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cDNA CLONING AND SEQUENCING OF HUMAN MILKBILE SALTSTIMULATED LIPASE
Bläckberg, Lars Bjursell, Gunnar Carlsson, Peter Enerbäck, Sven Hernell, Olle Nilsson, Jeanette
Bläckberg, Lars
Bjursell, Gunnar
Carlsson, Peter
Enerbäck, Sven
Hernell, Olle
Nilsson, Jeanette
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Issue Date
1991
Submitted date
2024-03-20
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Abstract
Wehave isolated and sequenced cDNAclones covering the entire coding sequence of human milk bile salt-stimulated lipase (BSSL). The deduced amino acid sequence starts with a 21 residues leader peptide. The open reading frame continues with 722 amino acid residues. The sequence contains in the C-terminal part a proline-rich repeat, 16 repeats of 11 amino acid residues each. The mRNAwasestimated to be approximately 2500 nt from Northern blot. The cDNAis 2432 bases long, which indicates that a near full-length copy of the transcript have been isolated. Comparisons with other enzymes show that BSSL is a new memberofthe supergene family of serine hydrolases. Not only is it closely related (in the N-terminal half virtually identical) to lysophospholipase from rat pancreas and cholesterol esterase from bovine pancreas, but also shows a high degree of homology to several esterases, e.g. acetyl choline esterase. It contains the sequence which has been proposedto be the acetylcholine binding site in acetyl choline esterase. In contrast, no such homologies could be found to typical lipases, with the exception of the consensus sequence GXSXGtypical for serine hydrolases.
Citation
Lipases : structure, mechanism and genetic engineering, 203 - 206
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Book chapter
conference paper
conference paper
Language
en
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Series/Report no.
GBF monographs ; Volume 16
ISSN
0930-4320
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ISBN
156081165X
3527283323
3527283323
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Attribution-NonCommercial-ShareAlike 4.0 International