Document Detail

Molecular dynamics simulations of human and dog gastric lipases: insights into domain movements.
MedLine Citation:
PMID:  20965171     Owner:  NLM     Status:  MEDLINE    
Mammalian gastric lipases are stable and active under acidic conditions and also in the duodenal lumen. There has been considerable interest in acid stable lipases owing to their potential application in the treatment of pancreatic exocrine insufficiency. In order to gain insights into the domain movements of these enzymes, molecular dynamics simulations of human gastric lipase was performed at an acidic pH and under neutral conditions. For comparative studies, simulation of dog gastric lipase was also performed at an acidic pH. Analyses show, that in addition to the lid region, there is another region of high mobility in these lipases. The potential role of this novel region is discussed.
Anitha Selvan; Chandrabhan Seniya; Srinivas Niranj Chandrasekaran; Nithyanand Siddharth; Sharmila Anishetty; Gautam Pennathur
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2010-10-20
Journal Detail:
Title:  FEBS letters     Volume:  584     ISSN:  1873-3468     ISO Abbreviation:  FEBS Lett.     Publication Date:  2010 Nov 
Date Detail:
Created Date:  2010-11-15     Completed Date:  2010-12-20     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0155157     Medline TA:  FEBS Lett     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  4599-605     Citation Subset:  IM    
Copyright Information:
Copyright © 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Centre for Biotechnology, Anna University Chennai, Chennai 600 025, India.
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MeSH Terms
Amino Acid Sequence
Hydrogen-Ion Concentration
Lipase / chemistry*,  metabolism*
Molecular Dynamics Simulation*
Molecular Sequence Data
Protein Structure, Tertiary
Sequence Alignment
Sequence Analysis, DNA
Reg. No./Substance:
EC; EC lipase, human

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