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S1951

Sigma-Aldrich

α-2,3-Sialyltransferase from Pasteurella multocida

recombinant, expressed in E. coli BL21, ≥2 units/mg protein

Synonyma:

CMP-N-acetylneuraminate:β-D-galactoside α-(2,3)-N-acetylneuraminyltransferase

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About This Item

Číslo enzymu podle klasifikace EK:
2.4.99.4 (BRENDA, IUBMB)
MDL number:
MFCD00130470
UNSPSC Code:
12352204
NACRES:
NA.54

recombinant

expressed in E. coli BL21

Quality Level

200

form

lyophilized powder

specific activity

≥2 units/mg protein

mol wt

46.4 kDa

shipped in

dry ice

storage temp.

−20°C

General description

Sialyltransferases belongs to the glycosyltransferases family with the capability of catalyzing the transfer of N-acetylneuraminic acid residues. It is a multifunctional enzyme with α-2,3-sialyltransferase activity, α-2,6-sialyltransferase activity, sialidase activity, and trans-sialidase activity. It has a molar mass of 46.4 kDa, with pI, pH being 5.94 and 7.5-8.5 respectively.

Biochem/physiol Actions

Sialyltransferase catalyzes the transfer of Neu5Ac from CMP-Neu5Ac as a donor substrate to the β-D-galactosyl-1,4-N-acetyl-D-glucosaminyl termini of acceptor molecules including glycoproteins, glycolipids, and oligosaccharides.
Sialyltransferase transfers Neu5Ac from CMP-Neu5Ac to the galactosyl terminus of acceptor molecules including glycoproteins, glycolipids, and oligosaccharides.

Unit Definition

One unit will catalyze the formation of 1.0 μmol Neu-5-Ac-α-2,3LacMU from CMP-Neu-5-Ac and Lac-β−OMU per minute at 37 °C at pH 8.0.

Physical form

Lyophilized powder containing Tris-HCl and NaCl

Preparation Note

Reconstitute the lyophilized powder with a volume of water in the range of 0.1 mL to 1 mL, to give a concentration in the range of 1 unit/mL (1 mL volume of water) to 10 units/mL (0.1 mL volume of water).

Analysis Note

Enzymatic activity assays performed in Tris-HCl buffer (100 mM, pH 8.0) containing CMP-Neu-5Ac (1 mM) and Lac-β−OMU (1 mM) at 37°C for 30 min and analyzed using HPLC with a fluorescence detector (excitation at 325 nm and emission at 372 nm).

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

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Navštívit knihovnu dokumentů

Sung-Wook Son et al.
Biochemical and biophysical research communications, 414(1), 159-164 (2011-09-29)
In this study we investigated for the first time the transcriptional regulation of pig Galβ1,3GalNAc α2,3-sialyltransferase (pST3Gal I) in response to TGF-β1 in porcine kidney PK-15 cells. The pST3Gal I gene was found to span about 90kb and to be
Vireak Thon et al.
Applied microbiology and biotechnology, 94(4), 977-985 (2011-11-15)
Pasteurella multocida (Pm) strain Pm70 has three putative sialyltransferase genes including Pm0188, Pm0508, and Pm1174. A Pm0188 gene homolog in Pm strain P-1059 encodes a multifunctional α2-3-sialyltransferase, PmST1, that prefers oligosaccharide acceptors. A Pm0508 gene homolog in the same strain
Yoshimitsu Kakuta et al.
Glycobiology, 18(1), 66-73 (2007-10-27)
Sialyltransferases are a family of glycosyltransferases that catalyze the transfer of N-acetylneuraminic acid residues from cytidine monophosphate N-acetylneuraminic acid (CMP-NeuAc) as a donor substrate to the carbohydrate groups of glycoproteins and glycolipids as acceptor substrates. We determined the crystal structure
Peng Zhang et al.
Bipolar disorders, 12(8), 786-792 (2010-12-24)
Multiple linkage and association studies have suggested chromosome 8q24 as a promising candidate region for bipolar disorder (BP). We performed a detailed association analysis assessing the contribution of common genetic variation in this region to the risk of BP. We
Lisheng Ni et al.
Biochemistry, 45(7), 2139-2148 (2006-02-16)
Sialyltransferases catalyze reactions that transfer a sialic acid from CMP-sialic acid to an acceptor (a structure terminated with galactose, N-acetylgalactosamine, or sialic acid). They are key enzymes that catalyze the synthesis of sialic acid-containing oligosaccharides, polysaccharides, and glycoconjugates that play
Zobrazit všechny související dokumenty

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