About: Cutinase from Fusarium solani pisi hydrolyzing triglyceride analogues. Effect of acyl chain length and position in the substrate molecule on activity and enantioselectivity

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About: Cutinase from Fusarium solani pisi hydrolyzing triglyceride analogues. Effect of acyl chain length and position in the substrate molecule on activity and enantioselectivity Goto Sponge NotDistinct Permalink

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scientific article published on 01 May 1995

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в травні 1995 (uk) artículu científicu espublizáu en mayu de 1995 (ast) scientific article published on 01 May 1995 (en) im Mai 1995 veröffentlicher wissenschaftlicher Artikel (de)
publication date	wds:Q72251581-E8AD3F3C-56B5-4200-9C3E-888791F2F114
publication date	1995-05-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q72251581-48C188E1-4766-4796-904E-9571AB11F013
language of work or name	English
author name string	wds:Q72251581-66A9679A-999F-4685-906B-3C11C2C49F06 wds:Q72251581-6C2A255D-DD74-412A-A93E-FE34594A6D19 wds:Q72251581-724F862A-6284-48F5-8CBC-059F99E35209 wds:Q72251581-A0F604DA-235D-4C39-A166-2BDC3B77BF4C wds:Q72251581-C4EC420C-E047-4512-8E64-210682BAD639 wds:Q72251581-D94CED4B-29C0-43FB-988E-3958D658F10B wds:Q72251581-DD73A979-0C8B-430B-B4EA-B32D0F18EB39 wds:Q72251581-EC9EB005-81EB-49CA-966B-DFE948D4C5EE
author name string	H M Verheij M R Egmond G H de Haas J de Vlieg R C Cox H T van der Hijden M L Mannesse B C Koops
rdfs:label	Cutinase from Fusarium solani pisi hydrolyzing triglyceride analogues. Effect of acyl chain length and position in the substrate molecule on activity and enantioselectivity (en) Cutinase from Fusarium solani pisi hydrolyzing triglyceride analogues. Effect of acyl chain length and position in the substrate molecule on activity and enantioselectivity (nl)
skos:prefLabel	Cutinase from Fusarium solani pisi hydrolyzing triglyceride analogues. Effect of acyl chain length and position in the substrate molecule on activity and enantioselectivity (en) Cutinase from Fusarium solani pisi hydrolyzing triglyceride analogues. Effect of acyl chain length and position in the substrate molecule on activity and enantioselectivity (nl)
name	Cutinase from Fusarium solani pisi hydrolyzing triglyceride analogues. Effect of acyl chain length and position in the substrate molecule on activity and enantioselectivity (en) Cutinase from Fusarium solani pisi hydrolyzing triglyceride analogues. Effect of acyl chain length and position in the substrate molecule on activity and enantioselectivity (nl)
title	wds:Q72251581-DB7956FB-D35E-469E-AF76-619CFB98F78E
title	Cutinase from Fusarium solani pisi hydrolyzing triglyceride analogues. Effect of acyl chain length and position in the substrate molecule on activity and enantioselectivity (en)
page(s)	wds:Q72251581-6A4160EF-0989-4E5F-B8AA-8DA53EA3B702
page(s)	6400-6407
instance of	wds:Q72251581-BAC44A25-C8E5-4FB1-A97A-CB3BBB9EE5D0
instance of	scholarly article
main subject	wds:Q72251581-05ED7B97-9890-40AF-8E73-38BCEA6D2D76 wds:Q72251581-29083E0D-E786-4CB8-89FF-D0ECB4733CC7
main subject	Fusarium solani enantioselectivity
PubMed ID	wds:Q72251581-C7973E2A-EDD0-4A83-85E7-363DC98686EF
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/7756270
PubMed ID	7756270
published in	wds:Q72251581-E2F370EC-AA52-4A66-BDDC-DEEA9B3ECD0D
published in	Biochemistry
issue	wds:Q72251581-FFD8F8F2-E093-4DE3-BF3A-140A8302B50D
volume	wds:Q72251581-CDE87430-9786-4A37-9EA4-8F928E99205C
issue	19
volume	34
DOI	wds:Q72251581-19A0AF5A-CF8D-4B96-A2F6-09D6F2D6BCF0
DOI	http://dx.doi.org/10.1021/BI00019A020
DOI	10.1021/BI00019A020
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q72251581
is cites work of	Impact of structural information on understanding lipolytic function Structure as basis for understanding interfacial properties of lipases How do lipases and esterases work: the electrostatic contribution Identification of residues involved in substrate specificity and cytotoxicity of two closely related cutinases from Mycobacterium tuberculosis Lipase protein engineering Mycobacterium tuberculosis lipolytic enzymes as potential biomarkers for the diagnosis of active tuberculosis Fusarium solani pisi cutinase Crystal structure of cutinase covalently inhibited by a triglyceride analogue Anatomy of lipase binding sites: the scissile fatty acid binding site Cutinases: properties and industrial applications Enantioselective properties of Fusarium solani pisi cutinase on transesterification of acyclic diols: activity and stability evaluation Structure-activity of cutinase, a small lipolytic enzyme Surface and electrostatics of cutinases Effect of the immobilization support on the hydrolytic activity of a cutinase from Fusarium solani pisi Pilot-scale extraction of an intracellular recombinant cutinase from E. coli cell homogenate using a thermoseparating aqueous two-phase system Cutinase stability in AOT reversed micelles: system optimization using the factorial design methodology Partitioning of peptide-tagged proteins in aqueous two-phase systems using hydrophobically modified micelle-forming thermoseparating polymer Cutinase binding and activity at the triolein-water interface monitored by oil drop tensiometry Rat hormone sensitive lipase inhibition by cyclipostins and their analogs. Substitutions of surface amino acid residues of cutinase probed by aqueous two-phase partitioning. Purification of recombinant cutinase by extraction in an aqueous two-phase system facilitated by a fatty acid substrate Novel microbial lipases: catalytic activity in reactions in organic media Cutinase-peptide fusions in thermoseparating aqueous two-phase systems. Prediction of partitioning and enhanced tag efficiency by detergent addition Tryptophan-tagged cutinase studied by steady state fluorescence for understanding of tag interactions in aqueous two-phase systems.
is cites work of	wds:Q37388727-3C0B1682-787A-4461-9F3E-9A66C769E269 wds:Q41778475-B2354058-F925-498D-A464-CD753B231E26 wds:Q44483149-EC843F18-D5AA-4CE8-827D-65D4883D6A13 wds:Q73902403-A296C4A9-9252-496D-AA6F-B5EE9C3D1C59 wds:Q28142279-D540FA67-8338-46B7-9AAB-87AFCD3F04EE wds:Q28744646-683BC9EC-653B-40AE-BFF0-25AA0F61F62E wds:Q77682974-D72EA403-3EE5-49C3-8F79-60522DDE7540 wds:Q41649776-29E7BBD4-2582-4727-AEF1-7CF17167E2B6 wds:Q43602006-D46618F4-CD5B-40BA-BCA8-D0009BE9C825 wds:Q31878227-0C0CAAE8-5224-4F25-991C-8CDD34B13514 wds:Q44225062-F46E22BA-DDED-4CE4-A784-D83A95414F18 wds:Q61466091-9F12DACA-C5DA-42EE-84FD-79711B9D003D wds:Q43902321-59679B2D-E546-4F94-9286-7D4C9C1073B3 wds:Q61466083-19E3D95D-1EE8-4204-AC93-FB3BD68B18D7 wds:Q56954024-A84D7717-8DA7-431A-A849-C84D4CD049A7 wds:Q34812287-96285C74-8D20-4A00-AB00-221FCE0F4030 wds:Q73414121-9D172D4D-5355-4C38-A919-DB077ABFB9FB wds:Q33778035-6B47E2DC-DCE3-40FE-9D8A-518F40CF772D wds:Q34447417-2A804FDC-917A-40AF-932D-AA1AB41F6824 wds:Q34094681-F39CBF30-7DE9-478D-AD59-3AC63D5A3989 wds:Q41987575-4F62EB79-D39B-4A54-8FBF-7DD623718FAD

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