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C1999

Sigma-Aldrich

CMP-Sialic Acid Synthetase from Neisseria meningitidis group B

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

Synonym(s):

CTP: N-Acylneuraminate cytidylyltransferase

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About This Item

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

recombinant

expressed in E. coli BL21

Quality Level

200

form

lyophilized solid

specific activity

≥10 units/mg protein

mol wt

26.0 kDa

shipped in

dry ice

storage temp.

−20°C

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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.

Unit Definition

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.

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).

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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)
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
Purification and characterization of the recombinant CMP-sialic acid synthetase from Neisseria meningitides.
Gilbert, M., et al
Biotechnology Letters, 19, 417-420 (1997)
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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