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UDP-acetylglucosamine deacetylase 11A, Pseudomonas aeruginosa
UDP-acetylglucosamine deacetylase 11A (PaLpx11A), assigned the E.C. number 3.5.1.108, is a derivative of Pseudomonas aeruginosa. It is a metal-dependent deacetylase that removes the acetyl group from the 2-amino group of UDP-(3-O-(R-3-hydroxymyristoyl))-N-acetylglucosamine (myr-UDP-GlcNAc)3 . The recombinant PaLpx11A, purified from Escherichia coli, is a single-domain Carbohydrate Esterase family 11 (CE11) enzyme (see more details at www.cazy.org).
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UDP-acetylglucosamine deacetylase 11A (PaLpx11A), assigned the E.C. number 3.5.1.108, is a derivative of Pseudomonas aeruginosa. It is a metal-dependent deacetylase that removes the acetyl group from the 2-amino group of UDP-(3-O-(R-3-hydroxymyristoyl))-N-acetylglucosamine (myr-UDP-GlcNAc)3 . The recombinant PaLpx11A, purified from Escherichia coli, is a single-domain Carbohydrate Esterase family 11 (CE11) enzyme (see more details at www.cazy.org).The protein is supplied in a solution containing 35 mM NaHepes buffer (pH 7.5), 750 mM NaCl, 200 mM Imidazole, 3.5 mM CaCl2, and 25% (v/v) glycerol, at a concentration of 1 mg/mL. Bulk quantities of this product can be made available upon request. To place an order, simply visit our website. We offer fast and secure shipping worldwide.
| Shipping Conditions | Shipping: Dry Ice to RT |
|---|---|
| Storage Conditions | -30°C to -15°C |
| Class | Carbohydrate Esterase |
| Activity | Acetylglucosamine deacetylases |
| Family | CE11 |
| EC number | 3.5.1.108 |
| Organism | Pseudomonas aeruginosa |
| Architecture | CE11 |
| Optimal pH | 8.5 |
| Optimal Temperature | 30°C |
| Substrates | UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine |
Hyland et al. (1997) J Bacteriol. 179(6): 2029–2037.
Mdluli et al. (2006) Antimicrob Agents Chemother. 50(6):2178-84.
Mochalkin et al. (2008) Protein Sci. 17(3): 450–457.
Liang et al. (2013) J Med Chem. 56(17):6954-6966.
Piizzi et al. (2017) J Med Chem. 60(12):5002-5014.
Cohen et al. (2019) ChemMedChem. 14(16):1560-1572.
Surivet et al. (2020) J Med Chem. 63(1):66-87.
Mdluli et al. (2006) Antimicrob Agents Chemother. 50(6):2178-84.
Mochalkin et al. (2008) Protein Sci. 17(3): 450–457.
Liang et al. (2013) J Med Chem. 56(17):6954-6966.
Piizzi et al. (2017) J Med Chem. 60(12):5002-5014.
Cohen et al. (2019) ChemMedChem. 14(16):1560-1572.
Surivet et al. (2020) J Med Chem. 63(1):66-87.
| Shipping Conditions | Shipping: Dry Ice to RT |
|---|---|
| Storage Conditions | -30°C to -15°C |
| Class | Carbohydrate Esterase |
| Activity | Acetylglucosamine deacetylases |
| Family | CE11 |
| EC number | 3.5.1.108 |
| Organism | Pseudomonas aeruginosa |
| Architecture | CE11 |
| Optimal pH | 8.5 |
| Optimal Temperature | 30°C |
| Substrates | UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine |
| Shipping Conditions | Shipping: Dry Ice to RT |
|---|---|
| Storage Conditions | -30°C to -15°C |
| Class | Carbohydrate Esterase |
| Activity | Acetylglucosamine deacetylases |
| Family | CE11 |
| EC number | 3.5.1.108 |
| Organism | Pseudomonas aeruginosa |
| Architecture | CE11 |
| Optimal pH | 8.5 |
| Optimal Temperature | 30°C |
| Substrates | UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine |
CoA
Certificate of Analysis
