBPases are metal-dependent enzymes, which are classified into five different classes based on their amino acid sequences. Eukaryotes are known to contain only the type-I FBPases, whereas all five types exist in various combinations in prokaryotes. Here we demonstrate that the uncharacterized protein YK23 from Saccharomyces cerevisiae efficiently hydrolyzes FBP in a metal-independent reaction. YK23 is a member of the histidine phosphatase (phosphoglyceromutase) superfamily with homologues found in all organisms. The crystal structure of the YK23 apo-form was solved at 1.75-A resolution and revealed the core domain with the alpha/beta/alpha-fold covered by two small cap domains. Two liganded structures of this protein show the presence of two phosphate molecules (an inhibitor) or FBP (a substrate) bound to the active site. FBP is bound in its linear, open conformation with the cleavable C1-phosphate positioned deep in the active site. Alanine replacement mutagenesis of YK23 identified six conserved residues absolutely required for activity and suggested that His(13) and Glu(99) are the primary catalytic residues. Thus, YK23 represents the first family of metal-independent FBPases and a second FBPase family in eukaryotes.
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