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Overview for MACiE Entry M0028

Version history

General Information

EC Number: 3.1.4.11 (A member of the Hydrolases, Acting on ester bonds, Phosphoric-diester hydrolases)

Enzyme Name: phosphoinositide phospholipase C

Biological Species: Rattus norvegicus (Rat)

Catalytic Chain UniprotKB Accession Codes:

  • P10688 - 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-1

Representative PDB Code: 1djx - PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C-DELTA1 FROM RATCOMPLEXED WITH INOSITOL-1,4,5-TRISPHOSPHATE (Resolution = 2.30 Å).

Catalytic CATH Codes:

  • 3.20.20.190 - Phosphatidylinositol (PI) phosphodiesterase

"Other" CATH Codes:

Display structure information

Overall Reaction:

Image of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate

Image of water

right arrow

Image of D-myo-inositol 1,4,5-trisphosphate

Image of 1,2-diacylglycerol

1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
C04637
CHEBI:58456
water
C00001
CHEBI:15377
D-myo-inositol 1,4,5-trisphosphate
C01245
CHEBI:16595
1,2-diacylglycerol
C00641
CHEBI:17815

View similar reactions


Stepwise Description of the Reaction

Step 1Glu390 deprotonates the hydroxyl group adjacent to the phosphate, which initiates a nucleophilic attack on the phosphorus in a substitution reaction that eliminates diacylglycerol which deprotonates His356.
Step 2His356 deprotonates water, which initiates a nucleophilic attack upon the phosphorus in a substitution reaction. The initial attacking hydroxyl is regenerated and deprotonates Glu390.

View similar reactions (composite manual annotation)


Catalytic Residues Involved

Type Number Chain Location of Function
His 311 A Side Chain
Asn 312 A Side Chain
His 356 A Side Chain
Glu 390 A Side Chain

Metal Cofactors for M0028

Type Het group Number Chain
calcium CA 2 A Overview

References

  1. D. W. Heinz et al. (1998), J. Mol. Biol., 275, 635-650. Structural and mechanistic comparison of prokaryotic and eukaryotic phosphoinositide-specific phospholipases C.
    Medline: 9466937
  2. L. O. Essen et al. (1997), Biochemistry, 36, 1704-1718. Structural mapping of the catalytic mechanism for a mammalian phosphoinositide-specific phospholipase C.
    Medline: 9048554

Homologue information for M0028 (1djx)

CSA Homologues

MACiE Homologues (within the PDB)

MACiE Homologues (within UniprotKB/SwissProt)



Entries with at least one Catalytic CATH code in common (different mechanisms):

MACiE Entry Enzyme Name
EC Number
PDB code CATH code Composite
Reaction Similarity
Catalytic Machinery
Similarity
M0242 sphingomyelin phosphodiesterase D
3.1.4.41
2f9r 3.20.20.190
0.35480.2499Compare
M0300 glycerophosphodiester phosphodiesterase
3.1.4.46
2pz0 3.20.20.190
0.69230.3999Compare
M0026 phosphatidylinositol diacylglycerol-lyase
4.6.1.13
1ptd 3.20.20.190
0.60.3413Compare

View a comparison of the other reactions in MACiE with the CATH domain 3.20.20.190


Links to this entry in other databases

Link to EC-PDB-SUM Link to PDB-SUM Link to RCSB PDB Link to PDBe Link to CSA
Link to MetaCyc Link to KEGG Link to BRENDA Link to ExplorENZ
Link to EzCatDB

GOA logo
phosphatidylinositol phospholipase C activity (molecular function)
phospholipase C activity (molecular function)
calcium ion binding (molecular function)
lipid metabolic process (biological process)
signal transduction (biological process)
phosphoric diester hydrolase activity (molecular function)
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