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Information on EC 2.8.2.11 - galactosylceramide sulfotransferase and Organism(s) Mus musculus and UniProt Accession Q9JHE4
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2.8.2.11 galactosylceramide sulfotransferaseIUBMB Comments
Also acts on lactosylceramide.
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Word Map
- 2.8.2.11
- sulfatide
- myelin
- glycolipids
-
sulfoglycolipids
-
paranodal
- sulfolipids
-
smkt-r3
- galactolipids
- seminolipid
-
3'-phosphohydrolase
-
axo-glial
- medicine
-
laccer
- diagnostics
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
cerebroside sulfotransferase, gal3st1, glycolipid sulfotransferase, galactosylceramide sulfotransferase, galactolipid sulfotransferase, galactocerebroside sulfotransferase, galcer sulfotransferase, galactosylceramide 3'-sulfotransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3'-phosphoadenosine-5'-phosphosulfate-cerebroside sulfotransferase
-
-
-
-
cerebroside sulfotransferase
CST
galactocerebroside sulfotransferase
galactolipid sulfotransferase
-
-
-
-
galactosylceramide sulfotransferase
-
-
-
-
glycolipid sulfotransferase
-
-
-
-
glycosphingolipid sulfotransferase
-
-
-
-
GSase
-
-
-
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sulfotransferase, galactocerebroside
-
-
-
-
cerebroside sulfotransferase
-
-
-
-
CST
-
-
-
-
galactocerebroside sulfotransferase
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-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3'-phosphoadenylyl sulfate + a galactosylceramide = adenosine 3',5'-bisphosphate + a galactosylceramidesulfate
the N-glycosylation of Asn-312 and Asn-66 is necessary to form a fully active enzyme
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
sulfate group transfer
sulfate group transfer
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
3'-phosphoadenylyl-sulfate:galactosylceramide 3'-sulfotransferase
Also acts on lactosylceramide.
CAS REGISTRY NUMBER
COMMENTARY
9081-06-5
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3'-phosphoadenylyl sulfate + a galactosylceramide
adenosine 3',5'-bisphosphate + a galactosylceramidesulfate
-
-
-
?
3'-phosphoadenylyl sulfate + galactoscerebroside
adenosine 3',5'-bisphosphate + galactocerebroside 3-sulfate
3'-phosphoadenylyl sulfate + a galactosylceramide
adenosine 3',5'-bisphosphate + a galactosylceramidesulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + cerebroside
adenosine 3',5'-bisphosphate + cerebroside 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + galactosylceramide
adenosine 3',5'-bisphosphate + galactosylceramide sulfate
-
-
-
-
?
galactocerebroside + 3'-phosphoadenylylsulfate
galactocerebroside 3-sulfate + adenosine 3',5'-bisphosphate
galactocerebroside + 3'-phosphoadenylylsulfate
sulfogalactoglycerolipid + adenosine 3',5'-bisphosphate
-
enzyme catalyses the biosynthesis of sulfatides, sulfatides are important components of myelin
-
-
?
galactosyl 1-alkyl-2-acyl-sn-glycerol + 3'-phosphoadenylylsulfate
galactosyl 1-alkyl-2-acyl-sn-glycerol sulfate + adenosine 3',5'-bisphosphate
-
-
-
-
?
galactosylceramide + 3'-phosphoadenylylsulfate
galactosylceramide sulfate + adenosine 3',5'-bisphosphate
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biotinylated and light-sensitive azido derivatives of lysogalactosylceramide are synthesized by the crude enzyme preparation, these derivatives remain effective substrates for the testicular enzyme
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-
?
3'-phosphoadenylyl sulfate + galactoscerebroside
adenosine 3',5'-bisphosphate + galactocerebroside 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + galactoscerebroside
adenosine 3',5'-bisphosphate + galactocerebroside 3-sulfate
galactocerebroside and sulfatide are two major glycolipids in myelin, absence of sulfatide in CST-deficient mice causes axonal disorders
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-
?
galactocerebroside + 3'-phosphoadenylylsulfate
galactocerebroside 3-sulfate + adenosine 3',5'-bisphosphate
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-
-
-
?
galactocerebroside + 3'-phosphoadenylylsulfate
galactocerebroside 3-sulfate + adenosine 3',5'-bisphosphate
-
-
-
?
additional information
?
-
-
enzyme is a key enzyme in the biosynthesis of sulfoglycolipids
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-
?
additional information
?
-
-
CST catalyzes the 3'-sulfation of galactose residues in several glycolipids, its major product in the mammalian brain is sulfatide, which is an essential myelin component
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-
?
additional information
?
-
CST catalyzes the 3'-sulfation of galactose residues in several glycolipids, its major product in the mammalian brain is sulfatide, which is an essential myelin component
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3'-phosphoadenylyl sulfate + a galactosylceramide
adenosine 3',5'-bisphosphate + a galactosylceramidesulfate
-
-
-
?
3'-phosphoadenylyl sulfate + galactoscerebroside
adenosine 3',5'-bisphosphate + galactocerebroside 3-sulfate
galactocerebroside and sulfatide are two major glycolipids in myelin, absence of sulfatide in CST-deficient mice causes axonal disorders
-
-
?
galactocerebroside + 3'-phosphoadenylylsulfate
sulfogalactoglycerolipid + adenosine 3',5'-bisphosphate
-
enzyme catalyses the biosynthesis of sulfatides, sulfatides are important components of myelin
-
-
?
additional information
?
-
-
enzyme is a key enzyme in the biosynthesis of sulfoglycolipids
-
-
?
additional information
?
-
-
CST catalyzes the 3'-sulfation of galactose residues in several glycolipids, its major product in the mammalian brain is sulfatide, which is an essential myelin component
-
-
?
additional information
?
-
CST catalyzes the 3'-sulfation of galactose residues in several glycolipids, its major product in the mammalian brain is sulfatide, which is an essential myelin component
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
major part of the enzyme, not to the trans-Golgi network
major part of the enzyme, the enzyme contains a transmembrane domain
additional information
additional information
determination of subcellular localization, overview
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
CST knockout (CST-/-) mice, in which sulfatide is completely depleted, are born healthy, but display myelin abnormalities and progressive tremors starting at 4-6 weeks of age. A one-third reduction of the major compact-myelin proteins (myelin basic protein, MBP, and proteolipid protein, PLP) and an equivalent post-developmental loss of myelin lipids is detected, providing the molecular basis behind the thinner myelin sheaths. Lipidomics data demonstrate that the observed global reduction of myelin lipid content is not due to an increase of lipid degradation but rather to the reduction of their synthesis by oligodendrocytes. Sulfatide depletion leads to region-specific effects on non-compact myelin, dramatically affecting the paranode (neurofascin 155) and the major inner-tongue myelin protein (myelin-associated glycoprotein). Progressive decline of high molecular weight PLP complexes in CST-/- mice. Loss of ST results in reduced GalCer synthesis and/or increased GalCer degradation. Proposed molecular mechanisms underlying the effects of ST depletion on myelin structure/function, overview
physiological function
physiological function
additional information
analysis of the major CNS myelin proteins and the major lipids enriched in the myelin in a spatiotemporal manner, overview
physiological function
cerebroside sulfotransferase (CST) catalyzes the production of sulfatide, a major class of myelin-specific lipids. Sulfatide plays a critical role in myelin maintenance/function. Sulfatide (ST) promotes the interaction between adjacent PLP extracellular domains. The myelin sheath is a multilamellar, spirally wrapping extension of the plasma membrane of oligodendrocytes (OLs) in the central nervous system (CNS). Sulfatide mediates intraperiod line and myelin-axon junction interactions, and it plays a critical role in maintaining compact myelin, nodal and paranodal homeostasis
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). G3ST1_MOUSE
423
1
48968
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
54000
2 * 54000, recombinant HA-tagged enzyme, SDS-PAGE, CST forms homodimers, and dimerization is mediated by the lumenal domain of the enzyme, overview
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
calculated, glycerol gradient centrifugation in vitro and fluorescence correlation spectroscopy in vivo
dimer
2 * 54000, recombinant HA-tagged enzyme, SDS-PAGE, CST forms homodimers, and dimerization is mediated by the lumenal domain of the enzyme, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
two N-glycosylation sites at N66 and N312 are present and used
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
a sulfatide (ST)-deficient mouse model is generated by disrupting the gene that encodes the enzyme cerebroside sulfotransferase (CST) that catalyzes the last step of ST biosynthesis. CST knockout (CST-/-) mice, which show a complete loss of ST in brain tissue, are born healthy, but begin displaying hindlimb weakness and tremors by 4-6 weeks of age. These defects aggravate with age, causing pronounced tremor and eventual ataxia, that lead to partial or complete paralysis by 12 months of age and eventually result in premature death which typically occurs around 15 months. Molecular fingerprints underlying the myelin phenotypes are described for CST KO mice, including (1) a one-third loss of compact-myelin proteins and major myelin lipids, presumably due to the loss of negative charges from ST species, (2) a striking post-developmental loss of MAG and NF155, and (3) a progressive loss of intermolecular PLP interactions. The tremor and ataxic phenotypes that occur in the absence of ST are a consequence of the loss of NF155 and PLP intermolecular interactions. Loss of ST results in reduced GalCer synthesis and/or increased GalCer degradation. ST depletion leads to a post-developmental disruption of myelin sphingolipid homeostasis. ST depletion leads to a dramatic and progressive loss of NF155 in every CNS region analyzed
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
ethylene glycol, 2-mercaptoethanol, 10 mM ATP and a mixture of phosphatidylcholine and phosphatidylethanolamine ratio 1:1 does not improve stability at -80°C
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in CHO-GalT cells or COS cells, enzyme can be expressed in a soluble form, that is active both in vitro and in vivo
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transcripts of the enzyme gene are detected in kidney, brain, testis, small intestine, stomach, liver, and lung, but the enzyme activity does not correlate with the amount of enzyme mRNA
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transient or stable expression as GFP-tagged enzyme in CHO-K1 cells, expression of CST fused to a HA-tag or EGFP in BHK cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
transcript levels are dramatically reduced in BORIS (brother of the regulator of imprinted sites) knockout testes
altered expression via protein-overload treatment, protein and gene expression of CST is significantly decreased in the liver in a time-dependent manner
-
altered expression via protein-overload treatment, renal expression of CST is markedly increased
-
chronic ethanol consumption decreases the expression of the enzyme in the liver
-
fenofibrate treatment increases cerebroside sulfotransferase mRNA level in the kidney, heart, liver, and small intestine, but not in brain and colon. Peroxisome proliferator-activated receptor alpha activation induces cerebroside sulfotransferase gene expression
-
the activity of galactocerebroside sulfotransferase decreases in a temperature-dependent manner
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
inhibition of CST could be an option for the treatment of metachromatic leukodystrophy
diagnostics
-
the newly developed system could provide useful basic data for the further analysis of seminolipid metabolism
medicine
-
the mechanism, indicating the crosstalk between kidney injury and specific liver functions, may prove useful to understand the situation where human hemodialysis patients have low levels of serum sulfatides
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sundaram, K.S.; Lev, M.
Purification and activation of brain sulfotransferase
J. Biol. Chem.
267
24041-24044
1992
Mus musculus
Burkart, T.; Siegrist, H.P.; Herschkowitz, N.N.; Wiesmann, U.N.
3-phosphoadenylylsulfate:galactosylceramide 3-sulfotransferase. An optimized assay in homogenates of developing brain
Biochim. Biophys. Acta
483
303-311
1977
Mus musculus
Hirahara, Y.; Tsuda, M.; Wada, Y.; Honke, K.
cDNA cloning, genomic cloning, and tissue-specific regulation of mouse cerebroside sulfotransferase
Eur. J. Biochem.
267
1909-1917
2000
Mus musculus
Eckhardt, M.; Fewou, S.N.; Ackermann, I.; Gieselmann, V.
N-glycosylation is required for full enzymic activity of the murine galactosylceramide sulphotransferase
Biochem. J.
368
317-324
2002
Mus musculus
Yaghootfam, A.; Sorkalla, T.; Haeberlein, H.; Gieselmann, V.; Kappler, J.; Eckhardt, M.
Cerebroside sulfotransferase forms homodimers in living cells
Biochemistry
46
9260-9269
2007
Mus musculus, Mus musculus (Q9JHE4)
Hoshi, T.; Suzuki, A.; Hayashi, S.; Tohyama, K.; Hayashi, A.; Yamaguchi, Y.; Takeuchi, K.; Baba, H.
Nodal protrusions, increased Schmidt-Lanterman incisures, and paranodal disorganization are characteristic features of sulfatide-deficient peripheral nerves
Glia
55
584-594
2007
Mus musculus (Q9JHE4)
Zhang, X.; Nakajima, T.; Kamijo, Y.; Li, G.; Hu, R.; Kannagi, R.; Kyogashima, M.; Aoyama, T.; Hara, A.
Acute kidney injury induced by protein-overload nephropathy down-regulates gene expression of hepatic cerebroside sulfotransferase in mice, resulting in reduction of liver and serum sulfatides
Biochem. Biophys. Res. Commun.
390
1382-1388
2009
Mus musculus
Nagai, K.I.; Tadano-Aritomi, K.; Niimura, Y.; Ishizuka, I.
Development and application of a system for seminolipid metabolism using mouse seminiferous tubules
Glycoconj. J.
27
181-187
2010
Mus musculus
Nakajima, T.; Kamijo, Y.; Yuzhe, H.; Kimura, T.; Tanaka, N.; Sugiyama, E.; Nakamura, K.; Kyogashima, M.; Hara, A.; Aoyama, T.
Peroxisome proliferator-activated receptor alpha mediates enhancement of gene expression of cerebroside sulfotransferase in several murine organs
Glycoconj. J.
30
553-560
2013
Mus musculus
Suzuki, T.; Kosaka-Suzuki, N.; Pack, S.; Shin, D.M.; Yoon, J.; Abdullaev, Z.; Pugacheva, E.; Morse, H.C.; Loukinov, D.; Lobanenkov, V.
Expression of a testis-specific form of Gal3st1 (CST), a gene essential for spermatogenesis, is regulated by the CTCF paralogous gene BORIS
Mol. Cell. Biol.
30
2473-2484
2010
Mus musculus (Q9JHE4)
Kanbe, H.; Kamijo, Y.; Nakajima, T.; Tanaka, N.; Sugiyama, E.; Wang, L.; Fang, Z.Z.; Hara, A.; Gonzalez, F.J.; Aoyama, T.
Chronic ethanol consumption decreases serum sulfatide levels by suppressing hepatic cerebroside sulfotransferase expression in mice
Arch. Toxicol.
88
367-379
2014
Mus musculus
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