GO:0008761 UDP-N-acetylglucosamine 2-epimerase activity: Mechanism, Genes and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0008761 describes the molecular function that catalyzes the reversible interconversion of UDP-N-acetyl-D-glucosamine (UDP-GlcNAc) and UDP-N-acetyl-D-mannosamine (UDP-ManNAc).
• The human enzyme carrying this activity is the bifunctional GNE protein, which also possesses N-acetylmannosamine kinase activity.
• Bacterial UDP-GlcNAc 2-epimerases are divided into hydrolyzing and non-hydrolyzing classes, with distinct catalytic mechanisms.
• The reaction product UDP-ManNAc is essential for bacterial cell wall and capsule biosynthesis, making the enzyme a potential antibacterial target.
• Mutations in the human GNE gene cause GNE myopathy, a progressive adult-onset muscle disorder.
• Small-molecule inhibitors and structural studies are active areas for probing this enzyme's mechanism and therapeutic potential.
Description
UDP-N-acetylglucosamine 2-epimerase activity (GO:0008761) is a molecular function that catalyzes the reversible epimerization of UDP-N-acetyl-D-glucosamine (UDP-GlcNAc) to UDP-N-acetyl-D-mannosamine (UDP-ManNAc). This reaction is a key step in the biosynthesis of sialic acid in humans and in the production of cell envelope components in many bacteria. The enzyme responsible in humans is a bifunctional protein, GNE, which also phosphorylates N-acetylmannosamine. In bacteria, the activity is often found as a standalone enzyme and is classified as either hydrolyzing or non-hydrolyzing depending on whether the reaction proceeds with release of free UDP. Researchers study GO:0008761 because of its central role in sialic acid biology and bacterial pathogenesis. In humans, mutations in GNE cause GNE myopathy, an adult-onset progressive muscle weakness disorder. In bacteria, the enzyme is required for the synthesis of UDP-ManNAc, a precursor for capsular polysaccharides and teichoic acids, and is therefore a target for antibiotic development. Structural and mechanistic studies have revealed that the enzyme belongs to the phosphoglycosyl transferase superfamily and undergoes a large domain movement during catalysis. Understanding the detailed mechanism, regulation, and inhibition of UDP-N-acetylglucosamine 2-epimerase activity is essential for developing therapies for GNE myopathy and for combating bacterial infections. This article summarizes the current knowledge based on QuickGO annotation and verified PubMed literature.
UDP-N-acetylglucosamine 2-epimerase activity At A Glance
| GO ID | GO:0008761 |
|---|---|
| GO term | UDP-N-acetylglucosamine 2-epimerase activity |
| Ontology | molecular_function |
| Synonym | UDP-GlcNAc-2-epimerase activity; UDP-N-acetyl-D-glucosamine 2-epimerase activity; UDP-N-acetylglucosamine 2'-epimerase activity; uridine diphosphate-N-acetylglucosamine-2'-epimerase activity; uridine diphosphoacetylglucosamine 2'-epimerase activity; uridine diphospho-N-acetylglucosamine 2'-epimerase activity |
| Major function | Catalyzes the reversible epimerization of UDP-N-acetyl-D-glucosamine to UDP-N-acetyl-D-mannosamine |
| Reaction | UDP-N-acetyl-D-glucosamine = UDP-N-acetyl-D-mannosamine |
| Human gene | GNE (bifunctional enzyme with kinase activity) |
| Bacterial examples | Escherichia coli, Neisseria meningitidis, Staphylococcus aureus |
| Related pathways | Sialic acid biosynthesis; bacterial cell wall and capsule biosynthesis |
What Is GO:0008761?
UDP-N-acetylglucosamine 2-epimerase activity is defined as the catalysis of the reaction: UDP-N-acetyl-D-glucosamine = UDP-N-acetyl-D-mannosamine. In other words, it is an enzyme activity that converts UDP-GlcNAc to its epimer UDP-ManNAc by inverting the stereochemistry at the 2-position of the sugar moiety. This activity is classified under the molecular_function aspect of the Gene Ontology with the identifier GO:0008761.
Why Is UDP-N-acetylglucosamine 2-epimerase activity Important in Cell Biology?
UDP-N-acetylglucosamine 2-epimerase activity is important because it sits at the branch point between amino sugar metabolism and sialic acid biosynthesis in humans, and between cell wall precursor synthesis and capsule formation in bacteria. In humans, the bifunctional GNE enzyme is the rate-limiting step for sialic acid production, and its dysfunction leads to GNE myopathy. In bacteria, the enzyme provides UDP-ManNAc for essential surface structures, and its inhibition could lead to new antibiotics. Thus, understanding this activity has direct implications for human health and infectious disease.
• Mutations in the human GNE gene cause GNE myopathy, a progressive muscle-wasting disease.
• The enzyme is a key regulator of sialic acid biosynthesis, affecting cell signaling and immune recognition.
• Bacterial UDP-GlcNAc 2-epimerases are essential for cell wall and capsule formation, making them antibacterial targets.
• The hydrolyzing bacterial enzyme from Escherichia coli represents a distinct mechanism from the human enzyme.
• Non-hydrolyzing bacterial enzymes, such as that from Neisseria meningitidis, are structurally and mechanistically characterized.
• Domain movement in Staphylococcus aureus enzyme is critical for catalysis and is studied by molecular dynamics.
• Small-molecule inhibitors of the human enzyme are being developed as research tools.
• The enzyme belongs to the phosphoglycosyl transferase superfamily, linking it to diverse glycosyltransferases.
• Glycation of GNE can interfere with its activity, linking diabetes to sialic acid metabolism.
• The activity is conserved across species, from bacteria to humans, making model organisms valuable for study.
Molecular Mechanism of UDP-N-acetylglucosamine 2-epimerase activity
Substrate Binding and Specificity
In simple terms: The enzyme grabs UDP-GlcNAc and holds it in place to flip one part of the sugar.
The enzyme binds UDP-N-acetyl-D-glucosamine (UDP-GlcNAc) as its primary substrate. Structural studies of the Escherichia coli enzyme revealed that it belongs to the phosphoglycosyl transferase superfamily and shares a common fold with other enzymes that act on nucleotide sugars. The active site accommodates the UDP moiety and the N-acetyl group, positioning the sugar for epimerization at the 2-position. Bacterial enzymes can be classified as hydrolyzing or non-hydrolyzing; the hydrolyzing enzyme from E. coli releases free UDP as a product, while the non-hydrolyzing enzyme from Neisseria meningitidis retains UDP and produces UDP-ManNAc. The human bifunctional enzyme GNE also binds UDP-GlcNAc and catalyzes the same epimerization, but the UDP moiety remains attached to the sugar product.
Catalytic Mechanism and Domain Movement
In simple terms: The enzyme changes shape to flip the sugar, using a large moving part to do the chemistry.
The catalytic mechanism involves a large conformational change. In the Staphylococcus aureus enzyme, molecular dynamics simulations and structural analyses have shown that a domain movement of about 20-30 Å occurs during catalysis, bringing catalytic residues into position. This movement is thought to be essential for substrate binding and product release. Active site mutants of the E. coli non-hydrolyzing enzyme have identified key residues, including a conserved cysteine and a histidine, that are critical for epimerization. The reaction proceeds via a transient oxidation-reduction or a direct epimerization mechanism, but the exact chemical steps remain under investigation. The human enzyme shares similar catalytic residues and likely employs a comparable mechanism.
Cofactors and Energy Requirements
In simple terms: The enzyme does not need ATP or other energy molecules; it simply rearranges the sugar.
UDP-N-acetylglucosamine 2-epimerase activity does not require any cofactors such as ATP, NAD+, or metal ions for the epimerization reaction. The reaction is reversible and near-equilibrium, with the equilibrium favoring UDP-GlcNAc under standard conditions. However, in the bifunctional human GNE, the epimerase domain is allosterically regulated by its own product, UDP-ManNAc, and by other nucleotide sugars. In bacteria, the non-hydrolyzing enzyme from Neisseria meningitidis can also use UDP-N-acetylmannosamine and derivatives as substrates, indicating some substrate tolerance.
Regulation and Inhibition
In simple terms: The enzyme can be turned on or off by molecules that bind to it, and drugs can block it.
The activity of UDP-N-acetylglucosamine 2-epimerase is regulated at multiple levels. In humans, the bifunctional GNE enzyme is feedback-inhibited by UDP-N-acetylmannosamine, the product of the epimerase reaction, and by CMP-sialic acid, the end product of the pathway. Glycation, a non-enzymatic modification by sugars, can interfere with GNE activity, linking hyperglycemia to reduced sialic acid production. Small molecules targeting the human enzyme have been identified, such as those described by Gorenflos López et al., which can inhibit the epimerase domain and serve as chemical probes. In bacteria, the enzyme is not known to be feedback-regulated, but its expression is controlled by the availability of UDP-GlcNAc and the demand for cell envelope components.
Key Genes Involved in GO:0008761 UDP-N-acetylglucosamine 2-epimerase activity
The following genes and proteins are directly associated with UDP-N-acetylglucosamine 2-epimerase activity or its regulation.
| Gene | Major Role | Research Relevance |
|---|---|---|
| GNE (human) | Bifunctional enzyme with UDP-GlcNAc 2-epimerase and ManNAc kinase activities | Mutations cause GNE myopathy; target for sialic acid disorders |
| GNE (mouse) | Ortholog of human GNE | Model for GNE myopathy and sialic acid metabolism |
| Escherichia coli neuC | Hydrolyzing UDP-GlcNAc 2-epimerase | Model for mechanistic studies of hydrolyzing enzymes |
| Escherichia coli rffE | Non-hydrolyzing UDP-GlcNAc 2-epimerase | Active site mutants reveal catalytic residues |
| Neisseria meningitidis sacB | Non-hydrolyzing UDP-GlcNAc 2-epimerase | Substrate specificity and capsule biosynthesis |
| Staphylococcus aureus capD | UDP-GlcNAc 2-epimerase involved in capsule synthesis | Domain movement and dynamics studied |
| Bacillus subtilis mnaA | UDP-GlcNAc 2-epimerase | Teichoic acid biosynthesis model |
| Streptococcus pneumoniae capD | UDP-GlcNAc 2-epimerase | Capsule biosynthesis and virulence |
| Pseudomonas aeruginosa wbpI | UDP-GlcNAc 2-epimerase | Biofilm and virulence |
| Vibrio cholerae wbfY | UDP-GlcNAc 2-epimerase | O-antigen biosynthesis |
| Salmonella enterica rffE | UDP-GlcNAc 2-epimerase | Lipopolysaccharide biosynthesis |
| Klebsiella pneumoniae orf9 | UDP-GlcNAc 2-epimerase | Capsule synthesis and antibiotic resistance |
| Campylobacter jejuni pglD | UDP-GlcNAc 2-epimerase | Protein glycosylation pathway |
| Helicobacter pylori capD | UDP-GlcNAc 2-epimerase | Lewis antigen biosynthesis |
| Clostridium difficile CD2767 | UDP-GlcNAc 2-epimerase | Cell wall biosynthesis |
| Mycobacterium tuberculosis Rv3634c | UDP-GlcNAc 2-epimerase | Cell wall arabinogalactan synthesis |
| Corynebacterium glutamicum mnaA | UDP-GlcNAc 2-epimerase | Amino sugar metabolism |
| Homo sapiens GNE (isoform 2) | Bifunctional enzyme with epimerase and kinase domains | Alternative splicing and disease relevance |
How Is UDP-N-acetylglucosamine 2-epimerase activity Regulated?
The activity of UDP-N-acetylglucosamine 2-epimerase is regulated primarily through feedback inhibition by downstream metabolites. In the human bifunctional GNE enzyme, the epimerase domain is allosterically inhibited by UDP-N-acetylmannosamine and by CMP-sialic acid, the final product of the sialic acid pathway. This ensures that sialic acid production matches cellular demand. Additionally, glycation of GNE by glucose or other sugars can reduce its enzymatic activity, providing a link between hyperglycemia and impaired sialic acid synthesis. In bacteria, regulation occurs at the transcriptional level in response to cell envelope stress and nutrient availability, but direct allosteric regulation of the enzyme has not been widely reported. Small-molecule inhibitors can also modulate activity, as demonstrated by compounds targeting the human enzyme.
UDP-N-acetylglucosamine 2-epimerase activity and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| GNE | GNE myopathy (hereditary inclusion body myopathy) | Knock-in mouse with M712T mutation; patient-derived iPSC-derived muscle cells |
| GNE | Sialic acid metabolism disorders | GNE knockout cell lines; overexpression of wild-type and mutant GNE |
| Escherichia coli rffE | Bacterial cell wall synthesis | Deletion mutants; complementation with human GNE |
| Neisseria meningitidis sacB | Capsule biosynthesis and virulence | Mouse infection model; capsule staining |
| Staphylococcus aureus capD | Capsule synthesis and antibiotic resistance | Gene knockout; biofilm formation assays |
GNE Myopathy
GNE myopathy is a rare autosomal recessive disorder caused by mutations in the GNE gene, which encodes the bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase. The disease typically presents in early adulthood with progressive weakness and atrophy of distal muscles, particularly the tibialis anterior. More than 200 mutations have been identified, with the most common being the M712T missense mutation in the kinase domain. The epimerase domain mutations, such as V572L, also cause disease, highlighting the importance of GO:0008761 activity for muscle function. The exact mechanism by which reduced sialic acid production leads to muscle degeneration is not fully understood, but it is thought to involve impaired glycosylation of muscle proteins and altered cell signaling.
Bacterial Pathogenesis and Antibiotic Resistance
In bacteria, UDP-N-acetylglucosamine 2-epimerase activity is essential for the synthesis of UDP-N-acetylmannosamine, a precursor for capsular polysaccharides, teichoic acids, and other cell envelope components. Deletion of the gene encoding this enzyme in Neisseria meningitidis, Staphylococcus aureus, or Escherichia coli leads to defects in capsule formation, increased susceptibility to antibiotics, and reduced virulence in animal models. Because the enzyme is absent in humans, it is an attractive target for the development of narrow-spectrum antibiotics. Structural studies of the Staphylococcus aureus enzyme have revealed a unique domain movement that could be exploited for inhibitor design.
Sialic Acid Metabolism and Cancer
Altered sialic acid metabolism is a hallmark of many cancers, and the human GNE enzyme is often overexpressed in tumor cells. Increased sialylation of cell surface glycoproteins and glycolipids promotes cell migration, invasion, and immune evasion. Small-molecule inhibitors of the epimerase domain, such as those described by Gorenflos López et al., are being explored as potential anticancer agents. However, the exact role of GO:0008761 in cancer progression requires further study, as most evidence comes from cell culture and animal models.
From UDP-N-acetylglucosamine 2-epimerase activity-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| What is the effect of GNE epimerase domain mutations on sialic acid production? | Point mutation knock-in in HEK293 or HeLa cells |
| Does loss of GNE epimerase activity cause muscle pathology? | GNE knockout mouse or muscle-specific knockout |
| Can small molecules inhibit human GNE epimerase in cells? | Overexpression of GNE in cancer cell lines followed by inhibitor treatment |
| What is the role of bacterial UDP-GlcNAc 2-epimerase in capsule formation? | Knockout of the gene in Neisseria meningitidis or Staphylococcus aureus |
| How does domain movement affect catalysis? | Site-directed mutagenesis of hinge residues in Staphylococcus aureus enzyme |
| Is the hydrolyzing enzyme from E. coli functionally distinct from non-hydrolyzing enzymes? | Knock-in of E. coli neuC into a non-hydrolyzing background |
How to Study the UDP-N-acetylglucosamine 2-epimerase activity Process
| Method | What It Measures | Typical Application |
|---|---|---|
| HPLC-based enzyme assay | Conversion of UDP-GlcNAc to UDP-ManNAc | Kinetic characterization of wild-type and mutant enzymes |
| Coupled dehydrogenase assay | NADH production from UDP-ManNAc | High-throughput screening of inhibitors |
| X-ray crystallography | Three-dimensional structure of enzyme-substrate complex | Active site mapping and drug design |
| Molecular dynamics simulation | Domain movement and conformational changes | Understanding catalytic mechanism |
| CRISPR knockout | Loss of gene function | Studying cellular phenotypes and sialylation |
| Metabolomics (LC-MS) | Intracellular levels of UDP-GlcNAc and UDP-ManNAc | Assessing pathway flux in disease models |
| Glycomics (lectin blot) | Sialic acid content on glycoproteins | Evaluating downstream effects of GNE mutations |
| Site-directed mutagenesis | Specific amino acid substitutions | Identifying catalytic residues |
Enzymatic Assays for Epimerase Activity
The activity of UDP-N-acetylglucosamine 2-epimerase can be measured using a coupled enzymatic assay. Typically, the reaction is incubated with UDP-GlcNAc, and the product UDP-ManNAc is quantified by high-performance liquid chromatography (HPLC) or capillary electrophoresis. Alternatively, a coupled assay with UDP-ManNAc dehydrogenase or a kinase can be used to monitor NADH production. For the human bifunctional enzyme, the epimerase activity can be separated from the kinase activity by using specific substrates and inhibitors. These assays are essential for characterizing mutant enzymes and testing small-molecule inhibitors.
Structural Biology and Molecular Dynamics
X-ray crystallography and cryo-electron microscopy have been used to determine the structures of bacterial UDP-GlcNAc 2-epimerases, revealing a two-domain architecture with a central cleft for substrate binding. Molecular dynamics simulations have been particularly useful for studying the large domain movement in the Staphylococcus aureus enzyme, which occurs on the microsecond timescale. These methods provide atomic-level insights into substrate binding, catalysis, and the effects of disease-causing mutations. For the human enzyme, homology models based on bacterial structures have been generated to guide mutagenesis studies.
Genetic and CRISPR Screens
CRISPR-Cas9 knockout screens have been used to identify genes required for sialic acid biosynthesis, including GNE. In cancer cell lines, knockout of GNE reduces sialylation and affects cell proliferation and migration. In bacteria, transposon sequencing (Tn-seq) and CRISPR interference (CRISPRi) have been employed to study the essentiality of UDP-GlcNAc 2-epimerase genes under different growth conditions. These screens can reveal synthetic lethal interactions and potential drug targets.
Metabolomics and Glycomics
Mass spectrometry-based metabolomics allows direct quantification of UDP-GlcNAc and UDP-ManNAc in cell extracts, providing a readout of epimerase activity in vivo. Glycomics, using lectins or mass spectrometry, can assess the downstream effects on sialylation of proteins and lipids. These methods are particularly useful for studying GNE myopathy models and for evaluating the efficacy of small-molecule inhibitors.
How CRISPR Can Be Used to Study GO:0008761 UDP-N-acetylglucosamine 2-epimerase activity
Knockout
CRISPR-Cas9 knockout of GNE in human cell lines abolishes UDP-N-acetylglucosamine 2-epimerase activity, leading to reduced sialic acid levels and altered cell surface glycosylation. Knockout models are used to study the consequences of GNE loss in muscle cells and to test for rescue by wild-type or mutant GNE. In bacteria, knockout of the epimerase gene results in defective capsule formation and increased antibiotic sensitivity.
Point Mutation
Point mutations in GNE, such as M712T or V572L, are introduced using CRISPR-Cas9 homology-directed repair to create isogenic cell lines that mimic GNE myopathy. These models allow researchers to study the specific effects of disease-causing mutations on enzyme activity, protein stability, and downstream sialylation. Point mutations in bacterial enzymes, such as the active site cysteine or histidine, are used to probe the catalytic mechanism.
Knock-in
Knock-in of tagged GNE (e.g., FLAG or GFP) at the endogenous locus enables real-time imaging and proteomic analysis of the enzyme in its native context. Knock-in of bacterial epimerase genes into heterologous hosts, such as E. coli, is used to study their function and substrate specificity. Conditional knock-in alleles can be generated to control expression in specific tissues or developmental stages.
Overexpression
Overexpression of wild-type or mutant GNE in mammalian cells increases UDP-N-acetylglucosamine 2-epimerase activity and sialic acid production, which can promote cell migration and invasion in cancer models. Overexpression of bacterial enzymes in E. coli is used for biochemical purification and structural studies. Inducible overexpression systems allow fine-tuning of enzyme levels to study dose-dependent effects.
How EDITGENE Supports UDP-N-acetylglucosamine 2-epimerase activity Research
Researchers studying UDP-N-acetylglucosamine 2-epimerase activity-related genes often need to determine whether a candidate gene is causally involved in a specific phenotype, such as sialic acid production, muscle degeneration, or bacterial capsule formation. CRISPR-based genome editing provides a precise way to create loss-of-function, point-mutation, knock-in, and overexpression models in relevant cell types and organisms. EDITGENE offers a comprehensive suite of services to support these studies.
Contact EDITGENE today to design your custom CRISPR model for UDP-N-acetylglucosamine 2-epimerase activity research.
Frequently Asked Questions About UDP-N-acetylglucosamine 2-epimerase activity
What is UDP-N-acetylglucosamine 2-epimerase activity?
It is the enzyme activity that catalyzes the reversible conversion of UDP-N-acetyl-D-glucosamine to UDP-N-acetyl-D-mannosamine, encoded by GO:0008761.
What genes are involved in UDP-N-acetylglucosamine 2-epimerase activity?
In humans, the GNE gene encodes the bifunctional enzyme with this activity. In bacteria, genes such as neuC, rffE, sacB, and capD are involved.
What is the function of GNE in sialic acid biosynthesis?
GNE catalyzes the first two steps of sialic acid biosynthesis: the epimerization of UDP-GlcNAc to UDP-ManNAc and the phosphorylation of ManNAc to ManNAc-6-phosphate.
How is UDP-N-acetylglucosamine 2-epimerase activity measured?
It is typically measured using HPLC-based assays or coupled enzymatic assays that detect the product UDP-ManNAc.
What diseases are associated with UDP-N-acetylglucosamine 2-epimerase activity?
Mutations in the human GNE gene cause GNE myopathy, a progressive muscle disorder. In bacteria, the enzyme is important for virulence and antibiotic resistance.
What is the mechanism of UDP-N-acetylglucosamine 2-epimerase?
The enzyme catalyzes epimerization via a large domain movement that brings catalytic residues into position, as shown for the Staphylococcus aureus enzyme.
Are there inhibitors of UDP-N-acetylglucosamine 2-epimerase?
Yes, small-molecule inhibitors targeting the human enzyme have been developed as research tools and potential therapeutics.
What is the difference between hydrolyzing and non-hydrolyzing UDP-GlcNAc 2-epimerases?
Hydrolyzing enzymes release free UDP as a product, while non-hydrolyzing enzymes retain UDP and produce UDP-ManNAc. Both types catalyze the same epimerization.
How can CRISPR be used to study UDP-N-acetylglucosamine 2-epimerase activity?
CRISPR can create knockout, point mutation, knock-in, and overexpression models in human cells and bacteria to study the enzyme's role in health and disease.
What model organisms are used to study UDP-N-acetylglucosamine 2-epimerase?
Common models include Escherichia coli, Neisseria meningitidis, Staphylococcus aureus, and mouse models of GNE myopathy.
Conclusion
UDP-N-acetylglucosamine 2-epimerase activity (GO:0008761) is a fundamental enzymatic function that bridges amino sugar metabolism and sialic acid biosynthesis in humans, and cell envelope synthesis in bacteria. Its central role in GNE myopathy and bacterial pathogenesis makes it a compelling target for therapeutic development. Continued research into its mechanism, regulation, and inhibition will likely yield new insights and treatments.
References
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- 2. Adam MP et al.. 1993. GNE Myopathy.. PMID: 20301439
- 3. Campbell RE et al.. 2000. The structure of UDP-N-acetylglucosamine 2-epimerase reveals homology to phosphoglycosyl transferases.. Biochemistry 39(49):14993-5001 PMID: 11106477
- 4. Gorenflos López JL et al.. 2023. Small Molecules Targeting Human UDP-GlcNAc 2-Epimerase.. Chembiochem 24(24):e202300555 PMID: 37769151
- 5. Murkin AS et al.. 2004. Identification and mechanism of a bacterial hydrolyzing UDP-N-acetylglucosamine 2-epimerase.. Biochemistry 43(44):14290-8 PMID: 15518580
- 6. Samuel J et al.. 2004. Active site mutants of the "non-hydrolyzing" UDP-N-acetylglucosamine 2-epimerase from Escherichia coli.. Biochim Biophys Acta 1700(1):85-91 PMID: 15210128
- 7. Zhang L et al.. 2016. Characterizing non-hydrolyzing Neisseria meningitidis serogroup A UDP-N-acetylglucosamine (UDP-GlcNAc) 2-epimerase using UDP-N-acetylmannosamine (UDP-ManNAc) and derivatives.. Carbohydr Res 419:18-28 PMID: 26598987
- 8. de Azevedo EC et al.. 2019. Energy landscape of the domain movement in Staphylococcus aureus UDP-N-acetylglucosamine 2-epimerase.. J Struct Biol 207(2):158-168 PMID: 31088716
