INHIBITION OF THE LIPASE FROM PSEUDOMONASSPEC. ATCC 21808 BY DIETHYL p-NITROPHENYL PHOSPHATE. HINTS FOR ONE BURIED ACTIVE SITE FOR LIPOLYTIC AND ESTEROLYTIC ACTIVITY
dc.contributor.author | Kordel, Marianne | |
dc.contributor.author | Schmid, Rolf D. | |
dc.date.accessioned | 2024-03-27T10:20:48Z | |
dc.date.available | 2024-03-27T10:20:48Z | |
dc.date.issued | 1991 | |
dc.date.submitted | 2024-03-27 | |
dc.identifier.citation | Lipases : structure, mechanism and genetic engineering, 385 - 387 | en_US |
dc.identifier.isbn | 156081165X | |
dc.identifier.isbn | 3527283323 | |
dc.identifier.issn | 0930-4320 | |
dc.identifier.uri | http://hdl.handle.net/10033/623745 | |
dc.description.abstract | Lipases have been shown to beserine-hydrolasessince they are inhibited by serine active reagents such as phenylmethylsulfonylfluoride (PMSF), boronic acids and organophosphates [1,2,3]. Furthermore, they are surface active enzymes,i.e. they are activated by binding to interfaces [4] comprising their natural substrates, the micelles of long chain fatty acid triglycerides. It has long been postulated that lipases undergo a conformational changein this activation process. Recently it became obvious from x-raystudies [1,5] that the active site is inaccessible to voluminoussubstrates unless a conformational change occurs sincethe active site is buried undera lid formed by a long peptide loop. The lipase from human pancreas presumably hydrolysessoluble substrateslike p-nitrophenyl acetate (pNPA)at a different site [5]. For the porcine pancreatic lipase it was reported that the C-terminal peptide fragment (336-449) shows the sameactivity towards pNPA as the complete enzyme but no activity towards triacylglycerols [6]. Whereas,in the triglyceride hydrolysis Ser-152 is involved [R. Verger, pers. communication]. Ourinhibition studies suggest that only one active site for both types of substrates exists for the lipase from Pseudomonas spec. ATCC 21808 and thatthis site is buried. | en_US |
dc.language.iso | en | en_US |
dc.publisher | GBF Gesellschaft für Biotechnologische Forschung mbH, Braunschweig | en_US |
dc.relation.ispartofseries | GBF monographs ; Volume 16 | en_US |
dc.rights | Attribution-NonCommercial-ShareAlike 4.0 International | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-sa/4.0/ | * |
dc.title | INHIBITION OF THE LIPASE FROM PSEUDOMONASSPEC. ATCC 21808 BY DIETHYL p-NITROPHENYL PHOSPHATE. HINTS FOR ONE BURIED ACTIVE SITE FOR LIPOLYTIC AND ESTEROLYTIC ACTIVITY | en_US |
dc.type | Book chapter | en_US |
dc.type | conference paper | en_US |
dc.contributor.department | GBF, Gesellschaft für Biotechnologische Forschung mbH, Dept. of Enzyme Technology, Mascheroder Weg 1, D-3300 Braunschweig | en_US |
dc.identifier.journal | Lipases : structure, mechanism and genetic engineering, 1991 | en_US |
refterms.dateFOA | 2024-03-27T10:20:49Z |
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