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Information on EC 3.5.1.69 - glycosphingolipid deacylase
for references in articles please use BRENDA:EC3.5.1.69
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EC Tree 3 Hydrolases
3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
3.5.1 In linear amides
3.5.1.69 glycosphingolipid deacylase
IUBMB Comments
Does not act on sphingolipids such as ceramide. Not identical with EC 3.5.1.23 ceramidase.
The enzyme appears in viruses and cellular organisms
showSynonyms
sa_scd, ps_scd, glycosphingolipid deacylase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
deacylase, glycosphingolipid ceramide
-
-
-
-
glycosphingolipid ceramide deacylase
-
-
-
-
SA_SCD
SCDase
sphingolipid ceramide N-deacylase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hydrolysis of gangliosides and neutral glycosphingolipids, releasing fatty acids to form the lyso-derivatives
hydrolysis of gangliosides and neutral glycosphingolipids, releasing fatty acids to form the lyso-derivatives
-
-
-
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hydrolysis of gangliosides and neutral glycosphingolipids, releasing fatty acids to form the lyso-derivatives
in addition to its primary deacylation function, this enzyme is able to reacylate lyso-sphingolipids under specific conditions
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of linear amides
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-
-
-
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SYSTEMATIC NAME
IUBMB Comments
glycosphingolipid amidohydrolase
Does not act on sphingolipids such as ceramide. Not identical with EC 3.5.1.23 ceramidase.
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CAS REGISTRY NUMBER
COMMENTARY
122544-53-0
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
gangliotetraosylceramide + H2O
glucosylceramide
-
Substrates: 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
Products: 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
Products: 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
?
16-(acetylsulfanyl)hexadecanoic acid + lyso-GM1a
? + H2O
-
Substrates: -
Products: -
Products: -
r
16-(acetylsulfanyl)hexadecanoic acid + lyso-GM1a
? + H2O
Substrates: -
Products: -
Products: -
r
16-[(prop-2-yn-1-yl)oxy]hexadecanoic acid + lyso-GM1a
? + H2O
-
Substrates: -
Products: -
Products: -
r
16-[(prop-2-yn-1-yl)oxy]hexadecanoic acid + lyso-GM1a
? + H2O
Substrates: -
Products: -
Products: -
r
2-hydroxydodecanoic acid + lyso-GM1a
? + H2O
Substrates: -
Products: -
Products: -
r
2-hydroxyhexadecanoic acid + lyso-GM1a
? + H2O
Substrates: -
Products: -
Products: -
r
asialoganglioside GM1 + H2O
fatty acid + ?
Substrates: -
Products: -
Products: -
?
asialoganglioside GM1 + H2O
fatty acid + ?
Substrates: -
Products: -
Products: -
?
eicosapentaenoic acid + lyso-GM1a
? + H2O
Substrates: -
Products: -
Products: -
r
ganglioside GD1a + H2O
fatty acid + lyso-GD1a-ganglioside
-
Substrates: -
Products: -
Products: -
?
ganglioside GD1a + H2O
fatty acid + lyso-GD1a-ganglioside
-
Substrates: -
Products: -
Products: -
?
ganglioside GM1 + H2O
octadecanoic acid + lyso-GM1-ganglioside
-
Substrates: -
Products: -
Products: -
?
ganglioside GM1 + H2O
octadecanoic acid + lyso-GM1-ganglioside
-
Substrates: -
Products: -
Products: -
?
ganglioside GM2 + H2O
fatty acid + lyso-GM2-ganglioside
-
Substrates: -
Products: -
Products: -
?
ganglioside GM2 + H2O
fatty acid + lyso-GM2-ganglioside
-
Substrates: -
Products: -
Products: -
?
ganglioside GM3 + H2O
fatty acid + lyso-GM3-ganglioside
-
Substrates: -
Products: -
Products: -
?
ganglioside GM3 + H2O
fatty acid + lyso-GM3-ganglioside
-
Substrates: -
Products: -
Products: -
?
hexadecanedioic acid methyl ester + lyso-GM1a
? + H2O
-
Substrates: -
Products: -
Products: -
r
hexadecanedioic acid methyl ester + lyso-GM1a
? + H2O
Substrates: -
Products: -
Products: -
r
omega-azido palmitic acid + lyso-GM1a
? + H2O
Substrates: -
Products: -
Products: -
r
omega-bromo-palmitic acid + lyso-GM1a
? + H2O
Substrates: -
Products: -
Products: -
r
omega-hydroxypalmitic acid + lyso-GM1a
? + H2O
Substrates: -
Products: -
Products: -
r
additional information
?
-
-
Substrates: does not act on sphingolipids such as ceramide, Galbeta(1-1')ceramide, Glcbeta(1-1')ceramide, Galbeta(1-4)Glcbeta(1-1')ceramide
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: the products are recovered by FluorosTM solid ohase extraction and analyzed by MALDI-QIT-TOF mass spectrometry and ESI-LIT mass spectrometry
Products: the products are recovered by FluorosTM solid ohase extraction and analyzed by MALDI-QIT-TOF mass spectrometry and ESI-LIT mass spectrometry
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: assay method optimization and evaluation, overview
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Fe2+
promotes the hydrolytic activity but inhibits the synthetic activity of the enzyme
Mg2+
Mn2+
Ni2+
promotes the hydrolytic activity but inhibits the synthetic activity of the enzyme
additional information
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+
promotes the hydrolytic activity but inhibits the synthetic activity of the enzyme
Mn2+
promotes the hydrolytic activity but inhibits the synthetic activity of the enzyme
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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+
inhibits the hydrolytic activity and the synthetic activity of the enzyme
Mn2+
promotes the hydrolytic activity but inhibits the synthetic activity of the enzyme
Zn2+
inhibits the hydrolytic activity and the synthetic activity of the enzyme
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
sodium cholate
activates at 0.07-0.7% w/v, loss of about 75% activation potency in absence of Ca2+
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
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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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.8
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
development of a facile method for controlling the reaction equilibrium of sphingolipid ceramide N-deacylase for lyso-glycosphingolipid production
additional information
-
development of a facile method for controlling the reaction equilibrium of sphingolipid ceramide N-deacylase for lyso-glycosphingolipid production
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
C-terminal processing of enzyme is necessary for full activity
proteolytic modification
-
C-terminal processing of enzyme is necessary for full activity
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
SCDase immobilised on magnetic macroporous cellulose maintains its activity without loss after 15 uses
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 50 mM phosphate buffer, pH 7, 0.1% Triton X-100, long-term stability is achieved by immobilisation on magnetic macroporous cellulose. The enzyme retains the same activity after 1.5 years in storage buffer
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme in Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged enzyme, lacking the secretion signal, from Escherichia coli strain BL21 (DE3) pLysS by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
the gene encoding the mature SA_SCD protein, which lacks its 38-residue N-terminal secretion signal sequence and from which the 277-residue C-terminal sequence is deleted, is codon-optimized and expressed in Escherichia coli strain BL21 (DE3) pLysS as Histagged enzyme
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
-
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 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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Shewanella algae (Q8RTY6), Shewanella algae, Pseudomonas sp., 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
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