EC number:3.1.1.4

Enzyme

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     3. Hydrolases
        3.1 Acting on ester bonds
            3.1.1 Carboxylic-ester hydrolases
ID:3.1.1.4
Description:Phospholipase A(2).
Alternative Name: Phospholipase A2.
Phosphatidylcholine 2-acylhydrolase.
Phosphatidolipase.
Phosphatidase.
Lecithinase A.
Prosite: PDOC00109;
PDB:
PDBScop
1Z76 8030413; 8042792; 8030413; 8042792;
1U73 8030413; 8042792; 8030413; 8042792;
1ZLB 8030413; 8042792;
1ZL7 8030413; 8042792;
1UMV 8030413; 8042792;
 » show all
Cath: 3.40.1090.10; 1.20.90.10; 2.30.30.1140; 2.40.160.20; 2.40.230.10; 3.40.50.1820; 2.60.40.150;

3D structure

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PDB

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1Z76; 1U73; 1ZLB; 1ZL7; 1UMV; 1GP7; 1MG6; 1MC2; 3CBI; 1Y38; 1TP2; 1OXL; 1KPM; 1JQ9; 1JQ8; 1FV0; 1FB2; 1CL5; 3H1X; 3G8F; 2ZBH; 2QVD; 2QUE; 2QU9; 2QHW; 2Q1P; 2PYC; 2PWS; 2PVT; 2PMJ; 2PB8; 2OYF; 2OUB; 2OTH; 2OTF; 2OLI; 2O1N; 2GNS; 2G58; 2FNX; 2DPZ; 2DO2; 2B17; 1ZYX; 1ZWP; 1ZR8; 1TK4; 1TJK; 1TJ9; 1TH6; 1TGM; 1TG4; 1TG1; 1TDV; 1SXK; 1SV9; 1SV3; 1SQZ; 1SKG; 1OYF; 1S8I; 1S8H; 2RD4; 1XXW; 1MH2; 1MH7; 1S6B; 1LE6; 6G5J; 5OWC; 5OW8; 5G3M; 4UY1; 1LE7; 1U4J; 1G0Z; 1GOD; 1AOK; 1VPI; 1VIP; 3CYL; 2Q2J; 1QLL; 2NOT; 4E4C; 1AE7; 1VAP; 1PSJ; 1BK9; 1PP2; 1POB; 1POA; 1POC; 1BUN; 5VFN; 5VFM; 5VFJ; 5VFH; 3MLM; 1PC9; 1PA0; 1P7O; 1OZ6; 1OQS; 1JLT; 1RGB; 1IJL; 1KVO; 1AYP; 5G3N; 3U8I; 3U8H; 3U8D; 1POE; 1N28; 1J1A; 3U8B; 1POD; 1N29; 1KQU; 1DCY; 1DB5; 1DB4; 1BBC; 3FVI; 5P2P; 3P2P; 2PHI; 1Y6P; 1Y6O; 1L8S; 1HN4; 1FXF; 1FX9; 4P2P; 4O1Y; 4G5I; 4DBK; 3QLM; 3O4M; 3L30; 3FVJ; 2B04; 2B03; 2B01; 2B00; 2AZZ; 2AZY; 1SFW; 1SFV; 1PIS; 1PIR; 1P2P; 1M8T; 1GMZ; 3Q4Y; 3OSH; 3NJU; 3JTI; 3JQL; 3JQ5; 3GCI; 1ZM6; 1YXL; 1TD7; 1T37; 1SZ8; 1OXR; 1MF4; 1LN8; 1PSH; 1A3F; 1OWS; 2WQ5; 1A3D; 1Y4L; 1CLP; 2BD1; 4BP2; 3BP2; 2ZP5; 2ZP4; 2ZP3; 2BPP; 2BP2; 2BCH; 2BAX; 2B96; 1VL9; 1VKQ; 1UNE; 1O3W; 1O2E; 1MKV; 1MKU; 1MKT; 1MKS; 1KVY; 1KVX; 1KVW; 1IRB; 1GH4; 1G4I; 1FDK; 1CEH; 1C74; 1BVM; 1BPQ; 1BP2; 6MQF; 6MQD; 6DIK; 6CE2; 6B84; 6B83; 6B81; 6B80; 6AL3; 5Y5E; 5WZW; 5WZV; 5WZU; 5WZT; 5WZS; 5WZO; 5WZM; 5TFV; 4YZ7; 4YV5; 4YU7; 4WTB; 4RFP; 4NTY; 4NTX; 4NTW; 4KF3; 4K09; 4K06; 4HG9; 4H0S; 3VC0; 3V9M; 3T0R; 3R0L; 3QNL; 3JR8; 3IQ3; 3I3I; 3I3H; 3I03; 3HZW; 3HZD; 3HSW; 3G8H; 3G8G; 3ELO; 3DIH; 3CXI; 3BJW; 2WG9; 2WG8; 2WG7; 2QOG; 2QHE; 2QHD; 2PH4; 2OSN; 2OSH; 2OQD; 2OK9; 2I0U; 2H8I; 2H4C; 2AOZ; 1YXH; 1Y75; 1XXS; 1TC8; 1S8G; 1Q5T; 1PPA; 1PO8; 1MH8; 1M8S; 1M8R; 1JIA; 1G2X; 1FE5; 1DPY; 1C1J; 1BJJ; 1B4W; 1A2A;

References

External Links

UniProtKB Enzyme Link: UniProtKB 3.1.1.4
BRENDA Enzyme Link: BRENDA 3.1.1.4
KEGG Enzyme Link: KEGG3.1.1.4
BioCyc Enzyme Link: BioCyc 3.1.1.4
ExPASy Enzyme Link: ExPASy3.1.1.4
EC2PDB Enzyme Link: EC2PDB 3.1.1.4
ExplorEnz Enzyme Link: ExplorEnz 3.1.1.4
PRIAM enzyme-specific profiles Link: PRIAM 3.1.1.4
IntEnz Enzyme Link: IntEnz 3.1.1.4
MEDLINE Enzyme Link: MEDLINE 3.1.1.4

EC number:3.1.1.4

MSA:

3.1.1.4;
Phylogenetic Tree:

3.1.1.4;
Uniprot:
M-CSA:
RHEA:36231 1-O-alkyl-2-acyl-sn-glycero-3-phosphocholine + H2O = 1-O-alkyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
RULE(radius=1) [*:1]-[O;H0;+0:2]-[C;H0;+0:3](-[*:4])=[*:5].[OH2;+0:6]>>[*:4]-[C;H0;+0:3](=[*:5])-[OH;+0:6].[*:1]-[OH;+0:2]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Purification and characterization of a catalytic domain of rat intestinal phospholipase B/lipase associated with brush border membranes.Tojo H, Ichida T, Okamoto M1998 Jan 239442064
RHEA:15801 a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
RULE(radius=1) [*:1]=[C;H0;+0:2](-[*:3])-[O;H0;+0:4]-[*:5].[OH2;+0:6]>>[*:5]-[OH;+0:4].[*:1]=[C;H0;+0:2](-[*:3])-[OH;+0:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Inherited human cPLA(2alpha) deficiency is associated with impaired eicosanoid biosynthesis, small intestinal ulceration, and platelet dysfunction.Adler DH, Cogan JD, Phillips JA 3rd, Schnetz-Boutaud N, Milne GL, Iverson T, Stein JA, Brenner DA, Morrow JD, Boutaud O, Oates JA2008 Jun18451993