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• W2017025152 endingPage "986" @default.
• W2017025152 startingPage "973" @default.
• W2017025152 abstract "Human gastric lipase (HGL) is a lipolytic enzyme that is secreted by the chief cells located in the fundic part of the stomach. HGL plays an important role in lipid digestion, since it promotes the subsequent hydrolytic action of pancreatic lipase in duodenal lumen. Physiological studies have shown that HGL is able of acting not only in the highly acid stomach environment but also in the duodenum in synergy with human pancreatic lipase (HPL). Recombinant HGL (r-HGL) was expressed in the baculovirus/insect cell system in the form of an active protein with a molecular mass of 45 kDa. The specific activities of r-HGL were found to be similar to that of the native enzyme when tested on various triacylglycerol (TG) substrates. The 3-D structure of r-HGL was the first solved within the mammalian acid lipase family. This globular enzyme (379 residues) shows a new feature, different from the other known lipases structures, which consists of a core domain having the alpha/beta hydrolase fold and a cap domain including a putative 'lid' of 30 residues covering the active site of the lipase (closed conformation). HPL is the major lipolytic enzyme involved in the digestion of dietary TG. HPL is a 50 kDa glycoprotein which is directly secreted as an active enzyme. HPL was the first mammalian lipase to be solved structurally, and it revealed the presence of two structural domains: a large N-terminal domain (residues 1-336) and a smaller C-terminal domain (residues 337-449). The large N-terminal domain belongs to the alpha/beta hydrolase fold and contains the active site. A surface loop called the lid domain (C237-C261) covers the active site in the closed conformation of the lipase. The 3-D structure of the lipase-procolipase complex illustrates how the procolipase might anchor the lipase at the interface in the presence of bile salts: procolipase binds to the C-terminal domain of HPL and exposes the hydrophobic tips of its fingers at the opposite site of its lipase-binding domain. These hydrophobic tips help to bring N-terminal domain into close conformation with the interface where the opening of the lid domain probably occurs. As a result of all these conformational changes, the open lid and the extremities of the procolipase form an impressive continuous hydrophobic plateau, extending over more than 50 A. This surface might able to interact strongly with a lipid-water interface. The biochemical, histochemical and clinical studies as well as the 3-D structures obtained will be a great help for a better understanding of the structure-function relationships of digestive lipases." @default.
• W2017025152 created "2016-06-24" @default.
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• W2017025152 date "2000-11-01" @default.
• W2017025152 modified "2023-10-17" @default.
• W2017025152 title "Digestive lipases: From three-dimensional structure to physiology" @default.
• W2017025152 cites W1481512261 @default.
• W2017025152 cites W1485044764 @default.
• W2017025152 cites W1503820853 @default.
• W2017025152 cites W1510971505 @default.
• W2017025152 cites W1514454969 @default.
• W2017025152 cites W1564777466 @default.
• W2017025152 cites W1597793844 @default.
• W2017025152 cites W1677547851 @default.
• W2017025152 cites W1781120710 @default.
• W2017025152 cites W1905174418 @default.
• W2017025152 cites W1918910070 @default.
• W2017025152 cites W1939955036 @default.
• W2017025152 cites W1969172212 @default.
• W2017025152 cites W1969818697 @default.
• W2017025152 cites W1970683900 @default.
• W2017025152 cites W1973678224 @default.
• W2017025152 cites W1975037895 @default.
• W2017025152 cites W1975138491 @default.
• W2017025152 cites W1976951969 @default.
• W2017025152 cites W1980525384 @default.
• W2017025152 cites W1983547248 @default.
• W2017025152 cites W1984198180 @default.
• W2017025152 cites W1988107392 @default.
• W2017025152 cites W1990488429 @default.
• W2017025152 cites W1990565924 @default.
• W2017025152 cites W1991623679 @default.
• W2017025152 cites W1994317940 @default.
• W2017025152 cites W1999688246 @default.
• W2017025152 cites W2002439130 @default.
• W2017025152 cites W2003735595 @default.
• W2017025152 cites W2004428295 @default.
• W2017025152 cites W2012176370 @default.
• W2017025152 cites W2012324886 @default.
• W2017025152 cites W2013934046 @default.
• W2017025152 cites W2016503677 @default.
• W2017025152 cites W2025566860 @default.
• W2017025152 cites W2025957822 @default.
• W2017025152 cites W2026793340 @default.
• W2017025152 cites W2027968658 @default.
• W2017025152 cites W2028416390 @default.
• W2017025152 cites W2029372575 @default.
• W2017025152 cites W2032976059 @default.
• W2017025152 cites W2036006275 @default.
• W2017025152 cites W2036414218 @default.
• W2017025152 cites W2045471153 @default.
• W2017025152 cites W2046429206 @default.
• W2017025152 cites W2048843295 @default.
• W2017025152 cites W2060576691 @default.
• W2017025152 cites W2064184667 @default.
• W2017025152 cites W2067975797 @default.
• W2017025152 cites W2074000366 @default.
• W2017025152 cites W2075167383 @default.
• W2017025152 cites W2076104132 @default.
• W2017025152 cites W2077418114 @default.
• W2017025152 cites W2078342497 @default.
• W2017025152 cites W2079186398 @default.
• W2017025152 cites W2082015820 @default.
• W2017025152 cites W2091223506 @default.
• W2017025152 cites W2093067488 @default.
• W2017025152 cites W2095740730 @default.
• W2017025152 cites W2100841562 @default.
• W2017025152 cites W2101480595 @default.
• W2017025152 cites W2102239141 @default.
• W2017025152 cites W2110202222 @default.
• W2017025152 cites W2112636022 @default.
• W2017025152 cites W2117794964 @default.
• W2017025152 cites W2127314425 @default.
• W2017025152 cites W2130153207 @default.
• W2017025152 cites W2138999678 @default.
• W2017025152 cites W2149523277 @default.
• W2017025152 cites W2154613262 @default.
• W2017025152 cites W2159102900 @default.
• W2017025152 cites W2162502068 @default.
• W2017025152 cites W2167217484 @default.
• W2017025152 cites W2182582855 @default.
• W2017025152 cites W2187950837 @default.
• W2017025152 cites W2412552238 @default.
• W2017025152 cites W2414307244 @default.
• W2017025152 cites W2416878388 @default.
• W2017025152 cites W2469450195 @default.
• W2017025152 cites W48920773 @default.
• W2017025152 cites W625010781 @default.
• W2017025152 cites W644142250 @default.
• W2017025152 cites W94077231 @default.

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