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B6db activities: 2.3.1.50

2.3.1.50
Description Serine C-palmitoyltransferase
Alternative names serine palmitoyltransferase;
SPT;
3-oxosphinganine synthetase;
acyl-CoA:serine C-2 acyltransferase (decarboxylating)
Catalyzed reaction Palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO(2).
Cofactor Pyridoxal-phosphate.
Comments Serine C-palmitoyltransferase belongs to a subset PLP-depentent enzymes collectively known as 2-oxoamine synthases. Oxoamine synthases are involved in several very important primary biosynthetic pathways: SPT in sphingolipid biosynthesis, 5-aminolevulinate synthase (EC 2.3.1.37) in heme biosynthesis, and 8-amino-7-oxononanoate synthase (EC 2.3.1.47) in biotin biosynthesis.
In mammals, serine palmitoyltransferase comprises two different but homologous subunits, LCB1 (most likely a membrane-bound protein) and LCB2. In this database, the two subunits have been included in subfamily a and b, respectively. (Note: LCB1 IS NOT PLP-DEPENDENT)
In humans, these two subunits may combine with a third one (similar but not identical to LCB2) forming in a high-molecular mass complex that appears to reside on the endoplasmic membrane.
Diseases hereditary sensory neuropathy type I
Prosite PROSITE; PDOC00518;
PDB 2JG2; 4BMK;
Organisms -Eubacteria -Plants -Fungi -Metazoa -Human
 

Family 

 
Links Enzyme (activities) 2.3.1.50
BRENDA (activities) 2.3.1.50
KEGG (pathways) 2.3.1.50
PLPMDB (PLP mutants) 2.3.1.50
 
References
 Hornemann T, Wei Y, von Eckardstein A. (2007) Is the mammalian serine palmitoyltransferase a high-molecular-mass complex? Biochem J 405 157-64.

 Ikushiro H, Islam MM, Tojo H, Hayashi H. (2007) Molecular characterization of membrane-associated soluble serine palmitoyltransferases from Sphingobacterium multivorum and Bdellovibrio stolpii J Bacteriol 189 5749-61.

 Yard BA, Carter LG, Johnson KA, Overton IM, Dorward M, Liu H, McMahon SA, Oke M, Puech D, Barton GJ, Naismith JH, Campopiano DJ (2007) The structure of serine palmitoyltransferase; gateway to sphingolipid biosynthesis J Mol Biol 370 870-86.

 Han G, Gable K, Yan L, Allen MJ, Wilson WH, Moitra P, Harmon JM, Dunn TM. (2006) Expression of a novel marine viral single-chain serine palmitoyltransferase and construction of yeast and mammalian single-chain chimera J Biol Chem 281 39935-42.

 Bae, J.H.; Sohn, J.H.; Park, C.S.; Rhee, J.S.; Choi, E.S. (2003) Integrative transformation system for the metabolic engineering of the sphingoid base-producing yeast Pichia ciferrii Appl Environ Microbiol 69 812-9.

 Hanada, K. (2003) Serine palmitoyltransferase, a key enzyme of sphingolipid metabolism Biochim Biophys Acta 1632 16-30.

 Zhang, K.; Showalter, M.; Revollo, J.; Hsu, F.F.; Turk, J.; Beverley, S.M. (2003) Sphingolipids are essential for differentiation but not growth in Leishmania EMBO J 22 6016-26..

 Ikushiro, H, Hayashi, H, Kagamiyama, H. (2001) A water-soluble homodimeric serine palmitoyltransferase from Sphingomonas paucimobilis EY2395T strain. Purification, characterization, cloning, and overproduction J. Biol. Chem. 276 18249-18256.

 Tamura, K.; Nishiura, H.; Mori, J.; Imai, H. (2000) Cloning and characterization of a cDNA encoding serine palmitoyltransferase in Arabidopsis thaliana Biochem Soc Trans 28 745-7.

 Hanada, K.; Hara, T.; Nishijima, M.; Kuge, O.; Dickson, R.C.; Nagiec, M.M. (1997) A mammalian homolog of the yeast LCB1 encodes a component of serine palmitoyltransferase, the enzyme catalyzing the first step in sphingolipid synthesis J Biol Chem 272 32108-14.

 Weiss, B.; Stoffel, W. (1997) Human and murine serine-palmitoyl-CoA transferase--cloning, expression and characterization of the key enzyme in sphingolipid synthesis Eur J Biochem 249 239-47.

 Nagiec, M.M.; Baltisberger, J.A.; Wells, G.B.; Lester, R.L.; Dickson, R.C. (1994) The LCB2 gene of Saccharomyces and the related LCB1 gene encode subunits of serine palmitoyltransferase, the initial enzyme in sphingolipid synthesis. Proc Natl Acad Sci U S A 91 7899-902.

 Buede, R.; Rinker-Schaffer, C.; Pinto, W. J.; Lester, R. L.; Dickson, R. C. (1991) Cloning and characterization of LCB1, a Saccharomyces gene required for biosynthesis of the long-chain base component of sphingolipids J Bacteriol 173 4325-32.

Articles on 2.3.1.50
 
last changed 2017/10/10 14:13

B6db activities