The expanding superfamily of phospholipase A(2) enzymes: classification and characterization.
By David A. Six, Edward A. Dennis. Biochimica et Biophysica Acta, 2000
1,395 citations recorded by the source corpus.
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.
Subfields: Cell Biology, Genetics, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/af35173269dc5a90b75cc07f9c9e0fed434fabd0
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Cell Biology
In Genetics
In Molecular Biology
Citations in the corpus
- Biology and Biochemistry of Plant Phospholipases (2011, background): “A well-conserved Histidine/Aspartate dyad has been identified in the catalytic site motif, which may function as a base for the deprotonation of ester carbonyl carbons of the substrate while the aspartate interacts with a Ca2+ cofactor (Six and Dennis, 2000).”
- Eicosanoid actions in insect cellular immune functions (2006, background): “Now over a dozen PLA 2 groups are recognized (Six & Dennis, 2000), many of which are entirely unrelated to eicosanoid biosynthesis.”
- Maximum Entropy Reconstructions of Dynamic Signaling Networks from Quantitative Proteomics Data (2009, background): “Annexin A2 is a phospholipase family member and has numerous functions including endocytosis and the generation of lipid secondary messengers[26].”
- How human neutrophils kill and degrade microbes: an integrated view (2007, background): “First, GpIIA-PLA2 is the most cationic of the secretory phospholipases with a net charge of þ16 (186).”