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metabolism
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intracellular phospholipase A1 and acyltransferase are involved in Caenorhabditis elegans stem cell divisions
evolution
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mechanisms of activation of the ExoU family of PLAs may be evolutionarily conserved
evolution
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evolutionary relationship and phylogenetics of isozymes Ves a 1.01-1.04, overview
evolution
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the enzyme is a member of the pancreatic lipase family
malfunction
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knockdown of intracellular PLA1gamma expression by RNAi does not affect the anterograde transport of ts045 vesicular stomatitis virus protein (VSVGts045) but dramatically delays two types of Golgi-to-endoplasmic reticulum retrograde membrane transport, i.e., transfer of the Golgi membrane into the endoplasmic reticulum in the presence of brefeldin A and delivery of cholera toxin B subunit from the Golgi complex to the endoplasmic reticulum. Knockdown of intracellular PLA1gamma does not impair coat protein complex I- and Rab6-dependent retrograde transports represented by ERGIC-53 recycling and endoplasmic reticulum delivery of Shiga toxin, respectively
malfunction
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Because orientation of seam cell division is randomized relative to the A-P axis in ipla-1 mutants, ipla-1 mutants exhibit aberrant orientation of seam cell divisions. Acl-8 acl-9 acl-10 triple mutations also cause misorientation of seam cell divisions similar to that observed in ipla-1 mutants
malfunction
in enzyme mutants, in the absence of transport to the Golgi, rhodopsin 1 is aberrantly glycosylated and is mislocalized. These defects lead to decreased levels of the protein and decreased sensitivity of the photoreceptors to light. Several GPCRs, including other rhodopsins and Bride of sevenless, are similarly affected, phenotypes, overview
malfunction
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phosphatidic acid-preferring phospholipase A1 depletion causes mitochondrial elongation, leading to a loss of motility
malfunction
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phosphatidic acid-preferring phospholipase A1 depletion causes mitochondrial elongation. Enzyme knock-out mice have a defect in sperm formation, spermatozoa from PA-PLA1-/- mice possess an annulus that is not attached to the mitochondrial sheath, whereas that in control mice is attached. In enzyme-deficient sperm, the mitochondrial structure is disorganized, and an abnormal gap structure exists between the middle and principal pieces.A flagellum is bent at that position, leading to a loss of motility
physiological function
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H-Rev107 functions principally as a Ca2+-independent PLA1/2 with a higher PLA1 activity. Transient expression of H-Rev107 in COS-7 cells does not appear to influence cell proliferation
physiological function
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H-Rev107 functions principally as a Ca2+-independent PLA1/2 with a higher PLA1 activity. Transient expression of H-Rev107 in COS-7 cells does not appear to influence cell proliferation
physiological function
H-Rev107 functions principally as a Ca2+-independent PLA1/2 with a higher PLA1 activity. Transient expression of H-Rev107 in COS-7 cells does not appear to influence cell proliferation
physiological function
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is capable for activation of human basophils, relevance of Ves v 1 in hymenoptera venom allergy
physiological function
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mediates a specific retrograde membrane transport pathway between the endoplasmic reticulum and the Golgi complex
physiological function
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simultaneous purification of plasmalogens and sphingomyelin with PLA1 in human erythrocytes. Relative concentration of the plasmalogens after treatment with PLA1 is 92% of phospholipids in the supernatant fraction, and that of sphingomyelin is 97.7% in the precipitate fraction
physiological function
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intracellular phospholipase A1 and acyltransferase, which are involved in Caenorhabditis elegans stem cell divisions, determine the sn-1 fatty acyl chain of phosphatidylinositol
physiological function
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PLA1 is the major allergen for humans in the wasp venom
physiological function
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the phospholipase A1 activity of lysophospholipase A-I links platelet activation to LPA production during blood coagulation
physiological function
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classical pancreatic lipase may fulfill in some cases additional biological functions as a phospholipase A1, PLA1, enzyme, compensating pancreatic lipase-related protein 2, PLRP2, deficiency in the digestive tract
physiological function
lysophospholipase activity in live Tryypanosoma cruzi parasites contributes to self protection against toxic compounds generated by phospholipase A1 activity
physiological function
the cytosolic enzyme is necessary for transit of selective transmembrane receptor cargo by the COPII coat for anterograde trafficking in Drosophila melanogaster. The enzme interacts with the coat protein II (COPII), the COPII coated vesicular system transports newly synthesized secretory and membrane proteins from the endoplasmic reticulum to the Golgi complex. The enzyme is required for the transport of rhodopsin 1, an N-glycosylated G protein-coupled receptor, from the endoplasmic reticulum to the Golgi complex, but the active site of PAPLA1 is not necessary for Rh1 maturation. The enzyme acts downstream of the rhodopsin 1 chaperone NinaA and upstream of the Golgi-resident protein dMPPE
physiological function
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the phosphatidic acid-preferring phospholipase A1 regulates mitochondrial dynamics
physiological function
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the phosphatidic acid-preferring phospholipase A1 regulates mitochondrial dynamics. When ectopically expressed in HeLa cells, it induces mitochondrial fragmentation, whereas its depletion causes mitochondrial elongation. The effects of the enzyme on mitochondrial morphology appear to counteract those of MitoPLD, a mitochondrion-localized phospholipase D that produces phosphatidic acid from cardiolipin
physiological function
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the T4SS-translocated effector protein VipD exhibits phospholipase A1 activity that is activated only upon binding to endosomal Rab5 or Rab22, VipD protects Legionella pneumophila from endosomal fusion, that way, the pathogen Legionella pneumophila bypasses the microbicidal endosomal compartment of mammalian macrophages. By catalyzing phosphatidylinositol 3-phosphate depletion in a Rab5-dependent manner, VipD alters the protein composition of endosomes thereby blocking fusion with Legionella-containing vacuoles, implicated molecular mechanism, overview. The enzyme VipD alters the endosomal protein and lipid composition
physiological function
by lowering the phosphatidylethanolamine content of the cell envelope, BveA increases the resistance of Brucella melitensis to polymyxin B. BveA is required for survival and replication of Brucella melitensis in macrophages and for persistent infection in mice
physiological function
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deletion of phospholipase DDL1 leads to respiratory growth defects. Introduction of COQ8, COQ9, or COQ5, which are involved in coenzyme Q synthesis, using a multicopy vector suppresses the respiratory growth defect of the DDL1 deletion mutant
physiological function
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the C-terminal region regulates the binding of PLA1 to phosphatidylcholine. The alpha9 helix of C-terminal region in PLA1 may not only control the opening of lid but also serve as a membrane anchor that assists in binding to phosphatidylcholine
physiological function
Brucella melitensis bv. 1 ATCC 23456
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by lowering the phosphatidylethanolamine content of the cell envelope, BveA increases the resistance of Brucella melitensis to polymyxin B. BveA is required for survival and replication of Brucella melitensis in macrophages and for persistent infection in mice
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additional information
residue Ser11 is essential for the catalytic function of the enzyme, the active site may include residues Ser216 and His218
additional information
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residue Ser11 is essential for the catalytic function of the enzyme, the active site may include residues Ser216 and His218
additional information
the enzyme's active site is composed of a Ser-His dyad (Ser11 and His218), whereby stabilization of the imidazole is provided by the main-chain carbonyl oxygen of Ser216, a common variation of the catalytic triad in many serine hydrolases, where this carbonyl maintains the orientation of the active site histidine residue. The hydrophobic pocket and cleft for lipid binding are adjacent to the active site, and are approximately 13-15 A deep and 14-16 A long
additional information
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the enzyme's active site is composed of a Ser-His dyad (Ser11 and His218), whereby stabilization of the imidazole is provided by the main-chain carbonyl oxygen of Ser216, a common variation of the catalytic triad in many serine hydrolases, where this carbonyl maintains the orientation of the active site histidine residue. The hydrophobic pocket and cleft for lipid binding are adjacent to the active site, and are approximately 13-15 A deep and 14-16 A long
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additional information
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residue Ser11 is essential for the catalytic function of the enzyme, the active site may include residues Ser216 and His218
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