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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
8
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pubmed:dateCreated |
1995-3-31
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pubmed:abstractText |
We describe the purification and first biochemical characterization of an enzymatic activity in venom from the marine snail Conus magus. This enzyme, named conodipine-M, is a novel phospholipase A2 with a molecular mass of 13.6 kDa and is comprised of two polypeptide chains linked by one or more disulfide bonds. The amino acid sequence of conodipine-M shows little if any homology to other previously sequenced phospholipase A2 enzymes (PLA2s). Conodipine-M thus represents a new group of PLA2s. This is remarkable, since conodipine-M displays a number of properties that are similar to those of previously characterized 14-kDa PLA2s. The enzyme shows little, if any, phospholipase A1, diacyglycerol lipase, triacylglycerol lipase, or lysophospholipase activities. Conodipine-M hydrolyzes the sn-2 ester of various preparations of phospholipid only in the presence of calcium and with specific activities that are comparable to those of well known 14-kDa snake venom and pancreatic PLA2s. The Conus enzyme binds tightly to vesicles of the negatively charged phospholipid 1,2-dimyristoyl-sn-glycero-3-phosphomethanol and catalyzes the hydrolysis of this substrate in a processive fashion. Conodipine-M does not significantly discriminate against phospholipids with unsaturated versus saturated fatty acids at the sn-2 position or with different polar head groups. Linoleoyl amide and a phospholipid analog containing an alkylphosphono group at the sn-2 position are potent inhibitors of conodipine-M. We suggest that the functional resemblance of conodipine-M to other PLA2s might be explained by the utilization of similar catalytic residues.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Mollusk Venoms,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipases A,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipases A1,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipases A2
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
24
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pubmed:volume |
270
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3518-26
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:7876086-Amino Acid Sequence,
pubmed-meshheading:7876086-Animals,
pubmed-meshheading:7876086-Calcium,
pubmed-meshheading:7876086-Molecular Sequence Data,
pubmed-meshheading:7876086-Mollusk Venoms,
pubmed-meshheading:7876086-Phospholipases A,
pubmed-meshheading:7876086-Phospholipases A1,
pubmed-meshheading:7876086-Phospholipases A2,
pubmed-meshheading:7876086-Phospholipases A2, Secretory,
pubmed-meshheading:7876086-Sequence Homology, Amino Acid,
pubmed-meshheading:7876086-Snails,
pubmed-meshheading:7876086-Substrate Specificity
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pubmed:year |
1995
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pubmed:articleTitle |
Conodipine-M, a novel phospholipase A2 isolated from the venom of the marine snail Conus magus.
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pubmed:affiliation |
Department of Psychiatry, University of Utah, Salt Lake City 84112.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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