| The expanding superfamily of phospholipase A(2) enzymes: classification and characterization. | |
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MedLine Citation:
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PMID: 11080672 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The phospholipase A(2) (PLA(2)) superfamily consists of a broad range of enzymes defined by their ability to catalyze the hydrolysis of the middle (sn-2) ester bond of substrate phospholipids. The hydrolysis products of this reaction, free fatty acid and lysophospholipid, have many important downstream roles, and are derived from the activity of a diverse and growing superfamily of PLA(2) enzymes. This review updates the classification of the various PLA(2)'s now described in the literature. Four criteria have been employed to classify these proteins into one of the 11 Groups (I-XI) of PLA(2)'s. First, the enzyme must catalyze the hydrolysis of the sn-2 ester bond of a natural phospholipid substrate, such as long fatty acid chain phospholipids, platelet activating factor, or short fatty acid chain oxidized phospholipids. Second, the complete amino acid sequence of the mature protein must be known. Third, each PLA(2) Group should include all of those enzymes that have readily identifiable sequence homology. If more than one homologous PLA(2) gene exists within a species, then each paralog should be assigned a Subgroup letter, as in the case of Groups IVA, IVB, and IVC PLA(2). Homologs from different species should be classified within the same Subgroup wherever such assignments are possible as is the case with zebra fish and human Group IVA PLA(2) orthologs. The current classification scheme does allow for historical exceptions of the highly homologous Groups I, II, V, and X PLA(2)'s. Fourth, catalytically active splice variants of the same gene are classified as the same Group and Subgroup, but distinguished using Arabic numbers, such as for Group VIA-1 PLA(2) and VIA-2 PLA(2)'s. These four criteria have led to the expansion or realignment of Groups VI, VII and VIII, as well as the addition of Group XI PLA(2) from plants. |
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Authors:
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D A Six; E A Dennis |
Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.; Review |
Journal Detail:
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Title: Biochimica et biophysica acta Volume: 1488 ISSN: 0006-3002 ISO Abbreviation: Biochim. Biophys. Acta Publication Date: 2000 Oct |
Date Detail:
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Created Date: 2000-12-15 Completed Date: 2001-01-11 Revised Date: 2007-11-14 |
Medline Journal Info:
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Nlm Unique ID: 0217513 Medline TA: Biochim Biophys Acta Country: NETHERLANDS |
Other Details:
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Languages: eng Pagination: 1-19 Citation Subset: IM |
Affiliation:
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Department of Chemistry and Biochemistry, MC 0601, Revelle College and School of Medicine, University of California, San Diego, La Jolla, CA 92093-0601, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals Binding Sites Cytosol / enzymology Histidine / chemistry Humans Molecular Sequence Data Phospholipases A / chemistry, classification*, genetics Phospholipids / chemistry Sequence Homology Serine / chemistry Species Specificity |
| Grant Support | |
ID/Acronym/Agency:
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GM07240/GM/NIGMS NIH HHS; GM20501/GM/NIGMS NIH HHS; HD26171/HD/NICHD NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Phospholipids; 56-45-1/Serine; 71-00-1/Histidine; EC 3.1.1.-/Phospholipases A |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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