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B6db references: 11018465

type Journal Article
authors Van Veldhoven, P.P.; Gijsbers, S.; Mannaerts, G.P.; Vermeesch, J.R.; Brys, V.
title Human sphingosine-1-phosphate lyase: cDNA cloning, functional expression studies and mapping to chromosome 10q22(1)
journal Biochim Biophys Acta
sel selected
ui 11018465
year (2000)
volume 1487
number 2-3
pages 128-34
keywords Aldehyde-Lyases/genetics/*physiology
abstract Sphingosine-1-phosphate lyase catalyzes the last step in sphingolipid breakdown, the cleavage of phosphorylated sphingoid bases such as sphingenine-1-phosphate. The latter lipid is not only a catabolite, but can influence as an inter- and/or intracellular second messenger many cellular processes. To allow for the diagnosis of human disorders that might be linked to a deficient lyase, the human sphingosine-1-phosphate lyase cDNA was cloned. The obtained cDNA encoded a protein of 568 amino acids with a calculated molecular mass of 63492 Da. Hydropathy plots revealed the presence of one membrane span near the amino-terminal which is however not required for enzyme activity since recombinant poly-His-tagged lyase, lacking this membrane span, was functionally active. Site-directed mutagenesis disclosed the importance of the cysteine residues 218 and 317 for the cleavage reaction. Northern analysis showed the presence of rare large-sized mRNAs of 6.7, 5.8 and 4 kb and the highest expression in liver. By fluorescent in situ hybridization, the gene was mapped to chromosome 10q22.
last changed 2009/06/23 09:14

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