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C1999

CMP-Sialic Acid Synthetase from Neisseria meningitidis group B

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

Synonym(e):

CTP: N-Acylneuraminate cytidylyltransferase

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Über diesen Artikel

UNSPSC Code:
12352204
NACRES:
NA.54
EG-Nummer:
MDL number:
Specific activity:
≥10 units/mg protein
Recombinant:
expressed in E. coli BL21

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Unterstützung erhalten

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

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Dieser Artikel
S1951S2076S1826
specific activity

≥10 units/mg protein

specific activity

≥2 units/mg protein

specific activity

≥5 units/mg protein

specific activity

≥3.0 units/mg protein

form

lyophilized solid

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

recombinant

expressed in E. coli BL21

recombinant

expressed in E. coli BL21

recombinant

expressed in E. coli BL21

recombinant

expressed in E. coli BL21

shipped in

dry ice

shipped in

dry ice

shipped in

dry ice

shipped in

dry ice

mol wt

26.0 kDa

mol wt

46.4 kDa

mol wt

56.8 kDa

mol wt

33.4 kDa

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

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.[1]

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.

Lagerklasse

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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Die Dokumentenbibliothek aufrufen

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
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, 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)
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)
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

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