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一般說明
Cytidine monophosphate (CMP)-Sialic Acid Synthetase from Neisseria meningitidis group B is encoded in neuA gene. The protein has a molecular weight of 24.8 kDa.
應用
The enzyme has been utilized to synthesize CMP-sialic acid and its derivatives.
生化/生理作用
Cytidine monophosphate (CMP)-sialic acid synthetase catalyses the conversion of N?acetylneuraminic acid (NeuNAc) to CMP-NeuNAc. CMP-sialic acid synthetase has globular α/β domain and is categorised under αβα three-layered sandwich fold. The dimerization domain aids the interaction between the monomers. It also has mononucleotide binding and NeuAc binding pocket. Mg2+ is essential for the catalytic functionality of CMP-sialic acid synthetase.
單位定義
One unit will catalyze the formation of 1 μmol CMP-Neu-5-Ac from Neu-5-Ac and CTP per minute at 37 °C at pH 8.0.
外觀
Supplied as a lyophilized powder containing Tris-HCl and NaCl.
分析報告
Enzymatic activity assays are performed in Tris-HCl buffer (100 mM, pH 8.5) containing Neu-5-Ac (1 mM) and CTP (1 mM) at 37 °C for 30 min and analyzed using capillary electrophoresis with a UV detector (200 nm).
儲存類別代碼
11 - Combustible Solids
水污染物質分類(WGK)
WGK 3
閃點(°F)
Not applicable
閃點(°C)
Not applicable
其他客户在看
Molecular cloning and analysis of genes for sialic acid synthesis in Neisseria meningitidis group B and purification of the meningococcal CMP-NeuNAc synthetase enzyme.
Journal of Bacteriology, 176(15), 4583-4589 (1994)
Biochemical and biophysical research communications, 359(4), 866-870 (2007-06-19)
We report an easy and direct application of 'Saturation Transfer Double Difference' (STDD) NMR spectroscopy to identify ligands that bind to a Sepharose-immobilised target protein. The model protein, cytidine 5'-monophosphate sialic acid (CMP-Sia) synthetase, was expressed as a Strep-Tag II
Structure of a sialic acid-activating synthetase, CMP-acylneuraminate synthetase in the presence and absence of CDP
The Journal of biological chemistry, 276(11), 8190-8196 (2001)
Applied microbiology and biotechnology, 76(4), 827-834 (2007-07-03)
In this study, we report the cloning, recombinant expression, and biochemical characterization of a heat-stable CMP-N-acylneuraminic acid (NeuAc) synthetase from Clostridium thermocellum ATCC 27405. A high throughput electrospray ionization mass spectrometry (ESI-MS)-based assay demonstrates that the enzyme has an absolute
Applied microbiology and biotechnology, 80(5), 757-765 (2008-08-22)
Sialic acids are abundant nine-carbon sugars expressed terminally on glycoconjugates of eukaryotic cells and are crucial for a variety of cell biological functions such as cell-cell adhesion, intracellular signaling, and in regulation of glycoproteins stability. In bacteria, N-acetylneuraminic acid (Neu5Ac)
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