セリンパルミトイルトランスフェラーゼ
- 関
- serine C-palmitoyltransferase
WordNet
- a sweetish crystalline amino acid involved in the synthesis by the body of cysteine
- any of various brown and yellow finches of parts of Europe
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2013/05/30 22:34:03」(JST)
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| serine C-palmitoyltransferase |
| Identifiers |
| EC number |
2.3.1.50 |
| CAS number |
62213-50-7 |
| Databases |
| IntEnz |
IntEnz view |
| BRENDA |
BRENDA entry |
| ExPASy |
NiceZyme view |
| KEGG |
KEGG entry |
| MetaCyc |
metabolic pathway |
| PRIAM |
profile |
| PDB structures |
RCSB PDB PDBe PDBsum |
| Gene Ontology |
AmiGO / EGO |
| Search |
| PMC |
articles |
| PubMed |
articles |
| NCBI |
proteins |
|
| Serine palmitoyltransferase |
Crystallographic structure of serine palmitoyltransferase from S. paucimobilis. The cofactor PLP is visible in the center.[1] |
| Identifiers |
| Symbol |
? |
| PDB |
2JG2 |
| UniProt |
Q93UV0 |
| Other data |
| EC number |
2.3.1.50 |
| serine palmitoyltransferase, long chain base subunit 1 |
| Identifiers |
| Symbol |
SPTLC1 |
| Alt. symbols |
HSN1 |
| Entrez |
10558 |
| HUGO |
11277 |
| OMIM |
605712 |
| RefSeq |
NM_006415 |
| UniProt |
O15269 |
| Other data |
| EC number |
2.3.1.50 |
| Locus |
Chr. 9 q22.31 |
| serine palmitoyltransferase, long chain base subunit 2 |
| Identifiers |
| Symbol |
SPTLC2 |
| Entrez |
9517 |
| HUGO |
11278 |
| OMIM |
605713 |
| RefSeq |
NM_004863 |
| UniProt |
O15270 |
| Other data |
| EC number |
2.3.1.50 |
| Locus |
Chr. 14 q24.3 |
| serine palmitoyltransferase, long chain base subunit 3 |
| Identifiers |
| Symbol |
SPTLC3 |
| Alt. symbols |
C20orf38, SPTLC2L |
| Entrez |
55304 |
| HUGO |
16253 |
| OMIM |
611120 |
| RefSeq |
NM_018327 |
| UniProt |
Q9NUV7 |
| Other data |
| EC number |
2.3.1.50 |
| Locus |
Chr. 20 p12.1 |
In enzymology, a serine C-palmitoyltransferase (EC 2.3.1.50) is an enzyme that catalyzes the chemical reaction:[2][3]
- palmitoyl-CoA + L-serine CoA + 3-dehydro-D-sphinganine + CO2
Thus, the two substrates of this enzyme are palmitoyl-CoA and L-serine, whereas its 3 products are CoA, 3-dehydro-D-sphinganine, and CO2.[4][5] This reaction is a key step in the biosynthesis of sphingosine which is a precursor of many other sphingolipids.[3]
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is palmitoyl-CoA:L-serine C-palmitoyltransferase (decarboxylating). Other names in common use include serine palmitoyltransferase, SPT, 3-oxosphinganine synthetase, and acyl-CoA:serine C-2 acyltransferase decarboxylating. This enzyme participates in sphingolipid metabolism. It employs one cofactor, pyridoxal phosphate.
Species distribution [edit]
This enzyme is expressed in a large number of species from bacteria to humans. The bacterial enzyme is a water soluble homodimer[2] whereas in eukaryotes the enzyme is a heterodimer which is anchored to the endoplasmic reticulum.[3] Humans and other mammals express three paralogous subunits SPTLC1, SPTLC2, and SPTLC3. It was originally proposed that the functional human enzyme is a heterodimer between a SPTLC1 subunit and a second subunit which is either SPTLC2 or SPTLC3.[6] However more recent data suggest that the enzyme may exist as a larger complex, possibly a octamer, comprising all three subunits.[7]
Structural studies [edit]
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2JG2 and 2JGT.[1]
References [edit]
- ^ a b PDB 2JG2; Yard BA, Carter LG, Johnson KA, Overton IM, Dorward M, Liu H, McMahon SA, Oke M, Puech D, Barton GJ, Naismith JH, Campopiano DJ (July 2007). "The structure of serine palmitoyltransferase; gateway to sphingolipid biosynthesis". J. Mol. Biol. 370 (5): 870–86. doi:10.1016/j.jmb.2007.04.086. PMID 17559874.
- ^ a b Ikushiro H, Hayashi H, Kagamiyama H (April 2003). "Bacterial serine palmitoyltransferase: a water-soluble homodimeric prototype of the eukaryotic enzyme". Biochim. Biophys. Acta 1647 (1-2): 116–20. doi:10.1016/S1570-9639(03)00074-8. PMID 12686119.
- ^ a b c Hanada K (June 2003). "Serine palmitoyltransferase, a key enzyme of sphingolipid metabolism". Biochim. Biophys. Acta 1632 (1-3): 16–30. doi:10.1016/S1388-1981(03)00059-3. PMID 12782147.
- ^ Brady RN, Di Mari SJ, Snell EE (January 1969). "Biosynthesis of sphingolipid bases. 3. Isolation and characterization of ketonic intermediates in the synthesis of sphingosine and dihydrosphingosine by cell-free extracts of Hansenula ciferri". J. Biol. Chem. 244 (2): 491–6. PMID 4388074.
- ^ Stoffel W, LeKim D, Sticht G (May 1968). "Biosynthesis of dihydrosphingosine in vitro". Hoppe-Seyler's Z. Physiol. Chem. 349 (5): 664–70. PMID 4386961.
- ^ Hornemann T, Richard S, Rütti MF, Wei Y, von Eckardstein A (December 2006). "Cloning and initial characterization of a new subunit for mammalian serine-palmitoyltransferase". J. Biol. Chem. 281 (49): 37275–81. doi:10.1074/jbc.M608066200. PMID 17023427.
- ^ Hornemann T, Wei Y, von Eckardstein A (July 2007). "Is the mammalian serine palmitoyltransferase a high-molecular-mass complex?". Biochem. J. 405 (1): 157–64. doi:10.1042/BJ20070025. PMC 1925250. PMID 17331073.
|
Transferases: acyltransferases (EC 2.3)
|
|
| 2.3.1: other than amino-acyl groups |
- acetyltransferases: Acetyl-Coenzyme A acetyltransferase
- N-Acetylglutamate synthase
- Choline acetyltransferase
- Dihydrolipoyl transacetylase
- Acetyl-CoA C-acyltransferase
- Beta-galactoside transacetylase
- Chloramphenicol acetyltransferase
- N-acetyltransferase
- Serotonin N-acetyl transferase
- HGSNAT
- ARD1A
- Histone acetyltransferase
- palmitoyltransferases: Carnitine O-palmitoyltransferase
- Serine C-palmitoyltransferase
- other: Acyltransferase like 2
- Aminolevulinic acid synthase
- Beta-ketoacyl-ACP synthase
- Glyceronephosphate O-acyltransferase
- Lecithin-cholesterol acyltransferase
- Glycerol-3-phosphate O-acyltransferase
- 1-acylglycerol-3-phosphate O-acyltransferase
- 2-acylglycerol-3-phosphate O-acyltransferase
- ABHD5
|
|
| 2.3.2: Aminoacyltransferases |
- Gamma-glutamyl transpeptidase
- Peptidyl transferase
- Transglutaminase
- Tissue transglutaminase
- Keratinocyte transglutaminase
- Factor XIII
|
|
| 2.3.3: converted into alkyl on transfer |
- Citrate synthase
- ATP citrate lyase
- HMG-CoA synthase
|
|
- B
- enzm
- 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 2.7.10
- 2.7.11-12
- 3.1
- 4.1
- 5.1
- 6.1-3
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Metabolism: lipid metabolism · glycolipid enzymes
|
|
| Sphingolipid |
|
To glycosphingolipid
|
- Glycosyltransferase · Sulfotransferase
|
|
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To ceramide
|
- From ganglioside: Beta-galactosidase
- Hexosaminidase A
- Neuraminidase
- Glucocerebrosidase
- From globoside: Hexosaminidase B
- Alpha-galactosidase
- Beta-galactosidase
- Glucocerebrosidase
- From sphingomyelin: Sphingomyelin phosphodiesterase (Sphingomyelin phosphodiesterase 1)
- From sulfatide: Arylsulfatase A
- Galactosylceramidase
|
|
|
To sphingosine
|
- Ceramidase
- ACER1
- ACER2
- ACER3
- ASAH1
- ASAH2
- ASAH2B
- ASAH2C
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Other
|
Sphingosine kinase
|
|
|
| NCL |
- Palmitoyl protein thioesterase
- Tripeptidyl peptidase I
- CLN3
- CLN5
- CLN6
- CLN8
|
|
| Ceramide synthesis |
- Serine C-palmitoyltransferase (SPTLC1)
- Ceramide glucosyltransferase (UGCG)
|
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|
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mt, k, c/g/r/p/y/i, f/h/s/l/o/e, a/u, n, m
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k, cgrp/y/i, f/h/s/l/o/e, au, n, m, epon
|
m (A16/C10), i (k, c/g/r/p/y/i, f/h/s/o/e, a/u, n, m)
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UpToDate Contents
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English Journal
- 1-Deoxysphingolipid-induced neurotoxicity involves N-methyl-D-aspartate receptor signaling.
- Güntert T1, Hänggi P1, Othman A2, Suriyanarayanan S3, Sonda S4, Zuellig RA5, Hornemann T2, Ogunshola OO6.
- Neuropharmacology.Neuropharmacology.2016 Mar 22. pii: S0028-3908(16)30105-8. doi: 10.1016/j.neuropharm.2016.03.033. [Epub ahead of print]
- 1-Deoxysphingolipids (1-deoxySL) are atypical and neurotoxic sphingolipids formed by alternate substrate usage of the enzyme serine-palmitoyltransferase. Pathologically increased 1-deoxySL formation causes hereditary sensory and autosomal neuropathy type 1 (HSAN1) - a progressive peripheral axonopat
- PMID 27016021
- Viral serine palmitoyltransferase induces metabolic switch in sphingolipid biosynthesis and is required for infection of a marine alga.
- Ziv C1, Malitsky S1, Othman A2, Ben-Dor S3, Wei Y4, Zheng S1, Aharoni A1, Hornemann T4, Vardi A5.
- Proceedings of the National Academy of Sciences of the United States of America.Proc Natl Acad Sci U S A.2016 Mar 16. pii: 201523168. [Epub ahead of print]
- Marine viruses are the most abundant biological entities in the oceans shaping community structure and nutrient cycling. The interaction between the bloom-forming alga Emiliania huxleyi and its specific large dsDNA virus (EhV) is a major factor determining the fate of carbon in the ocean, thus servi
- PMID 26984500
- The Role of ORMDL Proteins, Guardians of Cellular Sphingolipids, in Asthma.
- Paulenda T1, Draber P1.
- Allergy.Allergy.2016 Mar 10. doi: 10.1111/all.12877. [Epub ahead of print]
- A family of widely expressed ORM-like (ORMDL) proteins has been recently linked to asthma in genome-wide association studies in humans and extensively explored in in vivo studies in mice. ORMDL proteins are key regulators of serine palmitoyltransferase, an enzyme catalyzing the initial step of sphin
- PMID 26969910
Japanese Journal
- The Essential Structures of ISP-I that Influence Serine Palmitoyltransferase Inhibition in Chinese Hamster Ovary Cells
- Mizukoshi Koji,Matsumoto Katsuo,Hirose Ryoji,Fujita Tetsuro
- Biological and Pharmaceutical Bulletin 35(8), 1349-1353, 2012
- … We investigated the structure–activity relationship between various ISP-I (myriocin, thermozymocidin) analogous which has sphingosine-like structure and serine palmitoyltransferase (SPT) in Chinese hamster ovary (CHO) cells utilizing sphingolipid production as a marker. … In addition, a serine structure is necessary for SPT inhibitory activity, which confirms previous findings. …
- NAID 130001872155
- Effects of Serine Palmitoyltransferase Inhibitor ISP-I on the Stratum Corneum of Intact Mouse Skin
- Mizukoshi Koji,Matsumoto Katsuo,Hirose Ryouji,Fujita Tetsuro,Ishida-Yamamoto Akemi,Iizuka Hajime
- Biological and Pharmaceutical Bulletin 34(9), 1383-1389, 2011
- … Serine palmitoyltransferase (SPT) is involved in the ceramide synthesis pathway. … The activity of serine protease—an enzyme associated with the process of desquamation—was lower in the SC of ISP-I-treated skin than control. …
- NAID 130001872429
- セリンパルミトイル転移酵素の触媒反応におけるHis159の多機能的役割
- 生城 浩子,白岩 有桂,林 秀行
- ビタミン 84(9), 423-431, 2010-09-25
- … Serine palmitoyltransferase (SPT) is a key enzyme of sphingolipid biosynthesis and catalyzes the decarboxylative condensation of L-serine with palmitoyl-CoA to form 3-ketodihydrosphingosine. … All mutant SPTs formed the PLP-L-serine aldimine and catalyzed the abortive transamination of L-serine. …
- NAID 110007730458
Related Links
- 1. Biochim Biophys Acta. 2003 Jun 10;1632(1-3):16-30. Serine palmitoyltransferase, a key enzyme of sphingolipid metabolism. Hanada K(1). Author information: (1)Department of Biochemistry and Cell Biology, National ...
- 1. J Mol Biol. 2007 Jul 27;370(5):870-86. Epub 2007 May 10. The structure of serine palmitoyltransferase; gateway to sphingolipid biosynthesis. Yard BA(1), Carter LG, Johnson KA, Overton IM, Dorward M, Liu H ...
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パルミトイルトランスフェラーゼ、パルミチン酸転移酵素
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セリン
- 関
- L-serine、S、Ser