HORMONE-SENSITIVE LIPASE IS CLOSELY-RELATED TO SEVERAL BACTERIAL PROTEINS, AND DISTANTLY RELATED TO ACETYLCHOLINESTERASE AND LIPOPROTEIN-LIPASE - IDENTIFICATION OF A SUPERFAMILY OF ESTERASES AND LIPASES

被引:116
作者
HEMILA, H
KOIVULA, TT
PALVA, I
机构
[1] UNIV HELSINKI,DEPT GENET,HELSINKI,FINLAND
[2] AGR RES CTR,JOKIOINEN,FINLAND
来源
BIOCHIMICA ET BIOPHYSICA ACTA-LIPIDS AND LIPID METABOLISM | 1994年 / 1210卷 / 02期
关键词
LIPASE; CARBOXYLESTERASE; TRIACYLGLYCEROL; (B-ACIDOCALDARIUS);
D O I
10.1016/0005-2760(94)90129-5
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
We have sequenced a gene from Bacillus acidocaldarius which encodes an open reading frame (ORF3) of 310 amino acids. The ORF3 was found to be related to the mammalian hormone-sensitive lipase (HSL). Searching the protein data base revealed five other bacterial proteins related to the HSL. Upon further sequence comparisons this HSL-group was found to be related to the family of carboxylesterases, and to a family of lipases (lipoprotein, hepatic and pancreatic lipases). The evolutionary relationship of these serine-dependent hydrolytic enzymes has not been studied previously, and it has not been known that these proteins belong to the same superfamily. Finally, the alignment of the HSL with the bacterial proteins allowed us to infer the location of the hormone-sensitive regulatory domain of the HSL-protein.
引用
收藏
页码:249 / 253
页数:5
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