ArticleBiochemistry2013
Discovery of an L-fucono-1,5-lactonase from cog3618 of the amidohydrolase superfamily.
Article in Biochemistry, 2013. 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, 30 citations in OpenAlex.
- Orphan Enzymes in the Mammalian L-Fucose Degradation Pathway.Biomolecules · 2026Review
- Identification, functional characterization, and structural analysis of an atypical l-threonate 3-dehydrogenase.The Journal of biological chemistry · 2026Article
- WrtF fromProceedings of the National Academy of Sciences of the United States of America · 2025Article
- An l-fucose-responsive transcription factor cross-regulates the expression of a diverse array of carbohydrate-active enzymes in Trichoderma reesei.PLoS genetics · 2025Article
- Interactive tools for functional annotation of bacterial genomes.Database : the journal of biological databases and curation · 2024Article
- Crystal structure of L-2-keto-3-deoxyfuconate 4-dehydrogenase reveals a unique binding mode as a α-furanosyl hemiketal of substrates.Scientific reports · 2024Article
- Niche differentiation within bacterial key-taxa in stratified surface waters of the Southern Pacific Gyre.The ISME journal · 2024Article
- Construction of a synthetic metabolic pathway for biosynthesis of 2,4-dihydroxybutyric acid from ethylene glycol.Nature communications · 2023Article
- Comparative Analysis of the IclR-Family of Bacterial Transcription Factors and Their DNA-Binding Motifs: Structure, Positioning, Co-Evolution, Regulon Content.Frontiers in microbiology · 2021Article
- The gastrointestinal pathogen Campylobacter jejuni metabolizes sugars with potential help from commensal Bacteroides vulgatus.Communications biology · 2020Article
- Novel non-phosphorylative pathway of pentose metabolism from bacteria.Scientific reports · 2019Article
- Comparative Genomic Analysis of the Human Gut Microbiome Reveals a Broad Distribution of Metabolic Pathways for the Degradation of Host-Synthetized Mucin Glycans and Utilization of Mucin-Derived Monosaccharides.Frontiers in genetics · 2017Article
- Enzyme Function Initiative-Enzyme Similarity Tool (EFI-EST): A web tool for generating protein sequence similarity networks.Biochimica et biophysica acta · 2015Review
- Function discovery and structural characterization of a methylphosphonate esterase.Biochemistry · 2015Article
- Article
- Substrate deconstruction and the nonadditivity of enzyme recognition.Journal of the American Chemical Society · 2014Article
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9 authors at 2 institutions in 1 country.
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Abstract
A member of the amidohydrolase superfamily, BmulJ_04915 from Burkholderia multivorans, of unknown function was determined to hydrolyze a series of sugar lactones: L-fucono-1,4-lactone, D-arabino-1,4-lactone, L-xylono-1,4-lactone, D-lyxono-1,4-lactone, and L-galactono-1,4-lactone. The highest activity was shown for L-fucono-1,4-lactone with a k(cat) value of 140 s(-1) and a k(cat)/K(m) value of 1.0 × 10(5) M(-1) s(-1) at pH 8.3. The enzymatic product of an adjacent L-fucose dehydrogenase, BmulJ_04919, was shown to be L-fucono-1,5-lactone via nuclear magnetic resonance spectroscopy. L-Fucono-1,5-lactone is unstable and rapidly converts nonenzymatically to L-fucono-1,4-lactone. Because of the chemical instability of L-fucono-1,5-lactone, 4-deoxy-L-fucono-1,5-lactone was enzymatically synthesized from 4-deoxy-L-fucose using L-fucose dehydrogenase. BmulJ_04915 hydrolyzed 4-deoxy-L-fucono-1,5-lactone with a k(cat) value of 990 s(-1) and a k(cat)/K(m) value of 8.0 × 10(6) M(-1) s(-1) at pH 7.1. The protein does not require divalent cations in the active site for catalytic activity. BmulJ_04915 is the second enzyme from cog3618 of the amidohydrolase superfamily that does not require a divalent metal for catalytic activity. BmulJ_04915 is the first enzyme that has been shown to catalyze the hydrolysis of either L-fucono-1,4-lactone or L-fucono-1,5-lactone. The structures of the fuconolactonase and the fucose dehydrogenase were determined by X-ray diffraction methods.
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