The Enzymatic Activity of Lipases Correlates with Polarity-Induced Conformational Changes: A Trp-Induced Quenching Fluorescence Study-Reference-Cited by-同舟云学术

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The Enzymatic Activity of Lipases Correlates with Polarity-Induced Conformational Changes: A Trp-Induced Quenching Fluorescence Study

Published:2015-07-01 Issue:27 Volume:54 Page:4186-4196
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Skjold-Jørgensen Jakob¹²,Bhatia Vikram K.²,Vind Jesper²,Svendsen Allan²,Bjerrum Morten J.¹,Farrens David³

Affiliation:

1. Department of Chemistry, University of Copenhagen, Universitetsparken 5, DK 2100 Copenhagen, Denmark

2. Novozymes A/S, Brudelysvej 35, DK 2880 Bagværd, Denmark

3. Biochemistry & Molecular Biology, Oregon Health and Science University, 3181 Southwest Jackson Park Road, Portland, Oregon 97239, United States

Funder

National Center for Research Resources

Styrelsen for Forskning og Innovation

National Eye Institute

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.5b00328

Reference53 articles.

1. A serine protease triad forms the catalytic centre of a triacylglycerol lipase

2. A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex

3. Conformational lability of lipases observed in the absence of an oil-water interface: crystallographic studies of enzymes from the fungi Humicola lanuginosa and Rhizopus delemar.

4. Probing the nature of substrate binding in Humicola lanuginosa lipase through X-ray crystallography and intuitive modelling

5. Action de la lipase pancréatique sur les esters en émulsion

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