| Entry |
|
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| Name |
phospholipase A2;
lecithinase A;
phosphatidase;
phosphatidolipase;
phospholipase A |
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| Class |
Hydrolases;
Acting on ester bonds;
Carboxylic-ester hydrolases
 |
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| Sysname |
phosphatidylcholine 2-acylhydrolase |
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| Reaction(IUBMB) |
phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a
carboxylate [RN:R01313] |
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| Reaction(KEGG) |
R01313 > R01315 R01317 R07064 R07859;
(other) R02053 R03107 R07379 R07387
 |
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| Substrate |
phosphatidylcholine [CPD:C00157];
H2O [CPD:C00001] |
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| Product |
1-acylglycerophosphocholine [CPD:C04230];
carboxylate [CPD:C00060] |
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| Cofactor |
Calcium [CPD:C00076] |
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| Inhibitor |
AACOCF3 [CPD:C01397];
1-Hexadecylthio-1-deoxy-2-hexadecylphosphono-sn-glycero-3-phosphocho
line [CPD:C04862];
1-Hexadecylthio-2-hexadecanoylamino-1,2-dideoxy-sn-glycero-3-phospho
choline [CPD:C04873] |
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| Comment |
Also acts on phosphatidylethanolamine, choline plasmalogen and
phosphatides, removing the fatty acid attached to the 2-position.
Requires Ca2+. |
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| Pathway |
PATH: ec00564 Glycerophospholipid metabolism
PATH: ec00565 Ether lipid metabolism
PATH: ec00590 Arachidonic acid metabolism
PATH: ec00591 Linoleic acid metabolism
PATH: ec00592 alpha-Linolenic acid metabolism
PATH: ec01100 Metabolic pathways |
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| Orthology |
KO: K01047 phospholipase A2 |
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| Genes |
HSA: 100137049(PLA2G4B) 123745(PLA2G4E) 26279(PLA2G2D)
30814(PLA2G2E) 391013(PLA2G2C) 50487(PLA2G3) 5319(PLA2G1B)
5320(PLA2G2A) 5321(PLA2G4A) 5322(PLA2G5) 64600(PLA2G2F)
81579(PLA2G12A) 8398(PLA2G6) 8399(PLA2G10) 84647(PLA2G12B)
8681(JMJD7-PLA2G4B)
PTR: 456587(PLA2G2A) 456588(PLA2G5) 466292(PLA2G12B) 467664(PLA2G4E)
469137(PLA2G2C) 469200(PLA2G2D) 469617(PLA2G4A) 470183(PLA2G3)
740803(PLA2G10) 742280(PLA2G1B) 747584(PLA2G4B) 748864(PLA2G2E)
748868(PLA2G2F)
MCC: 696712(PLA2G1B) 704299(PLA2G2E) 704520(PLA2G2A) 704629
704735(PLA2G2D) 707262(JMJD7-PLA2G4B) 708031(PLA2G12B)
716635(PLA2G4A) 717084 717517 718321(PLA2G3)
MMU: 18778(Pla2g1b) 18780(Pla2g2a) 18781(Pla2g2c) 18782(Pla2g2d)
18783(Pla2g4a) 18784(Pla2g5) 211429(Pla2g4b) 237625(Pla2g3)
26565(Pla2g10) 26970(Pla2g2e) 26971(Pla2g2f) 329502(Pla2g4e)
53357(Pla2g6) 66350(Pla2g12a) 69836(Pla2g12b)
RNO: 24653(Pla2g4a) 289733(Pla2g3) 29354(Pla2g5) 29359(Pla2g10)
29387(Pla2g2c) 29526(Pla2g1b) 296091(Pla2g4e) 29692(Pla2g2a)
298579(Pla2g2d) 311341(Pla2g4b) 360426(Pla2g6) 362039(Pla2g12a)
367415(Pla2g12b) 684551
CFA: 404011(PLA2G1B) 478207(PLA2G5) 478514(PLA2G12A) 480048(PLA2G4A)
481256(PLA2G6) 486361(PLA2G3) 487396(PLA2G2C) 487397(PLA2G2F)
487398(PLA2G2D) 487399(PLA2G2E) 487512(JMJD7-PLA2G4B)
487514(PLA2G4E) 489045(PLA2G12B) 489997(PLA2G10)
BTA: 282457(PLA2G1B) 494318(PLA2G2D1) 503625(PLA2G2D4) 504978
505485(JMJD7-PLA2G4B) 506243(PLA2G2E) 507201(PLA2G2A)
512006(PLA2G12B) 521383(PLA2G2A) 525072(PLA2G4A)
526364(PLA2G4E) 527214(PLA2G12A) 527631(PLA2G3) 535381(PLA2G6)
541294(PLA2G2F) 613966(PLA2G10) 614911(PLA2G5) 615045
SSC: 100152331 100152597 100152927 100155284 445525(PLA2G1B)
ECB: 100033889(PLA2G1B) 100037401(SPLA2) 100050467 100054324
100055064(PLA2G6) 100058509 100058536 100063726
100071038(PLA2G4E) 100071062 100071826 100071833 100071838
100071870 100072858
MDO: 100009808 100009945 100010093 100023771 100024666 100026162
100027378 100027397 100027418 100027447 100027467 100028565
OAA: 100073869 100075955 100076775 100077303 100079251 100081113
100085458 100086135
GGA: 396394(PLA2G4A) 416425(PLA2G10) 416980(PLA2G1B) 418028(PLA2G6)
418356(PLA2G10) 423227(PLA2G4E) 423705(PLA2G12B)
426747(PLA2G2E) 426748(PLA2G2A) 770292(PLA2G1B) 771655(PLA2G5)
772082(PLA2G12A)
TGU: 100218087 100218133 100221364 100222459 100222730 100224457
100224711 100224874 100225180 100225467 100226460 100229594
XLA: 380561(pla2g4a) 443906 446689 447090
XTR: 100145401 100145529 100145731(pla2g4a) 493298(pla2g12b)
549850(pla2g12a) 780118(pla2g6)
DRE: 30554(cpla2) 402802 406370(pla2g6) 406739(pla2g12b) 436622
571738(pla2g1b) 641423
BFO: BRAFLDRAFT_125604
CIN: 100177702 100181039 100187153
SPU: 576520 585809 590364 752200 757138 759233 764528
DME: Dmel_CG10133 Dmel_CG10706(SK) Dmel_CG11124(sPLA2) Dmel_CG14507
Dmel_CG1583(GIIIspla2) Dmel_CG17035(GXIVsPLA2) Dmel_CG3009
Dmel_CG6718
DPO: Dpse_GA14287 Dpse_GA23437 Dpse_GA26956
DAN: Dana_GF16607 Dana_GF24681
AGA: AgaP_AGAP003846 AgaP_AGAP004812
AAG: AaeL_AAEL003561 AaeL_AAEL012835
CQU: CpipJ_CPIJ007422 CpipJ_CPIJ010429
AME: 409614 410570
NVI: 100117598 100121363
TCA: 659843
API: 100164748
CEL: C03H5.4(phospholipase) C07E3.9 W07A8.2
CBR: CBG01902 CBG02732
BMY: Bm1_40085
NVE: NEMVE_v1g105508 NEMVE_v1g106424 NEMVE_v1g106450 NEMVE_v1g131395
NEMVE_v1g199410 NEMVE_v1g29089 NEMVE_v1g39271 NEMVE_v1g94443
TAD: TRIADDRAFT_63140
OSA: 4333862(Os03g0708000)
AFM: AFUA_2G11970
UMA: UM05871.1
 |
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| Structures |
PDB: 1A2A 1A3D 1A3F 1AE7 1AOK 1AYP 1B4W 1BBC 1BCI 1BJJ
1BK9 1BP2 1BPQ 1BUN 1BVM 1C1J 1C74 1CEH 1CJY 1CL5
1CLP 1DB4 1DB5 1DCY 1DPY 1FAZ 1FDK 1FE5 1FX9 1FXF
1G0Z 1G2X 1G4I 1GH4 1GMZ 1GOD 1GP7 1HN4 1IJL 1IRB
1IT4 1IT5 1J1A 1JIA 1JLT 1JQ8 1JQ9 1KP4 1KPM 1KQU
1KVO 1KVW 1KVX 1KVY 1L8S 1LE6 1LE7 1LN8 1LWB 1M8R
1M8S 1M8T 1MF4 1MG6 1MH2 1MH7 1MH8 1MKS 1MKT 1MKU
1MKV 1N28 1N29 1O2E 1O3W 1OQS 1OWS 1OXL 1OXR 1OYF
1OZ6 1OZY 1P2P 1P7O 1PA0 1PC9 1PIR 1PIS 1PO8 1POA
1POB 1POC 1POD 1POE 1PP2 1PPA 1PSH 1PSJ 1PWO 1Q6V
1Q7A 1QLL 1RGB 1RLW 1S6B 1S8G 1S8H 1S8I 1SFV 1SFW
1SKG 1SQZ 1SV3 1SV9 1SXK 1SZ8 1T37 1TC8 1TD7 1TDV
1TG1 1TG4 1TGM 1TH6 1TJ9 1TJK 1TK4 1TP2 1U4J 1U73
1UNE 1VAP 1VIP 1VKQ 1VL9 1XXS 1XXW 1Y38 1Y4L 1Y6O
1Y6P 1Y75 1YXH 1YXL 1Z76 1ZL7 1ZLB 1ZM6 1ZR8 1ZWP
1ZYX 2ARM 2AZY 2AZZ 2B00 2B01 2B03 2B04 2B17 2B96
2BAX 2BCH 2BD1 2BPP 2DO2 2DPZ 2FNX 2G58 2GNS 2H4C
2I0U 2NOT 2O1N 2OK9 2OLI 2OQD 2OSH 2OSN 2OTF 2OTH
2OUB 2OYF 2PB8 2PHI 2PMJ 2PVT 2PWS 2PYC 2Q1P 2QHD
2QHE 2QHW 2QOG 2QU9 2QUE 2QVD 2RD4 2WG7 2WG8 2WG9
2ZBH 2ZP3 2ZP4 2ZP5 3BJW 3BP2 3CBI 3ELO 3FG5 3FO7
3G8F 3G8G 3G8H 3GCI 3H1X 3HSW 3JQ5 3JQL 3L30 3L69
3P2P 4BP2 4P2P 5P2P |
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Reference
Authors
Title
Journal
Organism
|
1 [PMID:13723433]
DOERY HM, PEARSON JE.
Haemolysins in venoms of Australian snakes. Observations on the
haemolysins of the venoms of some Australian snakes and the
separation of phospholipase A from the venom of Pseudechis
porphyriacus.
Biochem. J. 78 (1961) 820-7.
Pseudechis porphyriacus |
|---|
Reference
Authors
Title
Journal
Organism
|
2 [PMID:15433984]
FRAENKEL-CONRAT H, FRAENKEL-CONRAT J.
Inactivation of crotoxin by group-specific reagents.
Biochim. Biophys. Acta. 5 (1950) 98-104.
Crotalus terrificus terrificus |
|---|
Reference
Authors
Title
Journal
Organism
|
3 [PMID:14399412]
HANAHAN DJ, BROCKERHOFF H, BARRON EJ.
The site of attack of phospholipase (lecithinase) A on lecithin: a
re-evaluation. Position of fatty acids on lecithins and
triglycerides.
J. Biol. Chem. 235 (1960) 1917-23.
Crotalus adamanteus |
|---|
Reference
Authors
Title
Journal
Organism
|
4 [PMID:14124755]
MOORE JH, WILLIAMS DL.
SOME OBSERVATIONS ON THE SPECIFICITY OF PHOSPHOLIPASE A.
Biochim. Biophys. Acta. 84 (1964) 41-54.
Sus scofa [GN:ssc], Crotalus adamanteus |
|---|
Reference
Authors
Title
Journal
Organism
|
5 [PMID:14496116]
SAITO K, HANAHAN DJ.
A study of the purification and properties of the phospholipase A of
Crotalus admanteus venom.
Biochemistry. 1 (1962) 521-32.
Crotalus adamanteus |
|---|
Reference
Authors
Title
Journal
Organism
|
6 [PMID:6252969]
van den Bosch H.
Intracellular phospholipases A.
Biochim. Biophys. Acta. 604 (1980) 191-246.
Crotalus adamanteus |
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| Other DBs |
ExplorEnz - The Enzyme Database: 3.1.1.4
IUBMB Enzyme Nomenclature: 3.1.1.4
ExPASy - ENZYME nomenclature database: 3.1.1.4
BRENDA, the Enzyme Database: 3.1.1.4
CAS: 9001-84-7 |
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