| Description: |
This dataset describes binary donor specificity of GT1-family glycosyltransferases across a range of acceptor molecules. It was compiled through manual curation of published data from the literature, as specified in the References. The dataset comprises 218 unique GT1 enzyme sequences, 10 distinct donor sugars, and 108 acceptor compounds, yielding 1189 curated enzyme-donor-acceptor activity records. When different literature sources reported conflicting outcomes for the same enzymatic reaction, the reaction was classified as active if at least one source reported a positive result, regardless of other conflicting reports. This approach ensures the dataset reflects the most permissive interpretation of enzyme activity. Additionally, if the measured activity for a given donor-acceptor pair was less than 5% of the activity observed with the enzyme’s most active donor-acceptor pair, the reaction was considered inactive. The dataset is provided in two complementary formats: .xlsx (for visual inspection) A human-readable spreadsheet where each row represents a unique enzyme-acceptor pair, and activity against multiple donors is given across separate columns (Glc, Gal, Glu, Rha, GlcNAc, etc.). Binary activity values (1/0) are colour-coded (green = active, red = inactive) to aid quick interpretation. Columns: Plant: The source organism (species) from which the GT1 enzyme was derived. UGT: The name or identifier of the glycosyltransferase (UGT) enzyme, often following gene naming conventions. Uniprot/Genbank: A unique accession ID referencing the enzyme’s sequence in UniProt or GenBank databases. Glc, Gal, Glu, Rha, GlcNAc, Xyl, Ara, GalNAc, GalUA, Man: Binary activity values (0 = inactive, 1 = active) indicating whether the enzyme accepted each of these donor sugars when combined with the listed acceptor. Glc: Glucose Gal: Galactose Glu: Glucuronic acid Rha: Rhamnose GlcNAc: N-acetylglucosamine Xyl: Xylose Ara: Arabinose GalNAc: N-acetylgalactosamine GalUA: Galacturonic acid Man: Mannose Substrate: The name of the ... |