C1999
CMP-Sialic Acid Synthetase from Neisseria meningitidis group B
recombinant, expressed in E. coli BL21, ≥10 units/mg protein
Sinônimo(s):
CTP: N-Acylneuraminate cytidylyltransferase
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About This Item
Número MDL:
Código UNSPSC:
12352204
NACRES:
NA.54
Produtos recomendados
recombinante
expressed in E. coli BL21
Nível de qualidade
forma
lyophilized solid
atividade específica
≥10 units/mg protein
peso molecular
26.0 kDa
Condições de expedição
dry ice
temperatura de armazenamento
−20°C
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Descrição geral
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.
Aplicação
The enzyme has been utilized to synthesize CMP-sialic acid and its derivatives.
Ações bioquímicas/fisiológicas
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.
Definição da unidade
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.
forma física
Supplied as a lyophilized powder containing Tris-HCl and NaCl.
Nota de análise
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).
Código de classe de armazenamento
11 - Combustible Solids
Classe de risco de água (WGK)
WGK 3
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
Certificados de análise (COA)
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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)
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
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)
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
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)
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