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16-(acetylsulfanyl)hexadecanoic acid + lyso-GM1a
? + H2O
16-[(prop-2-yn-1-yl)oxy]hexadecanoic acid + lyso-GM1a
? + H2O
2-hydroxydodecanoic acid + lyso-GM1a
? + H2O
2-hydroxyhexadecanoic acid + lyso-GM1a
? + H2O
arachidic acid + lyso-GM1a
? + H2O
asialoganglioside GM1 + H2O
fatty acid + ?
behenic acid + lyso-GM1a
? + H2O
caproic acid + lyso-GM1a
? + H2O
caprylic acid + lyso-GM1a
? + H2O
D-galactosylceramide-3-O-sulfate + H2O
?
-
-
-
-
?
decanoic acid + lyso-GM1a
? + H2O
docosahexaenoic acid + lyso-GM1a
? + H2O
eicosapentaenoic acid + lyso-GM1a
? + H2O
galacosylceramide + H2O
?
-
-
-
-
?
galactosylceramide + H2O
?
-
-
-
?
ganglioside asialo-GM1 + H2O
?
ganglioside asialo-GM2 + H2O
?
-
-
-
-
?
ganglioside Gb3-ceramide + H2O
?
-
-
-
-
?
ganglioside GD1a + H2O
fatty acid + lyso-GD1a-ganglioside
ganglioside GD1b + H2O
fatty acid + ?
ganglioside GM1 + H2O
octadecanoic acid + lyso-GM1-ganglioside
ganglioside GM1a + H2O
fatty acid + ?
ganglioside GM2 + H2O
fatty acid + lyso-GM2-ganglioside
ganglioside GM3 + H2O
fatty acid + ?
ganglioside GM3 + H2O
fatty acid + lyso-GM3-ganglioside
ganglioside GQ1b + H2O
?
-
-
-
-
?
ganglioside GT1b + H2O
fatty acid + ?
gangliotetraosylceramide + H2O
glucosylceramide
-
immobilised enzyme, pH 5, 37°C. The rate of hydrolysis of the substrate by the immobilised enzyme is 62% after 20 h as compared to 48% with the soluble enzyme under the same reaction conditions
using the soluble form of the SCDase C17:0 glucosylceramide is prepared in bulk solution. Mass spectra reveal a considerable amount of contaminants in the final product. The contaminants are identified as glucosylceramide isoforms with C16:0 and C18:0 fatty acids. The total yield of glucosylceramide is 99%. Products are analyzed by HPTLC
-
?
globotetraosylceramide + H2O
?
-
-
-
-
?
glycosphingolipid + H2O
?
-
-
-
-
?
GM1a + H2O
stearic acid + lyso-GM1a
GM3 + H2O
stearic acid + lyso-GM3
hexadecanedioic acid + lyso-GM1a
? + H2O
hexadecanedioic acid methyl ester + lyso-GM1a
? + H2O
lactosylceramide + H2O
?
-
-
-
-
?
lauric acid + lyso-GM1a
? + H2O
lignoceric acid + lyso-GM1a
? + H2O
myristic acid + lyso-GM1a
? + H2O
oleic acid + lyso-GM1a
? + H2O
omega-azido palmitic acid + lyso-GM1a
? + H2O
omega-bromo-palmitic acid + lyso-GM1a
? + H2O
omega-hydroxypalmitic acid + lyso-GM1a
? + H2O
palmitic acid + lyso-GM1a
? + H2O
additional information
?
-
16-(acetylsulfanyl)hexadecanoic acid + lyso-GM1a
? + H2O
-
-
-
-
r
16-(acetylsulfanyl)hexadecanoic acid + lyso-GM1a
? + H2O
-
-
-
r
16-(acetylsulfanyl)hexadecanoic acid + lyso-GM1a
? + H2O
-
-
-
r
16-[(prop-2-yn-1-yl)oxy]hexadecanoic acid + lyso-GM1a
? + H2O
-
-
-
-
r
16-[(prop-2-yn-1-yl)oxy]hexadecanoic acid + lyso-GM1a
? + H2O
-
-
-
r
16-[(prop-2-yn-1-yl)oxy]hexadecanoic acid + lyso-GM1a
? + H2O
-
-
-
r
2-hydroxydodecanoic acid + lyso-GM1a
? + H2O
-
-
-
-
r
2-hydroxydodecanoic acid + lyso-GM1a
? + H2O
-
-
-
r
2-hydroxydodecanoic acid + lyso-GM1a
? + H2O
-
-
-
r
2-hydroxyhexadecanoic acid + lyso-GM1a
? + H2O
-
-
-
-
r
2-hydroxyhexadecanoic acid + lyso-GM1a
? + H2O
-
-
-
r
2-hydroxyhexadecanoic acid + lyso-GM1a
? + H2O
-
-
-
r
arachidic acid + lyso-GM1a
? + H2O
-
-
-
-
r
arachidic acid + lyso-GM1a
? + H2O
-
-
-
r
asialoganglioside GM1 + H2O
fatty acid + ?
-
-
?
asialoganglioside GM1 + H2O
fatty acid + ?
-
-
?
behenic acid + lyso-GM1a
? + H2O
-
-
-
-
r
behenic acid + lyso-GM1a
? + H2O
-
-
-
r
caproic acid + lyso-GM1a
? + H2O
-
-
-
-
r
caproic acid + lyso-GM1a
? + H2O
-
-
-
r
caprylic acid + lyso-GM1a
? + H2O
-
-
-
-
r
caprylic acid + lyso-GM1a
? + H2O
-
-
-
r
decanoic acid + lyso-GM1a
? + H2O
-
-
-
-
r
decanoic acid + lyso-GM1a
? + H2O
-
-
-
r
docosahexaenoic acid + lyso-GM1a
? + H2O
-
-
-
-
r
docosahexaenoic acid + lyso-GM1a
? + H2O
-
-
-
r
eicosapentaenoic acid + lyso-GM1a
? + H2O
-
-
-
-
r
eicosapentaenoic acid + lyso-GM1a
? + H2O
-
-
-
r
ganglioside asialo-GM1 + H2O
?
-
-
-
-
?
ganglioside asialo-GM1 + H2O
?
-
-
-
-
?
ganglioside GD1a + H2O
fatty acid + lyso-GD1a-ganglioside
-
-
-
-
?
ganglioside GD1a + H2O
fatty acid + lyso-GD1a-ganglioside
-
-
-
-
?
ganglioside GD1b + H2O
fatty acid + ?
-
-
?
ganglioside GD1b + H2O
fatty acid + ?
-
-
?
ganglioside GM1 + H2O
?
-
-
-
?
ganglioside GM1 + H2O
?
-
-
-
?
ganglioside GM1 + H2O
octadecanoic acid + lyso-GM1-ganglioside
-
-
-
-
?
ganglioside GM1 + H2O
octadecanoic acid + lyso-GM1-ganglioside
-
-
-
-
?
ganglioside GM1a + H2O
fatty acid + ?
-
-
?
ganglioside GM1a + H2O
fatty acid + ?
-
-
?
ganglioside GM2 + H2O
fatty acid + lyso-GM2-ganglioside
-
-
-
?
ganglioside GM2 + H2O
fatty acid + lyso-GM2-ganglioside
-
-
-
-
?
ganglioside GM3 + H2O
?
-
-
-
?
ganglioside GM3 + H2O
?
-
-
-
?
ganglioside GM3 + H2O
fatty acid + ?
-
-
?
ganglioside GM3 + H2O
fatty acid + ?
-
-
?
ganglioside GM3 + H2O
fatty acid + lyso-GM3-ganglioside
-
-
-
-
?
ganglioside GM3 + H2O
fatty acid + lyso-GM3-ganglioside
-
-
-
-
?
ganglioside GT1b + H2O
fatty acid + ?
-
-
?
ganglioside GT1b + H2O
fatty acid + ?
-
-
?
glucosylceramide + H2O
?
-
-
-
-
?
glucosylceramide + H2O
?
-
-
-
?
glucosylceramide + H2O
?
-
-
-
?
GM1a + H2O
stearic acid + lyso-GM1a
-
-
-
-
r
GM1a + H2O
stearic acid + lyso-GM1a
-
-
-
r
GM3 + H2O
stearic acid + lyso-GM3
-
-
-
-
r
GM3 + H2O
stearic acid + lyso-GM3
-
-
-
r
hexadecanedioic acid + lyso-GM1a
? + H2O
-
-
-
-
r
hexadecanedioic acid + lyso-GM1a
? + H2O
-
-
-
r
hexadecanedioic acid methyl ester + lyso-GM1a
? + H2O
-
-
-
-
r
hexadecanedioic acid methyl ester + lyso-GM1a
? + H2O
-
-
-
r
lauric acid + lyso-GM1a
? + H2O
-
-
-
-
r
lauric acid + lyso-GM1a
? + H2O
-
-
-
r
lignoceric acid + lyso-GM1a
? + H2O
-
-
-
-
r
lignoceric acid + lyso-GM1a
? + H2O
-
-
-
r
myristic acid + lyso-GM1a
? + H2O
-
-
-
-
r
myristic acid + lyso-GM1a
? + H2O
-
-
-
r
oleic acid + lyso-GM1a
? + H2O
-
-
-
-
r
oleic acid + lyso-GM1a
? + H2O
-
-
-
r
omega-azido palmitic acid + lyso-GM1a
? + H2O
-
-
-
-
r
omega-azido palmitic acid + lyso-GM1a
? + H2O
-
-
-
r
omega-bromo-palmitic acid + lyso-GM1a
? + H2O
-
-
-
-
r
omega-bromo-palmitic acid + lyso-GM1a
? + H2O
-
-
-
r
omega-hydroxypalmitic acid + lyso-GM1a
? + H2O
-
-
-
-
r
omega-hydroxypalmitic acid + lyso-GM1a
? + H2O
-
-
-
r
palmitic acid + lyso-GM1a
? + H2O
-
-
-
-
r
palmitic acid + lyso-GM1a
? + H2O
-
-
-
r
sphingomyelin + H2O
?
-
-
-
-
?
sphingomyelin + H2O
?
-
-
-
?
sphingomyelin + H2O
?
-
-
-
?
additional information
?
-
-
does not act on sphingolipids such as ceramide, Galbeta(1-1')ceramide, Glcbeta(1-1')ceramide, Galbeta(1-4)Glcbeta(1-1')ceramide
-
-
?
additional information
?
-
-
the enzyme catalyzes reversible reactions in which the amide linkage in glycosphingolipids is hydrolyzed or synthesized. PS_SCD also prefers glycosphingolipids possessing larger sugar moieties, but it does not show preference towards glycosphingolipids with charged head groups, the enzyme hydrolyzes sulfatide faster than GM1a and GM3, specificity of the hydrolytic and synthetic reactions of PS_SCD for hydrophilic head groups, overview
-
-
?
additional information
?
-
-
purified neutral glycosphingolipids and gangliosides from bovine brain tissue are treated with SCDase and derivatized by fluorocarbon-rich substituent tags. The products are recovered by FluorosTM solid phase extraction
the products are recovered by FluorosTM solid ohase extraction and analyzed by MALDI-QIT-TOF mass spectrometry and ESI-LIT mass spectrometry
-
?
additional information
?
-
the enzyme catalyzes reversible reactions in which the amide linkage in glycosphingolipids is hydrolyzed or synthesized. The enzyme shows high catalytic efficiency and has a very broad substrate specificity both in hydrolysis and synthesis, especially for unsaturated fatty acids and fatty acids with very short or long acyl chains. The enzyme SA_SCD hydrolyzes GM1a and GM3 fast, specificity of the hydrolytic and synthetic reactions of SA_SCD for hydrophilic head groups, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes reversible reactions in which the amide linkage in glycosphingolipids is hydrolyzed or synthesized. The enzyme shows high catalytic efficiency and has a very broad substrate specificity both in hydrolysis and synthesis, especially for unsaturated fatty acids and fatty acids with very short or long acyl chains. The enzyme SA_SCD hydrolyzes GM1a and GM3 fast, specificity of the hydrolytic and synthetic reactions of SA_SCD for hydrophilic head groups, overview
-
-
?
additional information
?
-
assay method optimization and evaluation, overview
-
-
?
additional information
?
-
the enzyme catalyzes reversible reactions in which the amide linkage in glycosphingolipids is hydrolyzed or synthesized. The enzyme shows high catalytic efficiency and has a very broad substrate specificity both in hydrolysis and synthesis, especially for unsaturated fatty acids and fatty acids with very short or long acyl chains. The enzyme SA_SCD hydrolyzes GM1a and GM3 fast, specificity of the hydrolytic and synthetic reactions of SA_SCD for hydrophilic head groups, overview
-
-
?
additional information
?
-
assay method optimization and evaluation, overview
-
-
?
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Ba2+
-
10 mM, slight activation
Fe2+
promotes the hydrolytic activity but inhibits the synthetic activity of the enzyme
Ni2+
promotes the hydrolytic activity but inhibits the synthetic activity of the enzyme
Ca2+
activation
Ca2+
promotes the hydrolytic activity but inhibits the synthetic activity of the enzyme
Ca2+
required, activtes. GM1 hydrolysis increases with increasing Ca 2+ concentration, compared with 40.7% yield in the absence of Ca2+, the addition of 100 mM Ca2+ enhances the yield to 81.6%. Best at 50-100 mM
Co2+
promotes the hydrolytic activity but inhibits the synthetic activity of the enzyme
Co2+
activates, but slightly less effectve compared to Ca2+, at 100 mM
Mg2+
-
10 mM, slight activation
Mg2+
promotes the hydrolytic activity but inhibits the synthetic activity of the enzyme
Mg2+
activates, but less effectve compared to Ca2+, at 100 mM
Mn2+
activation
Mn2+
promotes the hydrolytic activity but inhibits the synthetic activity of the enzyme
Mn2+
activates similar to Ca2+, at 100 mM
additional information
poor effect by EDTA
additional information
-
poor effect by EDTA
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Ca2+
promotes the hydrolytic activity but inhibits the synthetic activity of the enzyme
Co2+
promotes the hydrolytic activity but inhibits the synthetic activity of the enzyme
deoxycholic acid
complete inhibition of the hydrolytic and synthetic activity
dimethoxyethane
addition of 5% of DME strongly promoted the activity, further increasing the DME concentrations progressively inhibited synthetic activity
DMSO
low concentrations of DMSO, up to a maximum at 10%, enhance synthetic activity, while higher concentrations inhibit
Fe2+
promotes the hydrolytic activity but inhibits the synthetic activity of the enzyme
Mg2+
promotes the hydrolytic activity but inhibits the synthetic activity of the enzyme
Ni2+
promotes the hydrolytic activity but inhibits the synthetic activity of the enzyme
taurodeoxycholate
complete inhibition of the hydrolytic and synthetic activity
Triton X-100
activates the hydrolytic reaction, best at 0.5% w/v, but inhibits the synthetic reaction
Cu2+
-
10 mM, strong
Cu2+
inhibits the hydrolytic activity and the synthetic activity of the enzyme
EDTA
-
10 mM, 30% inhibition
Hg2+
-
10 mM, strong
Mn2+
-
10 mM, strong
Mn2+
promotes the hydrolytic activity but inhibits the synthetic activity of the enzyme
Zn2+
-
10 mM, strong
Zn2+
inhibits the hydrolytic activity and the synthetic activity of the enzyme
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sodium cholate
activates at 0.07-0.7% w/v, loss of about 75% activation potency in absence of Ca2+
sodium taurodeoxycholate
-
1.0 mg/ml, slight activation
taurodeoxycholate
may substitute for Triton X-100 at 0.5%
taurodeoxycholate hydrate
TDC, activates at 0.07-0.7% w/v, TDC-based enhancement of hydrolysis requires the presence of Ca2+. In the absence of Ca2+, GM1 hydrolysis is only 2.9%, 14fold lower than the same case of Triton X-100
Tween 80
activates 0.07-0.7% w/v, loss of about 65% activation potency in absence of Ca2+
Triton X-100
required, 0.1%
Triton X-100
activates the hydrolytic reaction, best at 0.5% w/v, but inhibits the synthetic reaction
Triton X-100
activates at 0.07-0.7% w/v, loss of about 50% activation potency in absence of Ca2+
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analysis
-
the enzyme is immobilised on magnetic macroporous cellulose and is used to semisynthesise C17:0 glucosylceramide and C17:0 sulfatide, which are required as internal standards for quantification of the corresponding glycosphingolipids by tandem mass spectrometry
synthesis
-
a method for generation of novel fluorocarbon derivatives of glycosphingolipids has been developed. SCDase is used to remove the fatty acid from the ceramide moiety, after which a fluorocarbon-rich substituent is incorporated at the free amine of the sphingoid
synthesis
-
the enzyme is immobilised on magnetic macroporous cellulose and is used to semisynthesise C17:0 glucosylceramide and C17:0 sulfatide, which are required as internal standards for quantification of the corresponding glycosphingolipids by tandem mass spectrometry. A high rate of conversion is achieved for both lipids, 80% for C17:0 sulfatide and 90% for C17:0 glucosylceramide. In contrast to synthesis with a soluble form of the enzyme, use of immobilised SCDase significantly reduces the contamination of the sphingolipid products with other isoforms, so further purification is not necessary
synthesis
-
the enzyme can serve as a biocatalyst in the enzymatic synthesis of glycosphingolipids since it catalyzes the reversible hydrolysis/synthesis of the amide linkage between the fatty acid and the sphingosine base in the ceramide moiety of glycosphingolipids
synthesis
the enzyme can serve as a biocatalyst in the enzymatic synthesis of glycosphingolipids since it catalyzes the reversible hydrolysis/synthesis of the amide linkage between the fatty acid and the sphingosine base in the ceramide moiety of glycosphingolipids
synthesis
sphingolipid ceramide N-deacylase is used for lyso-glycosphingolipid production. Application to large-scale preparation of gamglioside lyso-GM1, overview
synthesis
-
the enzyme can serve as a biocatalyst in the enzymatic synthesis of glycosphingolipids since it catalyzes the reversible hydrolysis/synthesis of the amide linkage between the fatty acid and the sphingosine base in the ceramide moiety of glycosphingolipids
-
synthesis
-
sphingolipid ceramide N-deacylase is used for lyso-glycosphingolipid production. Application to large-scale preparation of gamglioside lyso-GM1, overview
-
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Hirabayashi, Y.; Kimura, M.; Matsumoto, M.; Yamamoto, K.; Kadowaki, S.; Tochikura, T.
A novel glycosphingolipid hydrolyzing enzyme, glycosphingolipid ceramide deacylase, which cleaves the linkage between the fatty acid and sphingosine base in glycosphingolipids
J. Biochem.
103
1-4
1988
Nocardia sp.
brenda
Ito, M.; Kurita, T.; Kita, K.
A novel enzyme that cleaves the N-acyl linkage of ceramides in various glycospingolipids as well as sphingomyelin to produce their lyso forms
J. Biol. Chem.
41
24370-24374
1995
Pseudomonas sp.
brenda
Furusato, M.; Sueyoshi, N.; Mitsutake, S.; Sakaguchi, K.; Kita, K.; Okino, N.; Ichinose, S.; Omori, A.; Ito, M.
Molecular cloning and characterization of sphingolipid ceramide N-deacylase from a marine bacterium, Shewanella alga G8
J. Biol. Chem.
277
17300-17307
2002
Shewanella algae (Q8RTY6), Shewanella algae G8 (Q8RTY6)
brenda
Li, Y.; Arigi, E.; Eichert, H.; Levery, S.
Mass spectrometry of fluorocarbon-labeled glycosphingolipids
J. Mass Spectrom.
45
504-519
2010
Pseudomonas sp. TK4
brenda
Kuchar, L.; Rotkova, J.; Asfaw, B.; Lenfeld, J.; Horak, D.; Korecka, L.; Bilkova, Z.; Ledvinova, J.
Semisynthesis of C17:0 isoforms of sulphatide and glucosylceramide using immobilised sphingolipid ceramide N-deacylase for application in analytical mass spectrometry
Rapid Commun. Mass Spectrom.
24
2393-2399
2010
Pseudomonas sp. TK4
brenda
Frank, S.; Geyer, H.; Geyer, R.
Microscale analysis of glycosphingolipids from Schistosoma mansoni cercariae
J. Carbohydr. Chem.
30
233-248
2011
Pseudomonas sp.
-
brenda
Han, Y.B.; Wu, L.; Rich, J.R.; Huang, F.T.; Withers, S.G.; Feng, Y.; Yang, G.Y.
Comprehensive characterization of sphingolipid ceramide N-deacylase for the synthesis and fatty acid remodeling of glycosphingolipids
Appl. Microbiol. Biotechnol.
99
6715-6726
2015
Pseudomonas sp., Shewanella algae (Q8RTY6), Shewanella algae, Shewanella algae G8 (Q8RTY6)
brenda
Huang, F.T.; Han, Y.B.; Feng, Y.; Yang, G.Y.
A facile method for controlling the reaction equilibrium of sphingolipid ceramide N-deacylase for lyso-glycosphingolipid production
J. Lipid Res.
56
1836-1842
2015
Shewanella algae (Q8RTY6), Shewanella algae G8 (Q8RTY6)
brenda