|
type |
Journal Article |
authors |
Tamura, K.; Nishiura, H.; Mori, J.; Imai, H. |
title |
Cloning and characterization of a cDNA encoding serine palmitoyltransferase in Arabidopsis thaliana |
journal |
Biochem Soc Trans |
Activity |
2.3.1.50 |
Family |
2.3.1.50.b |
sel |
selected |
ui |
11171191 |
year |
(2000) |
volume |
28 |
number |
6 |
pages |
745-7 |
| |
keywords |
Acyltransferases/*genetics/*metabolism |
abstract |
The first and committed step in de novo sphingolipid synthesis is catalysed by serine palmitoyltransferase (EC 2.3.1.50), which condenses serine and palmitoyl-CoA to form 3-ketosphinganine in a pyridoxal-5'- phosphate-dependent reaction. We have isolated and characterized a cDNA clone from Arabidopsis thaliana that is homologous to yeast and mammalian LCB2. For a functional identification, the A. thaliana homologous cDNA was expressed in Escherichia coli, which resulted in significant production of new sphinganine in E. coli cells. |
last changed |
2009/01/12 19:20 |
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