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Merck

S2563

Sigma-Aldrich

Sphingolipid Ceramide N-Deacylase from Pseudomonas sp.

Sinónimos:

SCDase

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About This Item

MDL number:
UNSPSC Code:
12352211
NACRES:
NA.32

foreign activity

exoglycosidases: α- and β-galactosidase, α- and β-N-acetylgalactosaminidase, β-N-acetylglucosaminidase, α-mannosidase, α-fucosidase, and sialidase., essentially free
protease and sphingomyelinase, essentially free

Quality Level

shipped in

dry ice

storage temp.

−20°C

General description

Sphingolipid Ceramide N-Deacylase from Pseudomonas sp. is a hydrolytic enzyme.

Application

Sphingolipid Ceramide N-Deacylase from Pseudomonas sp. has been used in enzymatic conversion and derivatization of sulfatides. It has also been used to hydrolyze the fatty acid chain of mactosyl ceramide.

Biochem/physiol Actions

Sphingolipid Ceramide N-Deacylase from Pseudomonas sp., under certain conditions, can recyclate lyso-sphingolipids. It condenses fatty acids to sphingosine to generate ceramide. The enzyme mainly acts on neutral and acidic glycosphingolipids.
Hydrolyzes the N-acyl linkage between fatty acids and sphingosines in ceramides of various sphingolipids.

Unit Definition

One unit will hydrolyze 1 μmol of asialo GM1 per minute at pH 6.0 at 37 °C.

Physical form

Solution in 50 mM sodium acetate, pH 6.0, with 0.1% Lubrol PX.

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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Characterization of the reversible nature of the reaction catalyzed by sphingolipid ceramide N-deacylase. A novel form of reverse hydrolysis reaction.
Kita K
European Journal of Biochemistry, 268(3), 592-602 (2001)
Sulfatide Analysis by Mass Spectrometry for Screening of Metachromatic Leukodystrophy in Dried Blood and Urine Samples.
Spacil Z
Clinical Chemistry, 62(1), 279-286 (2016)
A novel enzyme that cleaves the N-acyl linkage of ceramides in various glycosphingolipids as well as sphingomyelin to produce their lyso forms.
Ito M
The Journal of Biological Chemistry, 270(41), 24370-24374 (1995)

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