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AdipoGen Life Sciences
NAD Kinase (M. tuberculosis) (rec.) (His)
490
CHF
CHF 490.00
In stock
AG-40T-0107-C05050 µgCHF 490.00
Product Details | |
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Synonyms | Probable Inorganic Polyphosphate/ATP-NAD kinase; Poly(P)/ATP NAD Kinase 1; ppnK1; EC 2.7.1.23 |
Product Type | Protein |
Properties | |
Source/Host | E. coli |
Sequence | NAD kinase (Mycobacterium tuberculosis) is fused at the N-terminus to a His-tag. |
Biological Activity |
~1.2 U/mg protein. (Substrate: NAD (+ ATP)) ~3.8 U/mg protein. (Substrate: NAD (+ poly(P)) One unit is defined as the amount of enzyme that synthesizes 1µmol nicotinamide adenine dinucleotide phosphate (NADP) per min. |
MW | ~33.0kDa |
Purity | ≥98% (SDS-PAGE) |
Endotoxin Content | N/A |
Concentration | 0.5mg/ml (Lot specific) |
Formulation | Liquid. In 10mM TRIS at pH 8.0, containing 1mM MgCl2, 0.5mM EDTA, 1mM DTT and 1mM PMSF. |
Other Product Data | UniProt link P0A5S6: NAD Kinase (M. tuberculosis) |
Shipping and Handling | |
Shipping | DRY ICE |
Short Term Storage | -20°C |
Long Term Storage | -80°C |
Handling Advice |
After opening, prepare aliquots and store at -80°C. Avoid freeze/thaw cycles. |
Use/Stability | Stable for at least 6 months after receipt when stored at -80°C. |
Documents | |
MSDS | Download PDF |
Product Specification Sheet | |
Datasheet | Download PDF |
Description
NAD kinase catalyzes the transfer of a phosphate group from ATP to NAD+ to generate NADP+, which in its reduced form acts as an electron donor for biosynthetic reactions. NADP+ is an essential coenzyme in metabolism and provides reducing power to biosynthetic processes such as fatty acid biosynthesis. NAD kinase from Mycobacterium tuberculosis is not ATP-dependent but has a broader substrate specificity than human NAD kinase. It can economically produce NADP+ by using other nucleoside triphosphates as well as inorganic polyphosphate as a source of phosphorus. Was identified as a high-confidence drug target.
Catalytic activity: ATP + NAD+ = ADP + NADP+
Catalytic activity: ATP + NAD+ = ADP + NADP+
Product References
- Characterization of Mycobacterium tuberculosis NAD Kinase: Functional Analysis of the Full-Length Enzyme by Site-Directed Mutagenesis: N. Raffaelli, et al.; Biochemistry 43, 7610 (2004)
- A Novel Fold Revealed by Mycobacterium tuberculosis NAD Kinase, a Key Allosteric Enzyme in NADP Biosynthesis: S. Garavaglia, et al.; J. Biol. Chem. 279, 40980 (2004)