ReviewApplied microbiology and biotechnology2024
The many functions of carbohydrate-active enzymes in family GH65: diversity and application.
Review in Applied microbiology and biotechnology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed.
- Discovery of a Thermostable Nigerose Phosphorylase for the Efficient Chemoenzymatic Radiosynthesis of aJournal of nuclear medicine : official publication, Society of Nuclear Medicine · 2026Article
- Detecting Bacteria in Their Mammalian Hosts Using Metabolism-Targeted [ACS central science · 2026Article
- Article
- Dual-Activity Mannosyltransferase Phosphorylases in Family 130 of Glycoside Hydrolases.ACS catalysis · 2026Article
- Flavor compounds regulation in rice-flavor Baijiu byFrontiers in microbiology · 2026Article
- Diversity, metabolic potential and global distribution of the anaerobic fermentative bacteria Phylum Candidatus Cloacimonadota.Environmental microbiome · 2025Article
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Authors and funding
3 authors.
Funding
Abstract
Glycoside Hydrolase family 65 (GH65) is a unique family of carbohydrate-active enzymes. It is the first protein family to bring together glycoside hydrolases, glycoside phosphorylases and glycosyltransferases, thereby spanning a broad range of reaction types. These enzymes catalyze the hydrolysis, reversible phosphorolysis or synthesis of various α-glucosides, typically α-glucobioses or their derivatives. In this review, we present a comprehensive overview of the diverse reaction types and substrate specificities found in family GH65. We describe the determinants that control this remarkable diversity, as well as the applications of GH65 enzymes for carbohydrate synthesis.
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Registered trials
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