Abstract
Secreted phospholipase A2 (sPLA2) is an enzyme that hydrolyzes the phospholipids at a specific site and initiates the inflammatory/arachidonic acid (AA) pathway. Snake venom sPLA2s are neuro- and myo- toxins while different tissues of human body produce sPLA2s involved in inflammation, signalling and atherosclerosis. These wide ranges of pharmacological activities exerted by sPLA2s with a conserved structural domain thrust scientists to understand the molecular mechanism behind it, in the past two decades. This resulted in availability of well characterized biological data on function of sPLA2s of almost all types and continuous deposition of their structural data in the protein data bank. Additionally, the isoform specific inhibitors can also be retrieved from different chemical compound databases for futuristic and knowledge-based computational studies. Hence, inhibition or regulation of sPLA2s deserves a significant clinical and pharmacological importance, despite their anti-bacterial and anti-viral activities. In the present situation with increase in snake bite or envenomation cases worldwide, particularly in tropical countries, further studies on catalytic and inhibition mechanisms of sPLA2 isoforms at atomic details are necessary to confront the associated pathologies. This chapter is structured to provide detailed information of the current knowledge on the sPLA2 biology and future perspectives.
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References
Arni RK, Ward RJ (1996) Phospholipase A2 – a structural review. Toxicon 34:827–841. https://doi.org/10.1016/0041-0101(96)00036-0
Aung HT, Nikai T, Niwa M, Takaya Y (2010) Rosmarinic acid in Argusia argentea inhibits snake venom-induced hemorrhage. J Nat Med 64:482–486. https://doi.org/10.1007/s11418-010-0428-3
Bala P, Grochowski P, Nowinski K, Lesyng B, McCammon JA (2000) Quantum-dynamical picture of a multistep enzymatic process: reaction catalyzed by phospholipase A(2). Biophys J 79:1253–1262. https://doi.org/10.1016/S0006-3495(00)76379-X
Balsinde J, Balboa MA, Insel PA, Dennis EA (1999) Regulation and inhibition of phospholipase A2. Annu Rev Pharmacol Toxicol 39:175–189. https://doi.org/10.1146/annurev.pharmtox.39.1.175
Berg OG, Gelb MH, Tsai MD, Jain MK (2001) Interfacial enzymology: the secreted phospholipase A(2)-paradigm. Chem Rev 101:2613–2654
Bezzine S et al (2000) Exogenously added human group X secreted phospholipase A(2) but not the group IB, IIA, and V enzymes efficiently release arachidonic acid from adherent mammalian cells. J Biol Chem 275:3179–3191
Bjelic S, Aqvist J (2004) Computational prediction of structure, substrate binding mode, mechanism, and rate for a malaria protease with a novel type of active site. Biochemistry 43:14521–14528. https://doi.org/10.1021/bi048252q
Boilard E et al (2010) A novel anti-inflammatory role for secretory phospholipase A2 in immune complex-mediated arthritis. EMBO Mol Med 2:172–187. https://doi.org/10.1002/emmm.201000072
Bowers KJ, Dror RO, Shaw DE (2006) The midpoint method for parallelization of particle simulations. J Chem Phys 124:184109. https://doi.org/10.1063/1.2191489
Brunk E, Rothlisberger U (2015) Mixed quantum mechanical/molecular mechanical molecular dynamics simulations of biological systems in ground and electronically excited states. Chem Rev 115:6217–6263. https://doi.org/10.1021/cr500628b
Bucher D, Hsu YH, Mouchlis VD, Dennis EA, McCammon JA (2013) Insertion of the Ca(2)(+)-independent phospholipase A(2) into a phospholipid bilayer via coarse-grained and atomistic molecular dynamics simulations. PLoS Comput Biol 9:e1003156. https://doi.org/10.1371/journal.pcbi.1003156
Campos PC, de Melo LA, Dias GLF, Fortes-Dias CL (2016) Endogenous phospholipase A2 inhibitors in snakes: a brief overview. J Venom Anim Toxins Incl Trop Dis 22:37. https://doi.org/10.1186/s40409-016-0092-5
Chandra V, Jasti J, Kaur P, Betzel C, Srinivasan A, Singh TP (2002) First structural evidence of a specific inhibition of phospholipase A2 by α-tocopherol (vitamin E) and its implications in inflammation: crystal structure of the complex formed between phospholipase A2 and α-tocopherol at 1.8 Å resolution. J Mol Biol 320:215–222. https://doi.org/10.1016/S0022-2836(02)00473-4
Chioato L, Aragao EA, Lopes Ferreira T, Medeiros AI, Faccioli LH, Ward RJ (2007) Mapping of the structural determinants of artificial and biological membrane damaging activities of a Lys49 phospholipase A2 by scanning alanine mutagenesis. Biochim Biophys Acta 1768:1247–1257. https://doi.org/10.1016/j.bbamem.2007.01.023
Chothia C, Lesk AM (1986) The relation between the divergence of sequence and structure in proteins. EMBO J 5:823–826
Claeyssens F et al (2006) High-accuracy computation of reaction barriers in enzymes. Ange Chem 45:6856–6859. https://doi.org/10.1002/anie.200602711
Davidson FF, Dennis EA (1990) Evolutionary relationships and implications for the regulation of phospholipase A2 from snake venom to human secreted forms. J Mol Evol 31:228–238
Demaret J-P, Brunie S (1992) A unique structural feature of a phospholipase A2 is probed by molecular dynamics. J Mol Graph 10:257–260. https://doi.org/10.1016/0263-7855(92)80079-S
Dennis EA (1994) Diversity of group types, regulation, and function of phospholipase A2. J Biol Chem 269:13057–13060
Dennis EA (1997) The growing phospholipase A2 superfamily of signal transduction enzymes. Trends Biochem Sci 22:1–2
Dijkstra BW, Kalk KH, Hol WG, Drenth J (1981) Structure of bovine pancreatic phospholipase A2 at 1.7A resolution. J Mol Biol 147:97–123
Dijkstra BW, Kalk KH, Drenth J, de Haas GH, Egmond MR, Slotboom AJ (1984) Role of the N-terminus in the interaction of pancreatic phospholipase A2 with aggregated substrates. Properties and crystal structure of transaminated phospholipase A2. Biochemistry 23:2759–2766
Fremont DH, Anderson DH, Wilson IA, Dennis EA, Xuong NH (1993) Crystal structure of phospholipase A2 from Indian cobra reveals a trimeric association. Proc Natl Acad Sci 90:342–346
Friesner RA et al (2004) Glide: a new approach for rapid, accurate docking and scoring. 1. Method and assessment of docking accuracy. J Med Chem 47:1739–1749. https://doi.org/10.1021/jm0306430
Funk CD (2001) Prostaglandins and leukotrienes: advances in eicosanoid biology. Science 294:1871–1875. https://doi.org/10.1126/science.294.5548.1871
Gaulton A et al (2012) ChEMBL: a large-scale bioactivity database for drug discovery. Nucl Acids Res 40:D1100–D1107. https://doi.org/10.1093/nar/gkr777
Gelb MH, Jain MK, Hanel AM, Berg OG (1995) Interfacial enzymology of glycerolipid hydrolases: lessons from secreted phospholipases A2. Annu Rev Biochem 64:653–688. https://doi.org/10.1146/annurev.bi.64.070195.003253
Gutierrez JM, Ownby CL (2003) Skeletal muscle degeneration induced by venom phospholipases A2: insights into the mechanisms of local and systemic myotoxicity. Toxicon 42:915–931. https://doi.org/10.1016/j.toxicon.2003.11.005
Hallstrand TS, Chi EY, Singer AG, Gelb MH, Henderson WR Jr (2007) Secreted phospholipase A2 group X overexpression in asthma and bronchial hyperresponsiveness. Am J Respir Crit Care Med 176:1072–1078. https://doi.org/10.1164/rccm.200707-1088OC
Jain MK, Berg OG (1989) The kinetics of interfacial catalysis by phospholipase A2 and regulation of interfacial activation: hopping versus scooting. Biochim Biophys Acta 1002:127–156
Jain MK, Cordes EH (1973) Phospholipases. I. Effect of n-alkanols on the rate of enzymatic hydrolysis of egg phosphatidylcholine. J Membr Biol 14:101–118
Jeyaseelan K, Armugam A, Donghui M, Tan N-H (2000) Structure and phylogeny of the venom group I phospholipase A2 gene. Mol Biol Evol 17:1010–1021
Jones G, Willett P, Glen RC, Leach AR, Taylor R (1997) Development and validation of a genetic algorithm for flexible docking. J Mol Biol 267:727–748. https://doi.org/10.1006/jmbi.1996.0897
Kaiser J (2005) Science resources. Chemists want NIH to curtail database. Science 308:774. https://doi.org/10.1126/science.308.5723.774a
Kamerlin SC, Warshel A (2010) At the dawn of the 21st century: Is dynamics the missing link for understanding enzyme catalysis? Proteins 78:1339–1375. https://doi.org/10.1002/prot.22654
Karabina SA et al (2006) Atherogenic properties of LDL particles modified by human group X secreted phospholipase A2 on human endothelial cell function. FASEB J 20:2547–2549. https://doi.org/10.1096/fj.06-6018fje
Kimura-Matsumoto M et al (2008) Expression of secretory phospholipase A2s in human atherosclerosis development. Atherosclerosis 196:81–91. https://doi.org/10.1016/j.atherosclerosis.2006.08.062
Kini RM (2003) Excitement ahead: structure, function and mechanism of snake venom phospholipase A2 enzymes. Toxicon 42:827–840. https://doi.org/10.1016/j.toxicon.2003.11.002
Kini RM (2006) Anticoagulant proteins from snake venoms: structure, function and mechanism. Biochem J 397:377–387. https://doi.org/10.1042/BJ20060302
Lambeau G, Gelb MH (2008) Biochemistry and physiology of mammalian secreted phospholipases A2. Annu Rev Biochem 77:495–520. https://doi.org/10.1146/annurev.biochem.76.062405.154007
Li X, Shridas P, Forrest K, Bailey W, Webb NR (2010) Group X secretory phospholipase A2 negatively regulates adipogenesis in murine models. FASEB J 24:4313–4324. https://doi.org/10.1096/fj.10-154716
Lippert RA et al (2007) A common, avoidable source of error in molecular dynamics integrators. J Chem Phys 126:046101. https://doi.org/10.1063/1.2431176
Liu T, Lin Y, Wen X, Jorissen RN, Gilson MK (2007) BindingDB: a web-accessible database of experimentally determined protein-ligand binding affinities. Nucl Acids Res 35:D198–D201. https://doi.org/10.1093/nar/gkl999
Lomonte B, Rangel J (2012) Snake venom Lys49 myotoxins: From phospholipases A(2) to non-enzymatic membrane disruptors. Toxicon 60:520–530. https://doi.org/10.1016/j.toxicon.2012.02.007
Mallat Z et al (2005) Circulating secretory phospholipase A2 activity predicts recurrent events in patients with severe acute coronary syndromes. J Am Coll Cardiol 46:1249–1257. https://doi.org/10.1016/j.jacc.2005.06.056
Manby FR, Werner HJ, Adler TB, May AJ (2006) Explicitly correlated local second-order perturbation theory with a frozen geminal correlation factor. J Chem Phys 124:94103. https://doi.org/10.1063/1.2173247
Marti-Renom MA, Stuart AC, Fiser A, Sanchez R, Melo F, Sali A (2000) Comparative protein structure modeling of genes and genomes. Annu Rev Biophys Biomol Struct 29:291–325. https://doi.org/10.1146/annurev.biophys.29.1.291
Masuda S, Murakami M, Mitsuishi M, Komiyama K, Ishikawa Y, Ishii T, Kudo I (2005) Expression of secretory phospholipase A2 enzymes in lungs of humans with pneumonia and their potential prostaglandin-synthetic function in human lung-derived cells. Biochem J 387:27–38. https://doi.org/10.1042/BJ20041307
Melo PA et al (2010) Ability of a synthetic coumestan to antagonize Bothrops snake venom activities. Toxicon 55:488–496. https://doi.org/10.1016/j.toxicon.2009.09.021
Menschikowski M, Hagelgans A, Siegert G (2006) Secretory phospholipase A2 of group IIA: is it an offensive or a defensive player during atherosclerosis and other inflammatory diseases? Prostaglandins Other Lipid Mediat 79:1–33. https://doi.org/10.1016/j.prostaglandins.2005.10.005
Morris GM, Huey R, Lindstrom W, Sanner MF, Belew RK, Goodsell DS, Olson AJ (2009) AutoDock4 and AutoDockTools4: Automated docking with selective receptor flexibility. J Comput Chem 30:2785–2791. https://doi.org/10.1002/jcc.21256
Mors WB, Nascimento MC, Pereira BM, Pereira NA (2000) Plant natural products active against snake bite – the molecular approach. Phytochemistry 55:627–642
Mouchlis VD, Bucher D, McCammon JA, Dennis EA (2015) Membranes serve as allosteric activators of phospholipase A2, enabling it to extract, bind, and hydrolyze phospholipid substrates. Proc Natl Acad Sci U S A 112:E516–E525. https://doi.org/10.1073/pnas.1424651112
Moustakas DT, Lang PT, Pegg S, Pettersen E, Kuntz ID, Brooijmans N, Rizzo RC (2006) Development and validation of a modular, extensible docking program: DOCK 5. J Comput Aided Mol Des 20:601–619. https://doi.org/10.1007/s10822-006-9060-4
Mukherjee AK (2012) Green medicine as a harmonizing tool to antivenom therapy for the clinical management of snakebite: the road ahead. Indian J Med Res 136:10–12
Mukherjee AK, Doley R, Saikia D (2008) Isolation of a snake venom phospholipase A2 (PLA2) inhibitor (AIPLAI) from leaves of Azadirachta indica (Neem): mechanism of PLA2 inhibition by AIPLAI in vitro condition. Toxicon 51:1548–1553. https://doi.org/10.1016/j.toxicon.2008.03.021
Munoz NM, Meliton AY, Arm JP, Bonventre JV, Cho W, Leff AR (2007) Deletion of secretory group V phospholipase A2 attenuates cell migration and airway hyperresponsiveness in immunosensitized mice. J Immunol 179:4800–4807
Murakami M, Kudo I (2003) New phospholipase A(2) isozymes with a potential role in atherosclerosis. Curr Opin Lipidol 14:431–436. https://doi.org/10.1097/01.mol.0000092629.86399.d6
Murakami M, Shimbara S, Kambe T, Kuwata H, Winstead MV, Tischfield JA, Kudo I (1998) The functions of five distinct mammalian phospholipase A2S in regulating arachidonic acid release. Type IIa and type V secretory phospholipase A2S are functionally redundant and act in concert with cytosolic phospholipase A2. J Biol Chem 273:14411–14423
Murakami M et al (1999) Different functional aspects of the group II subfamily (Types IIA and V) and type X secretory phospholipase A(2)s in regulating arachidonic acid release and prostaglandin generation. Implications of cyclooxygenase-2 induction and phospholipid scramblase-mediated cellular membrane perturbation. J Biol Chem 274:31435–31444
Murakami M, Taketomi Y, Sato H, Yamamoto K (2011) Secreted phospholipase A2 revisited. J Biochem 150:233–255. https://doi.org/10.1093/jb/mvr088
Murakami M, Sato H, Miki Y, Yamamoto K, Taketomi Y (2015) A new era of secreted phospholipase A(2). J Lipid Res 56:1248–1261. https://doi.org/10.1194/jlr.R058123
Nevalainen TJ, Cardoso JC, Riikonen PT (2012) Conserved domains and evolution of secreted phospholipases A(2). FEBS J 279:636–649. https://doi.org/10.1111/j.1742-4658.2011.08453.x
Ohtsuki M et al (2006) Transgenic expression of group V, but not group X, secreted phospholipase A2 in mice leads to neonatal lethality because of lung dysfunction. J Biol Chem 281:36420–36433. https://doi.org/10.1074/jbc.M607975200
Otero R et al (2002) Complications of Bothrops, Porthidium, and Bothriechis snakebites in Colombia. A clinical and epidemiological study of 39 cases attended in a university hospital. Toxicon 40:1107–1114
Perumal Samy R, Gopalakrishnakone P, Chow VT (2012) Therapeutic application of natural inhibitors against snake venom phospholipase A(2). Bioinformation 8:48–57
Phillips JC et al (2005) Scalable molecular dynamics with NAMD. J Comput Chem 26:1781–1802. https://doi.org/10.1002/jcc.20289
Ponder JW, Richards FM (1987) An efficient newton-like method for molecular mechanics energy minimization of large molecules. J Comput Chem 8:1016–1024. https://doi.org/10.1002/jcc.540080710
Ponder JW et al (2010) Current status of the AMOEBA polarizable force field. J Phys Chem B 114:2549–2564. https://doi.org/10.1021/jp910674d
Qin SS, Yu YX, Li QK, Yu ZW (2013) Interaction of human synovial phospholipase A2 with mixed lipid bilayers: a coarse-grain and all-atom molecular dynamics simulation study. Biochemistry 52:1477–1489. https://doi.org/10.1021/bi3012687
Rajakannan V et al (2002) Observation of additional calcium ion in the crystal structure of the triple mutant K56,120,121M of bovine pancreatic phospholipase A2. J Mol Biol 324:755–762
Ramakrishnan C, Subramanian V, Velmurugan D (2010) Molecular dynamics study of secretory phospholipase A2 of Russell’s viper and bovine pancreatic sources. J Phys Chem B 114:13463–13472. https://doi.org/10.1021/jp102073f
Ramakrishnan C, Joshi V, Joseph JM, Vishwanath BS, Velmurugan D (2014) Identification of novel inhibitors of Daboia russelli phospholipase A2 using the combined pharmacophore modeling approach. Chem Biol Drug Design 84:379–392. https://doi.org/10.1111/cbdd.12332
Ramirez F, Jain MK (1991) Phospholipase A2 at the bilayer interface. Proteins: Structure, Function, and Bioinformatics 9:229–239
Ranawaka UK, Lalloo DG, de Silva HJ (2013) Neurotoxicity in snakebite—the limits of our knowledge. PLoS Negl Trop Dis 7:e2302. https://doi.org/10.1371/journal.pntd.0002302
Rivera R, Chun J (2008) Biological effects of lysophospholipids. Rev Physiol Biochem Pharmacol 160:25–46. https://doi.org/10.1007/112_0507
Rosengren B, Jonsson-Rylander AC, Peilot H, Camejo G, Hurt-Camejo E (2006) Distinctiveness of secretory phospholipase A2 group IIA and V suggesting unique roles in atherosclerosis. Biochim Biophys Acta 1761:1301–1308. https://doi.org/10.1016/j.bbalip.2006.06.008
Rosenson RS, Gelb MH (2009) Secretory phospholipase A2: a multifaceted family of proatherogenic enzymes. Curr Cardiol Rep 11:445–451
Saikia D, Thakur R, Mukherjee AK (2011) An acidic phospholipase A(2) (RVVA-PLA(2)-I) purified from Daboia russelli venom exerts its anticoagulant activity by enzymatic hydrolysis of plasma phospholipids and by non-enzymatic inhibition of factor Xa in a phospholipids/Ca(2+) independent manner. Toxicon 57:841–850. https://doi.org/10.1016/j.toxicon.2011.02.018
Seilhamer JJ, Pruzanski W, Vadas P, Plant S, Miller JA, Kloss J, Johnson LK (1989) Cloning and recombinant expression of phospholipase A2 present in rheumatoid arthritic synovial fluid. J Biol Chem 264:5335–5338
Sekar K et al (2003) Crystal structures of the free and anisic acid bound triple mutant of phospholipase A2. J Mol Biol 333:367–376
Shukla PK, Gautam L, Sinha M, Kaur P, Sharma S, Singh TP (2015) Structures and binding studies of the complexes of phospholipase A2 with five inhibitors. Biochim Biophys Acta 1854:269–277. https://doi.org/10.1016/j.bbapap.2014.12.017
Singh P, Yasir M, Hazarika R, Sugunan S, Shrivastava R (2017) A review on venom enzymes neutralizing ability of secondary metabolites from medicinal plants. J Pharmacopunct 20:173–178. https://doi.org/10.3831/KPI.2017.20.020
Six DA, Dennis EA (2000) The expanding superfamily of phospholipase A(2) enzymes: classification and characterization. Biochim Biophys Acta 1488:1–19
Soares AM et al (2005) Medicinal plants with inhibitory properties against snake venoms. Curr Med Chem 12:2625–2641
Stefansson S, Kini RM, Evans HJ (1990) The basic phospholipase A2 from Naja nigricollis venom inhibits the prothrombinase complex by a novel nonenzymatic mechanism. Biochemistry 29:7742–7746
Stephens JWW, Myers W (1898) The action of cobra poison on the blood: a contribution to the study of passive immunity. J Pathol Bacteriol 5:279–301. https://doi.org/10.1002/path.1700050307
Sterling T, Irwin JJ (2015) ZINC 15 – ligand discovery for everyone. J Chem Inform Model 55:2324–2337. https://doi.org/10.1021/acs.jcim.5b00559
Strauch MA et al (2013) Antiophidic activity of the extract of the Amazon plant Humirianthera ampla and constituents. J Ethnopharmacol 145:50–58. https://doi.org/10.1016/j.jep.2012.10.033
Thwin MM, Gopalakrishnakone P (1998) Snake envenomation and protective natural endogenous proteins: a mini review of the recent developments (1991-1997). Toxicon 36:1471–1482
Trott O, Olson AJ (2010) AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. J Comput Chem 31:455–461. https://doi.org/10.1002/jcc.21334
Valentin E, Lambeau G (2000) Increasing molecular diversity of secreted phospholipases A(2) and their receptors and binding proteins. Biochim Biophys Acta 1488:59–70
Van Der Spoel D, Lindahl E, Hess B, Groenhof G, Mark AE, Berendsen HJ (2005) GROMACS: fast, flexible, and free. J Comput Chem 26:1701–1718. https://doi.org/10.1002/jcc.20291
Venkatesan C et al (2014) Antivenom activity of triterpenoid (C34H68O2) from Leucas aspera Linn. against Naja naja naja venom induced toxicity: antioxidant and histological study in mice. Hum Exp Toxicol 33:336–359. https://doi.org/10.1177/0960327113494901
Verger R, De Haas GH (1973) Enzyme reactions in a membrane model. 1. A new technique to study enzyme reactions in monolayers. Chem Phys Lipids 10:127–136
Verger R, Mieras MC, de Haas GH (1973) Action of phospholipase A at interfaces. J Biol Chem 248:4023–4034
Verheij HM, Slotboom AJ, de Haas GH (1981) Structure and function of phospholipase A2. Rev Physiol Biochem Pharmacol 91:91–203
Ward RJ, Alves AR, Ruggiero Neto J, Arni RK, Casari G (1998) A SequenceSpace analysis of Lys49 phopholipases A2: clues towards identification of residues involved in a novel mechanism of membrane damage and in myotoxicity. Protein Eng 11:285–294
Warrell DA (2010) Snake bite. Lancet 375:77–88. https://doi.org/10.1016/S0140-6736(09)61754-2
Warshel A, Levitt M (1976) Theoretical studies of enzymic reactions: dielectric, electrostatic and steric stabilization of the carbonium ion in the reaction of lysozyme. J Mol Biol 103:227–249
Warshel A, Weiss RM (1980) An empirical valence bond approach for comparing reactions in solutions and in enzymes. J Am Chem Soc 102:6218–6226. https://doi.org/10.1021/ja00540a008
Warshel A, Weiss RM (1981) Empirical valence bond calculations of enzyme catalysis. Ann N Y Acad Sci 367:370–382
Webb NR (2005) Secretory phospholipase A2 enzymes in atherogenesis. Curr Opin Lipidol 16:341–344
Wee CL, Balali-Mood K, Gavaghan D, Sansom MS (2008) The interaction of phospholipase A2 with a phospholipid bilayer: coarse-grained molecular dynamics simulations. Biophys J 95:1649–1657. https://doi.org/10.1529/biophysj.107.123190
Winget JM, Pan YH, Bahnson BJ (2006) The interfacial binding surface of phospholipase A2s. Biochim Biophys Acta 1761:1260–1269. https://doi.org/10.1016/j.bbalip.2006.08.002
Wishart DS et al (2006) DrugBank: a comprehensive resource for in silico drug discovery and exploration. Nucl Acids Res 34:D668–D672. https://doi.org/10.1093/nar/gkj067
Wootton PT et al (2007) Tagging SNP haplotype analysis of the secretory PLA2-V gene, PLA2G5, shows strong association with LDL and oxLDL levels, suggesting functional distinction from sPLA2-IIA: results from the UDACS study. Hum Mol Genet 16:1437–1444. https://doi.org/10.1093/hmg/ddm094
Yamamoto K, Miki Y, Sato H, Murase R, Taketomi Y, Murakami M (2017) Secreted phospholipase A2 specificity on natural membrane phospholipids. Methods Enzymol 583:101–117. https://doi.org/10.1016/bs.mie.2016.09.007
Yuan W, Quinn DM, Sigler PB, Gelb MH (1990) Kinetic and inhibition studies of phospholipase A2 with short-chain substrates and inhibitors. Biochemistry 29:6082–6094. https://doi.org/10.1021/bi00477a028
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Chandrasekaran, R., Bhattacharjee, A., Devadasan, V. (2019). Anti-inflammatory and Antidote Drug Discovery with Secreted Phospholipase A2 . In: Husain, Q., Ullah, M. (eds) Biocatalysis. Springer, Cham. https://doi.org/10.1007/978-3-030-25023-2_10
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