Human milk bile‐salt stimulated lipase Sequence similarity with rat lysophospholipase and homology with the active site region of cholinesterases

FEBS Letters

Cleverly, Douglas R.¹  O'Connor, Charmian J.¹  Christie, David L.² 

[1] Department of Chemistry, University of Auckland, Private Bag, Auckland, New Zealand;Department of Biochemistry, University of Auckland, Private Bag, Auckland, New Zealand

关键词: Human milk bile-salt stimulated lipase;    Lysophospholipase;    Active site;    Acetylcholinesterase;    BSSL;    human milk bile-salt stimulated lipase;    DFP;    diisopropylfluorophosphate;    CEH;    pancreatic carboxyl-ester hydrolase;    CB;    CNBr-cleavage peptide;   

DOI  :  10.1016/0014-5793(91)80114-I

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

To determine the active site residue, human milk bile-salt stimulated lipase (BSSL) was labelled with [³H]diisopropyl fluorophosphate (DFP). Partial sequence analysis or cyanogen bromide fragments (a total of 146 residues from 6 peptides) revealed 84% sequence identity with a putative rat lysophospholipase. Sequence analysis of a [³H]DFP-labelled peptide indicated that the active site serine was contained in the sequence Gly-Glu-Scr-Ala-Gly. In addition to similarity with rat lysophospholipase, this sequence showed homology with regions of human butyrylcholinesterase and electric ray acetylcholinesterase (68% identity). It is concluded that these proteins are members of a new supergene family.

【 授权许可】

Unknown