N-Acetylglucosamine-1-P uridyltransferase, Homo sapien  (Synonyms: GlcNAc1pUT)

N-acetylglucosamine-1-P uridyltransferase (AGX1) (EC 2.3.1.157) (GlcNAc1pUT) is a bifunctional acetyltransferase/uridyltransferase. N-acetylglucosamine-1-P uridyltransferase (AGX1) binds GlcNAc-1-P and UTP, and catalyzes an uridyltransfer reaction to synthesize UDP-GlcNAc. N-acetylglucosamine-1-P uridyltransferase (AGX1) is a bifunctional enzyme exclusive to prokaryotes^[1].

Product Information
This product is recombinantly expressed in E. coli, with N-terminal His Tag, molecular weight of 57 kDa, and storage buffer composed of 20 mM Tris-HCl, 200mM NaCl pH 8.0, 5% glycerol. It can be used to catalyze GlcNAc/GalNAc to form UDP-GlcNAc/UDP-GalNAc, as a donor for glycosyltransferase to transfer sugar groups, and can also be used as a tool enzyme for the synthesis of UDP-GlcNAc and UDP-GalNAc.

Instructions
1. Add substrate according to the reaction system, 5 mM MgCl₂, and appropriate buffer salts such as Tris-HCl can be added to adjust the pH to 7.5-8.5, and add appropriate amount of Enzyme (according to the reaction requirements);
2. After mixing, incubate the sample at 37℃ for 30-60 min. It is most active in a buffer with a pH close to neutral pH. The recommended reaction buffer is Tris-HCL (pH 8.0), and most common biological buffers are also suitable, such as Tris or PBS.

Notes
When the system is scaled up, the incubation time or enzyme amount needs to be adjusted according to the actual situation. It can be mixed by low-speed shaking. Adding Inorganic pyrophosphatase, Saccharomyces cerevisiae (HY-P2992) can increase the conversion rate.

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

Liquid

Colorless to light yellow

[N-Acetylglucosamine-1-P uridyltransferase, Homo sapien]

Room temperature in continental US; may vary elsewhere.

Please store the product under the recommended conditions in the Certificate of Analysis.

• [1]. Vithani N, et, al. GlmU (N-acetylglucosamine-1-phosphate uridyltransferase) bound to three magnesium ions and ATP at the active site. Acta Crystallogr F Struct Biol Commun. 2014 Jun;70(Pt 6):703-8.  [Content Brief]