N-Acetylhexosamine kinase (NahK) 

N-Acetylhexosamine kinase (NahK) is an anomeric kinase acting on a glucose-type substrate. N-Acetylhexosamine kinase catalyzes the phosphorylation of GlcNAc or GalNAc at the anomeric C1 position with ATP to form N-acetylhexosamine 1-phosphate (GlcNAc-1P/GalNAc-1P)^[1][2].

Product Information
This product is expressed by recombinant E. coli, N-terminal His Tagged, molecular weight 41 kDa, can be used for phosphorylation of position 1 of GalNAc or GlcNAc.

Instructions
1. Add substrate according to the reaction system, add appropriate buffer salt (such as Tris-HCl), adjust the pH to 7.5, and add appropriate amount of N-Acetylhexosamine kinase (according to the reaction requirements);
2. After mixing, incubate the sample at 37°C for 0.5-1 h.

Notes
1. When the system is scaled up, the incubation time or enzyme amount needs to be adjusted according to the actual situation, and the mixing can be done by low-speed shaking.
2. Most common biological buffers are applicable, such as Tris or PBS. Buffers outside this pH range (such as acetate buffer) may be applicable, but the incubation time or enzyme amount needs to be optimized according to the actual situation.

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

1609980-80-4

Liquid

Colorless to light yellow

[N-Acetylhexosamine kinase (NahK)]

2.7.1.162

≥1 U/mg soild

One unit is defined as the amount of enzyme that will consume 1 μmol ATP and GalNAc to generate GalNAc-1-p per minute at 37℃

Room temperature in continental US; may vary elsewhere.

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

• [1]. Sato M, et al. Open-close structural change upon ligand binding and two magnesium ions required for the catalysis of N-acetylhexosamine 1-kinase. Biochim Biophys Acta. 2015 May;1854(5):333-40.  [Content Brief]

  [2]. Wang KC, et al. Insights into the binding specificity and catalytic mechanism of N-acetylhexosamine 1-phosphate kinases through multiple reaction complexes. Acta Crystallogr D Biol Crystallogr. 2014 May;70(Pt 5):1401-10.  [Content Brief]