The enzyme catalyzes the hydrolysis of fatty acids from the sn-2 position of glycerophospholipids to produce free fatty acids, such as arachidonic acid, and lyso PL. Many members of this family where reported to be Ca2+ dependent enzymes (PMID9020581).
CATALYTIC METAL(S)
| Metal/Site Information | |||||
| Residue in MACiE* | Atom in MACiE* | Residue Type in MACiE | Physiological Metal |
Site Type |
Function(s) |
| CA 314 x | CA | calcium | calcium | mononuclear | Coordinates substrate Electrostatic stabiliser Increases electrophilicity |
*It refers to the MACiE reference pdb: 1l8s
| Metal/s Properties in Resting State | ||||||
| CA 314 x | Resting state enzyme (1mkt) | |||||
| Oxidation State | 2 | |||||
| Coordination Geometry | octahedral | |||||
| Coordination Number | 7 | |||||
| Notes | - | |||||
| References |
| -Cha SS, Lee D, Adams J, Kurdyla JT, Jones CS, Marshall LA, Bolognese B, Abdel-Meguid SS, Oh BH High-resolution X-ray crystallography reveals precise binding interactions between human nonpancreatic secreted phospholipase A2 and a highly potent inhibitor (FPL67047XX). J Med Chem. 1996 Sep 27;39(20):3878-81.(MEDLINE:8831753) |
| -Pan YH, Yu BZ, Berg OG, Jain MK, Bahnson BJ Crystal structure of phospholipase A2 complex with the hydrolysis products of platelet activating factor: equilibrium binding of fatty acid and lysophospholipid-ether at the active site may be mutually exclusive. Biochemistry. 2002 Dec 17;41(50):14790-800.(MEDLINE:12475227) |