KEGG   ENZYME: 4.6.1.13Help
Entry
EC 4.6.1.13                 Enzyme                                 

Name
phosphatidylinositol diacylglycerol-lyase;
monophosphatidylinositol phosphodiesterase;
phosphatidylinositol phospholipase C;
1-phosphatidylinositol phosphodiesterase;
1-phosphatidyl-D-myo-inositol inositolphosphohydrolase (cyclic-phosphate-forming);
1-phosphatidyl-1D-myo-inositol diacylglycerol-lyase (1,2-cyclic-phosphate-forming)
Class
Lyases;
Phosphorus-oxygen lyases;
Phosphorus-oxygen lyases (only sub-subclass identified to date)
BRITE hierarchy
Sysname
1-phosphatidyl-1D-myo-inositol 1,2-diacyl-sn-glycerol-lyase (1D-myo-inositol-1,2-cyclic-phosphate-forming)
Reaction(IUBMB)
1-phosphatidyl-1D-myo-inositol = 1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol [RN:R03364]
Reaction(KEGG)
R03364;
(other) R03332
Show
Substrate
1-phosphatidyl-1D-myo-inositol [CPD:C01194]
Product
1D-myo-inositol 1,2-cyclic phosphate [CPD:C04299];
1,2-diacyl-sn-glycerol [CPD:C00641]
Comment
This enzyme is bacterial. Activity is also found in animals, but this activity is due to the presence of EC 3.1.4.11, phosphoinositide phospholipase C.
History
EC 4.6.1.13 created 1972 as EC 3.1.4.10, modified 1976, transferred 2002 to EC 4.6.1.13
Pathway
ec00562  Inositol phosphate metabolism
Orthology
K01771  1-phosphatidylinositol phosphodiesterase
Genes
OAA: 107547964
GGA: 101751271
MGP: 104912324
CJO: 107317149
ACYG: 106041539
FAB: 107603775
PHI: 106628453
PMAJ: 107198622
FPG: 106112280
FCH: 106631759
CLV: 106145769
ACS: 100567546
PVT: 110071763
PBI: 103068284
XLA: 108710460
XTR: 100494672
NPR: 108790680
DRE: 100000275 100006223(si:dkey-266f7.9)
SRX: 107750812
SANH: 107693279
CCAR: 109105457
IPU: 108256182
TRU: 101062629
OLA: 101162017
XMA: 102223877
NFU: 107394624
KMR: 108239495
CSEM: 103394551
HCQ: 109511995
BPEC: 110161150
SASA: 106570214
APLC: 110987958
MDL: 103572022
TUT: 107363869
LJA: Lj1g3v3343840.1(Lj1g3v3343840.1)
ERC: Ecym_2326
TBL: TBLA_0G03650(TBLA0G03650)
CDU: CD36_17390(PLC22) CD36_17810
CAUR: QG37_01069
SLB: AWJ20_1356 AWJ20_281(PLC2)
NTE: NEUTE1DRAFT149986(NEUTE1DRAFT_149986)
MGR: MGG_04834
MBE: MBM_05780
ANI: AN3636.2
ANG: ANI_1_2710014(An01g07280)
ABE: ARB_00415
TVE: TRV_02704
PTE: PTT_15969
ABP: AGABI1DRAFT104838(AGABI1DRAFT_104838) AGABI1DRAFT121976(AGABI1DRAFT_121976)
ABV: AGABI2DRAFT200290(AGABI2DRAFT_200290) AGABI2DRAFT210674(AGABI2DRAFT_210674)
YEY: Y11_08861
YET: CH48_3722
YAL: AT01_349
YFR: AW19_1307
YKR: CH54_355
EPY: EpC_18250
EPR: EPYR_01964(plc)
EAM: EAMY_1766(plc)
EAY: EAM_1731
MMK: MU9_1927
HSO: HS_1585
HSM: HSM_0426
PMAN: OU5_0316
SPSW: Sps_01725
MVS: MVIS_0305
OAI: OLEAN_C15740(plcA)
BVE: AK36_3592
BCN: Bcen_3596
BCJ: BCAM1969
BCEW: DM40_4728
BCEO: I35_5800
BAM: Bamb_4154
BCT: GEM_3692
BCED: DM42_6033
BCON: NL30_02460
BUB: BW23_5558
BLAT: WK25_26120
BTEI: WS51_07210
BSEM: WJ12_29890
BMEC: WJ16_28455
BSTG: WT74_28980
BUK: MYA_4903
PSPU: NA29_20190
BAN: BA_3891
BAR: GBAA_3891
BAT: BAS3604
BAI: BAA_3915
BANT: A16_38960
BANR: A16R_39410
BANS: BAPAT_3727
BANV: DJ46_2594
BCE: BC3761
BCA: BCE_3793
BCQ: BCQ_3547
BCX: BCA_3856
BAL: BACI_c37040(plcA)
BNC: BCN_3582
BCF: bcf_18650
BCER: BCK_16440
BTL: BALH_3388
BTW: BF38_4930
BWW: bwei_1197(plcA2) bwei_2488(plcA)
LSP: Bsph_1112
SAU: SA0091(plc)
SAV: SAV0095(plc)
SAW: SAHV_0094(plc)
SAM: MW0070(plc)
SAR: SAR0105(plc)
SAC: SACOL0078(plc)
SAX: USA300HOU_0108(plc)
SAA: SAUSA300_0099(plc)
SAE: NWMN_0041
SAD: SAAV_0043(plc)
SUE: SAOV_0049(plc)
SUJ: SAA6159_00079(plc)
SUK: SAA6008_00080(plc)
SUC: ECTR2_52
SUZ: MS7_0088
SUX: SAEMRSA15_00670(plc)
SUW: SATW20_01140(plc)
SUG: SAPIG0113
SUF: SARLGA251_00750(plc)
SAUA: SAAG_00586
SAUE: RSAU_000049(plc)
SAUS: SA40_0066(plc)
SAUU: SA957_0081(plc)
SAUG: SA268_0078(plc)
SAUZ: SAZ172_0112(plc)
SAUT: SAI1T1_2000520(plc)
SAUJ: SAI2T2_1000520(plc)
SAUK: SAI3T3_1000520(plc)
SAUQ: SAI4T8_1000520(plc)
SAUV: SAI7S6_1000520(plc)
SAUW: SAI5S5_1000520(plc)
SAUX: SAI6T6_1000520(plc)
SAUY: SAI8T7_1000520(plc)
SAUF: X998_0075
SAB: SAB0038(plc)
SUY: SA2981_0095(plc)
SAUB: C248_0089(plc)
SAUM: BN843_990
SAUC: CA347_110
SAUR: SABB_06012
SAUI: AZ30_00505
SAUD: CH52_05240
SAMS: NI36_00415
LMO: lmo0201(plcA)
LMN: LM5578_2817(plcA)
LMY: LM5923_2766(plcA)
LMOC: LMOSLCC5850_0195(plcA)
LMOE: BN418_0211
LMOB: BN419_0215
LMOD: LMON_0199(plcA)
LMOW: AX10_09460
LMOQ: LM6179_0491(plcA)
LMR: LMR479A_0210(plcA)
LMOM: IJ09_09360
LMF: LMOf2365_0212(plcA)
LMC: Lm4b_00198(plcA)
LMOG: BN389_02150(plcA)
LMP: MUO_01150
LMOL: LMOL312_0199(plcA)
LMOX: AX24_13615
LMQ: LMM7_0222(plcA)
LML: lmo4a_0217(plcA)
LMS: LMLG_2384
LMW: LMOSLCC2755_0200(plcA)
LMX: LMOSLCC2372_0202(plcA)
LMZ: LMOSLCC2482_0201(plcA)
LMON: LMOSLCC2376_0172(plcA)
LMOO: LMOSLCC2378_0214(plcA)
LMOY: LMOSLCC2479_0201(plcA)
LMOT: LMOSLCC2540_0204(plcA)
LMOA: LMOATCC19117_0209(plcA)
LMOK: CQ02_01080
LSG: lse_0182(plcA)
CBN: CbC4_5030
CSB: CLSA_c09880(plc)
ASF: SFBM_0755
BFI: CIY_07500
SGR: SGR_3955
SGB: WQO_15845
SFA: Sfla_2893
SBH: SBI_02964
SVE: SVEN_3910
SALS: SLNWT_4056
STRP: F750_3899
SFI: SFUL_3949
SALU: DC74_6875
SALL: SAZ_35715
STRE: GZL_01891
SLD: T261_1098
STRM: M444_16580
SPRI: SPRI_4007
SMAL: SMALA_6015
SLX: SLAV_17900(plcA)
FAL: FRAAL3352
ACTN: L083_6541
CAI: Caci_6736
SNA: Snas_3757
MPK: VL20_4487
BFR: BF1750
CPI: Cpin_5471
FLN: FLA_0323
DFE: Dfer_0819
EAO: BD94_2786
ELB: VO54_03886(plc)
CHZ: CHSO_1681 CHSO_4603(plc)
TMAR: MARIT_2145
 » show all
Taxonomy
Reference
1  [PMID:4377210]
  Authors
Allan D, Michell RH.
  Title
Phosphatidylinositol cleavage catalysed by the soluble fraction from lymphocytes. Activity at pH5.5 and pH7.0.
  Journal
Biochem J 142:591-7 (1974)
Reference
2  [PMID:4294905]
  Authors
Friedel RO, Brown JD, Durell.
  Title
Monophosphatidyl inositol inositolphosphohydrolase in guinea-pig brain.
  Journal
Biochim Biophys Acta 144:684-6 (1967)
DOI:10.1016/0005-2760(67)90059-8
Reference
3  [PMID:6297738]
  Authors
Irvine RF.
  Title
The enzymology of stimulated inositol lipid turnover.
  Journal
Cell Calcium 3:295-309 (1982)
DOI:10.1016/0143-4160(82)90018-5
Reference
4  [PMID:236918]
  Authors
Michell RH, Allan D.
  Title
Inositol cyclis phosphate as a product of phosphatidylinositol breakdown by phospholipase C (Bacillus cereus).
  Journal
FEBS Lett 53:302-4 (1975)
DOI:10.1016/0014-5793(75)80041-X
Reference
5  [PMID:588258]
  Authors
Low MG, Finean JB.
  Title
Release of alkaline phosphatase from membranes by a phosphatidylinositol-specific phospholipase C.
  Journal
Biochem J 167:281-4 (1977)
Reference
6  [PMID:3194218]
  Authors
Henner DJ, Yang M, Chen E, Hellmiss R, Rodriguez H, Low MG.
  Title
Sequence of the Bacillus thuringiensis phosphatidylinositol specific phospholipase C.
  Journal
Nucleic Acids Res 16:10383 (1988)
DOI:10.1093/nar/16.21.10383
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 4.6.1.13
IUBMB Enzyme Nomenclature: 4.6.1.13
ExPASy - ENZYME nomenclature database: 4.6.1.13
BRENDA, the Enzyme Database: 4.6.1.13
CAS: 37288-19-0

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