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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
24
|
| pubmed:dateCreated |
1990-3-14
|
| pubmed:abstractText |
The Staphylococcus hyicus lipase gene has been cloned and expressed in Staphylococcus carnosus. From the latter organism the enzyme was secreted into the medium as a protein with an apparent molecular mass of 86 kDa. This protein was purified, and the amino-terminal sequence showed that the primary gene product was indeed cleaved at the proposed signal peptide cleavage site. The protein was purified from large-scale preparations after tryptic digestion. This limited proteolysis reduced the molecular mass to 46 kDa and increased the specific activity about 3-fold. Although the enzyme had a low specific activity in the absence of divalent cations, the activity increased about 40-fold in the presence of Sr2+ or Ca2+ ions. The purified lipase has a broad substrate specificity. The acyl chains were removed from the primary and secondary positions of natural neutral glycerides and from a variety of synthetic glyceride analogues. Thus triglycerides were fully hydrolyzed to free fatty acid and glycerol. The enzyme hydrolyzed naturally occurring phosphatidylcholines, their synthetic short-chain analogues, and lysophospholipids to free fatty acids and water-soluble products. The enzyme had a 2-fold higher activity on micelles of short-chain D-lecithins than on micelles composed of the L-isomers. Thus the enzyme from S. hyicus has lipase activity and also high phospholipase A and lysophospholipase activity.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Lipase,
http://linkedlifedata.com/resource/pubmed/chemical/Pancreatin,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipids,
http://linkedlifedata.com/resource/pubmed/chemical/Strontium,
http://linkedlifedata.com/resource/pubmed/chemical/Triglycerides,
http://linkedlifedata.com/resource/pubmed/chemical/tributyrin
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Nov
|
| pubmed:issn |
0006-2960
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
28
|
| pubmed:volume |
28
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
9278-85
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:2611229-Amino Acid Sequence,
pubmed-meshheading:2611229-Animals,
pubmed-meshheading:2611229-Calcium,
pubmed-meshheading:2611229-Cloning, Molecular,
pubmed-meshheading:2611229-Humans,
pubmed-meshheading:2611229-Hydrogen-Ion Concentration,
pubmed-meshheading:2611229-Kinetics,
pubmed-meshheading:2611229-Lipase,
pubmed-meshheading:2611229-Lipid Metabolism,
pubmed-meshheading:2611229-Molecular Sequence Data,
pubmed-meshheading:2611229-Molecular Structure,
pubmed-meshheading:2611229-Pancreatin,
pubmed-meshheading:2611229-Phospholipids,
pubmed-meshheading:2611229-Sequence Homology, Nucleic Acid,
pubmed-meshheading:2611229-Staphylococcus,
pubmed-meshheading:2611229-Strontium,
pubmed-meshheading:2611229-Substrate Specificity,
pubmed-meshheading:2611229-Swine,
pubmed-meshheading:2611229-Triglycerides
|
| pubmed:year |
1989
|
| pubmed:articleTitle |
Purification and substrate specificity of Staphylococcus hyicus lipase.
|
| pubmed:affiliation |
Department of Biochemistry, State University of Utrecht, The Netherlands.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|