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Merck
CN

C1999

CMP-Sialic Acid Synthetase from Neisseria meningitidis group B

recombinant, expressed in E. coli BL21, ≥10 units/mg protein

别名:

CTP: N-Acylneuraminate cytidylyltransferase

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关于此项目

UNSPSC Code:
12352204
NACRES:
NA.54
EC 号:
2.7.7.43 (BRENDA, IUBMB)
MDL number:
MFCD01323074

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产品名称

CMP-Sialic Acid Synthetase from Neisseria meningitidis group B, recombinant, expressed in E. coli BL21, ≥10 units/mg protein

recombinant

expressed in E. coli BL21

form

lyophilized solid

specific activity

≥10 units/mg protein

mol wt

26.0 kDa

shipped in

dry ice

storage temp.

−20°C

Quality Level

200

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Analysis Note

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).

Application

The enzyme has been utilized to synthesize CMP-sialic acid and its derivatives.

Biochem/physiol Actions

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.

General description

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.

Other Notes

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.

Physical form

Supplied as a lyophilized powder containing Tris-HCl and NaCl.

存储类别

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

法规信息

常规特殊物品
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分析证书(COA)

Lot/Batch Number
0000502928
0000502928
0000431963
0000431963
0000429781

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Structure of a sialic acid-activating synthetase, CMP-acylneuraminate synthetase in the presence and absence of CDP
Mosimann S, et al.
The Journal of biological chemistry, 276(11), 8190-8196 (2001)
Thomas Haselhorst et al.
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
Molecular cloning and analysis of genes for sialic acid synthesis in Neisseria meningitidis group B and purification of the meningococcal CMP-NeuNAc synthetase enzyme.
Ganguli S, et al.
Journal of Bacteriology, 176(15), 4583-4589 (1994)
Rahman M Mizanur et al.
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)
Rahman M Mizanur et al.
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
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