ArticleBiochemical and biophysical research communications2016
A systematic analysis of acceptor specificity and reaction kinetics of five human α(2,3)sialyltransferases: Product inhibition studies illustrate reaction mechanism for ST3Gal-I.
Article in Biochemical and biophysical research communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers, 1 of them a synthesis that pooled it.
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Who cites it
25 citing papers in PubMed, 1 synthesis or guideline pooled it, 28 citations in OpenAlex.
- Pooled it
- From Glycocode to Precision Oncology: Therapeutic Strategies Targeting Aberrant O-GalNAc Glycosylation in Cancer.Chemical reviews · 2026Review
- Mapping ST3GAL transferase specificities in the glycosylation landscape of N/TERT-1 keratinocytes using Glycogenomics and mass spectrometry.Glycobiology · 2026Article
- CRISPR activation screens map the genomic landscape of cancer glycome remodeling.Cell genomics · 2026Article
- Identification of β4GALNT2 as an anti-hPIV3 factor through genome-wide CRISPR/Cas9 library screening.Emerging microbes & infections · 2025Article
- Engineering glycosyltransferases into glycan binding proteins using a mammalian surface display platform.Nature communications · 2025Article
- Mammalian Cell Surface Display for High-Throughput Protein Engineering of Glycosyltransferases.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
- Article
- Glycosyltransferases: glycoengineers in human milk oligosaccharide synthesis and manufacturing.Frontiers in molecular biosciences · 2025Review
- Glycosphingolipids: from metabolism to chemoenzymatic total synthesis.Organic & biomolecular chemistry · 2024Review
- One-pot multienzyme (OPME) chemoenzymatic synthesis of brain ganglioside glycans with human ST3GAL II expressed inChemCatChem · 2022Article
- Cellular and Molecular Engineering of Glycan Sialylation in Heterologous Systems.Molecules (Basel, Switzerland) · 2021Review
- Aberrant Sialylation in Cancer: Biomarker and Potential Target for Therapeutic Intervention?Cancers · 2021Review
- A Markov model of glycosylation elucidates isozyme specificity and glycosyltransferase interactions for glycoengineering.Current research in biotechnology · 2020Article
- Knockdown of α2,3-Sialyltransferases Impairs Pancreatic Cancer Cell Migration, Invasion and E-selectin-Dependent Adhesion.International journal of molecular sciences · 2020Article
- Robustness in glycosylation systems: effect of modified monosaccharides, acceptor decoys and azido sugars on cellular nucleotide-sugar levels and pattern of N-linked glycosylation.Molecular omics · 2020Article
- Promiscuity and specificity of eukaryotic glycosyltransferases.Biochemical Society transactions · 2020Review
- Global analysis of human glycosyltransferases reveals novel targets for pancreatic cancer pathogenesis.British journal of cancer · 2020Article
- The Human Lung Glycome Reveals Novel Glycan Ligands for Influenza A Virus.Scientific reports · 2020Article
- Cell Line-, Protein-, and Sialoglycosite-Specific Control of Flux-Based Sialylation in Human Breast Cells: Implications for Cancer Progression.Frontiers in chemistry · 2020Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Sialyltransferases (STs) catalyze the addition of sialic acids to the non-reducing ends of glycoproteins and glycolipids. In this work, we examined the acceptor specificity of five human α(2,3)sialyltransferases, namely ST3Gal -I, -II, -III, -IV and -VI. KM values for each of these enzymes is presented using radioactivity for acceptors containing Type-I (Galβ1,3GlcNAc), Type-II (Galβ1,4GlcNAc), Type-III (Galβ1,3GalNAc) and Core-2 (Galβ1,3(GlcNAcβ1,6)GalNAc) reactive groups. Several variants of acceptors inhibited ST3Gal activity emphasizing structural role of acceptor in enzyme-catalyzed reactions. In some cases, mass spectrometry was performed for structural verification. The results demonstrate human ST3Gal-I catalysis towards Type-III and Core-2 acceptors with KM = 5-50 μM and high VMax values. The KM for ST3Gal-I and ST3Gal-II was 100 and 30-fold lower, respectively, for Type-III compared to Type-I acceptors. Variants of Type-I and Type-II structures characterized ST3Gal-III, -IV and -VI for their catalytic specificity. This manuscript also estimates KM for human ST3Gal-VI using Type-I and Type-II substrates. Together, these findings built a platform for designing inhibitors of STs having therapeutic potential.
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