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Information on EC 2.7.8.27 - sphingomyelin synthase and Organism(s) Rattus norvegicus and UniProt Accession Q4JM44

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IUBMB Comments
The reaction can occur in both directions . This enzyme occupies a central position in sphingolipid and glycerophospholipid metabolism . Up- and down-regulation of its activity has been linked to mitogenic and pro-apoptotic signalling in a variety of mammalian cell types . Unlike EC 2.7.8.3, ceramide cholinephosphotransferase, CDP-choline cannot replace phosphatidylcholine as the donor of the phosphocholine moiety of sphingomyelin .
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Rattus norvegicus
UNIPROT: Q4JM44
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Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
sphingomyelin synthase, sm synthase, sgms1, sphingomyelin synthase 1, sphingomyelin synthase 2, sgms2, sphingomyelin-synthase, sm synthase 1, sphingomyelin synthases 1, sphingomyelin synthase-related protein, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
sphingomyelin synthase 2
-
SM synthase
-
-
sphingomyelin synthase 1
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
substituted phospho group transfer
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
ceramide:phosphatidylcholine cholinephosphotransferase
The reaction can occur in both directions [3]. This enzyme occupies a central position in sphingolipid and glycerophospholipid metabolism [4]. Up- and down-regulation of its activity has been linked to mitogenic and pro-apoptotic signalling in a variety of mammalian cell types [4]. Unlike EC 2.7.8.3, ceramide cholinephosphotransferase, CDP-choline cannot replace phosphatidylcholine as the donor of the phosphocholine moiety of sphingomyelin [2].
CAS REGISTRY NUMBER
COMMENTARY hide
58703-97-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
phosphatidylcholine + ceramide
sphingomyelin + diacylglycerol
show the reaction diagram
phosphatidylcholine + ceramide
sphingomyelin + 1,2-diacyl-sn-glycerol
show the reaction diagram
-
-
-
-
?
sphingomyelin + diacylglycerol
ceramide + phosphatidylcholine
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
phosphatidylcholine + ceramide
sphingomyelin + diacylglycerol
show the reaction diagram
SMS2 is crucial to cellular lipid metabolism
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Thioacetamide
-
thioacetamide-induced increase in microsomal sphingomyelin by a stimulation of sphingomyelin synthase
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.112
diacylglycerol
-
-
0.0356
sphingomyelin
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Sprague-Dawley rats
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
primary culture
Manually annotated by BRENDA team
primary culture
Manually annotated by BRENDA team
-
changes in the mRNA expression of the SMS1 gene occur in rats after focal cerebral ischemia. In damaged ipsilateral cortex in the ischemic cortex, the level of SMS1 transcripts is decreased, overview
Manually annotated by BRENDA team
expression of SMS2 is limited to late round spermatids and elongating spermatids, not detected in late elongate spermatids. SMS2 associates with the developing acrosome beginning in late round spermatids through elongating spermatids and in the cell membrane. SMS2 may play a crucial role in the plasma membrane restructuring from late round spermatids to early elongating spermatids
Manually annotated by BRENDA team
seminiferous epithelium of adult rat
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
SMS2 associates with the developing acrosome beginning in late round spermatids through elongating spermatids. SMS2 may play a crucial role in the arosome formation
-
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
-
isoform SMS1 and SMS2
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
down-regulation of isoform SMS1 and SMS2 reduces the localization of the DAG-binding protein, protein kinase D to the Golgi. Inhibition of the enzyme significantly reduces insulin secretion in rat INS-1 cells
physiological function
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isoform SMS1 and SMS2 are capable of regulating trans golgi network-mediated protein trafficking and secretion. Both isoform activities are critical to retain the correct morphology of both cis-Golgi and trans-Golgi network
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SMS2_RAT
365
6
42223
Swiss-Prot
other Location (Reliability: 1)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene SMS2 from testis, DNA and amino acid sequence determination and analysis, sequence comparison, tissue expression analysis, overview
gene SMS1, expression analysis in healthy and ischemic neurons, effect of permanent middle cerebral artery occlusion on expression of SMS1 transcripts, overview
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Miro-Obradors, M.J.; Osada, J.; Aylagas, H.; Sanchez-Vegazo, I.; Palacios-Alaiz, E.
Microsomal sphingomyelin accumulation in thioacetamide-injured regenerating rat liver: involvement of sphingomyelin synthase activity
Carcinogenesis
14
941-946
1993
Rattus norvegicus
Manually annotated by BRENDA team
Albi, E.; Magni, M.V.
Sphingomyelin synthase in rat liver nuclear membrane and chromatin
FEBS Lett.
460
369-372
1999
Rattus norvegicus
Manually annotated by BRENDA team
Albi, E.; Lazzarini, R.; Magni, M.V.
Reverse sphingomyelin-synthase in rat liver chromatin
FEBS Lett.
549
152-156
2003
Rattus norvegicus
Manually annotated by BRENDA team
Lee, N.P.; Mruk, D.D.; Xia, W.; Cheng, C.Y.
Cellular localization of sphingomyelin synthase 2 in the seminiferous epithelium of adult rat testes
J. Endocrinol.
192
17-32
2007
Rattus norvegicus, Rattus norvegicus (Q4JM44)
Manually annotated by BRENDA team
Dmitrieva, V.G.; Torshina, E.V.; Yuzhakov, V.V.; Povarova, O.V.; Skvortsova, V.I.; Limborska, S.A.; Dergunova, L.V.
Expression of sphingomyelin synthase 1 gene in rat brain focal ischemia
Brain Res.
1188
222-227
2008
Rattus norvegicus
Manually annotated by BRENDA team
Subathra, M.; Qureshi, A.; Luberto, C.
Sphingomyelin synthases regulate protein trafficking and secretion
PLoS ONE
6
e23644
2011
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team