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
Specific activity:
≥10 units/mg protein
Recombinant:
expressed in E. coli BL21
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.
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.
Physical form
Supplied as a lyophilized powder containing Tris-HCl and NaCl.
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).
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.
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
此项目有
Purification and characterization of the recombinant CMP-sialic acid synthetase from Neisseria meningitides.
Gilbert, M., et al
Biotechnology Letters, 19, 417-420 (1997)
Jessica H Wong et al.
Organic & biomolecular chemistry, 7(1), 27-29 (2008-12-17)
A modular replacement approach to the synthesis of sulfo-nucleotide analogs prepared from condensation of nucleoside aldehydes with bis phosphonate Horner-Wadsworth-Emmons reagents is disclosed. These analogs were shown to be inhibitors of Neisseria meningitidis CSS (NmCSS), which is a key enzyme
Hai Yu et al.
Bioorganic & medicinal chemistry, 12(24), 6427-6435 (2004-11-24)
Three C terminal His6-tagged recombinant microbial CMP-sialic acid synthetases [EC 2.7.7.43] cloned from Neisseria meningitidis group B, Streptococcus agalactiae serotype V, and Escherichia coli K1, respectively, were evaluated for their ability in the synthesis of CMP-sialic acid derivatives in a
CMP-sialic acid synthetase: the point of constriction in the sialylation pathway
SialoGlyco Chemistry and Biology I, 139-167 (2013)
Sandra Ratzow et al.
Journal of clinical microbiology, 45(6), 1965-1968 (2007-04-06)
The standard sequence-based method for the typing of Legionella pneumophila serogroup 1 strains was extended by using the gspA and neuA alleles. The use of neuA as a seventh allele for typing significantly increased the index of discrimination calculated for
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