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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11
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pubmed:dateCreated |
1997-2-11
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pubmed:databankReference |
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pubmed:abstractText |
The guinea pig pancreatic lipase-related protein 2 (GPLRP2) differs from classical pancreatic lipases in that it displays both lipase and phospholipase A1 activities; classical pancreatic lipases have no phospholipase activity. The sequence of GPLRP2 is 63 % identical to that of human pancreatic lipase (HPL), but the so-called lid domain, is much reduced in GPLRP2. A phospholipase A1 from hornet venom (Dolml PLA1) is very similar to HPL and GPLRP2 but is devoid of lipase activity; Dolml PLA1 also contains a reduced lid domain and lacks a region termed the beta9 loop, which is located in the vicinity of the HPL and GPLRP2 active sites. The structure determination of a chimera of GPLRP2 and HPL and domain building of Dolml PLA1 were undertaken to gain a better understanding of the structural parameters responsible for the differences in lipase versus phospholipase activity among these structurally related enzymes.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0969-2126
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
4
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1363-74
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:8939760-Amino Acid Sequence,
pubmed-meshheading:8939760-Animals,
pubmed-meshheading:8939760-Binding Sites,
pubmed-meshheading:8939760-Computer Simulation,
pubmed-meshheading:8939760-Crystallography, X-Ray,
pubmed-meshheading:8939760-Enzyme Activation,
pubmed-meshheading:8939760-Guinea Pigs,
pubmed-meshheading:8939760-Humans,
pubmed-meshheading:8939760-Lipase,
pubmed-meshheading:8939760-Models, Molecular,
pubmed-meshheading:8939760-Molecular Sequence Data,
pubmed-meshheading:8939760-Mutation,
pubmed-meshheading:8939760-Pancreas,
pubmed-meshheading:8939760-Phospholipases A,
pubmed-meshheading:8939760-Phospholipases A1,
pubmed-meshheading:8939760-Phospholipids,
pubmed-meshheading:8939760-Protein Conformation,
pubmed-meshheading:8939760-Recombinant Fusion Proteins,
pubmed-meshheading:8939760-Reproducibility of Results,
pubmed-meshheading:8939760-Sequence Homology, Amino Acid,
pubmed-meshheading:8939760-Wasps,
pubmed-meshheading:8939760-Water
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pubmed:year |
1996
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pubmed:articleTitle |
A pancreatic lipase with a phospholipase A1 activity: crystal structure of a chimeric pancreatic lipase-related protein 2 from guinea pig.
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pubmed:affiliation |
Architecture et Fonction des Macromolécules Biologiques, CNRS-IFR1 UPR9039, 31 chemin Joseph Aiguier, 13402 Marseille cedex 20, France. cambilau@afmb.cnrs-mrs.fr
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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