S00236
type: Enzyme
rlcp: p76
cath: TIM Barrel
ec: https://purl.uniprot.org/enzyme/4.6.1.13
csa: 2plc
macie: M0026
uniprot: P34024
uniprot: P14262
uniprot: P08954
kegg enzyme: phosphatidylinositol diacylglycerol-lyase
kegg enzyme: monophosphatidylinositol phosphodiesterase
kegg enzyme: phosphatidylinositol phospholipase C
kegg enzyme: 1-phosphatidylinositol phosphodiesterase
kegg enzyme: 1-phosphatidyl-D-myo-inositol inositolphosphohydrolase(cyclic-phosphate-forming)
kegg enzyme: 1-phosphatidyl-1D-myo-inositol diacylglycerol-lyase(1,2-cyclic-phosphate-forming)
kegg pathway: Inositol phosphate metabolism
kegg substrate: 1-Phosphatidyl-D-myo-inositol
kegg product: D-myo-Inositol 1,2-cyclic phosphate
kegg product: Diacylglycerol
pdb: 1aodA
pdb: 2plcA
pdb: 1gymA
pdb: 1ptdA
pdb: 1ptgA
pdb: 2ptdA
pdb: 3ptdA
pdb: 4ptdA
pdb: 5ptdA
pdb: 6ptdA
pdb: 7ptdA
pdb: 1t6mA
pdb: 1t6mB
pdb: 2or2A
pdb: 2or2B
pdb bound state: Unbound
  compound: 1-Phosphatidyl-D-myo-inositol
  pdb: 1aodA
active site residues resources: Short-chain phosphatidylinositol conformation and its relevance to phosphatidylinositol-specific phospholipase C.
active site residues resources: Structural and mechanistic comparison of prokaryotic and eukaryotic phosphoinositide-specific phospholipases C.
active site residues resources: Bacterial phosphatidylinositol-specific phospholipase C: structure, function, and interaction with lipids.
active site residues resources: Mutagenesis of active-site histidines of Listeria monocytogenes phosphatidylinositol-specific phospholipase C: effects on enzyme activity and biological function.
active site residues resources: A catalytic diad involved in substrate-assisted catalysis: NMR study of hydrogen bonding and dynamics at the active site of phosphatidylinositol-specific phospholipase C.
active site residues resources: N-terminal EF-hand-like domain is required for phosphoinositide-specific phospholipase C activity in Arabidopsis thaliana.
active site residues resources: Water-miscible organic cosolvents enhance phosphatidylinositol-specific phospholipase C phosphotransferase as well as phosphodiesterase activity.
active site residues resources: X-ray structure of the R69D phosphatidylinositol-specific phospholipase C enzyme: insight into the role of calcium and surrounding amino acids in active site geometry and catalysis.
references: Phospholipids chiral at phosphorus. Stereochemical mechanism of reactions catalyzed by phosphatidylinositide-specific phospholipase C from Bacillus cereus and guinea pig uterus.
references: Divalent cation regulation of phosphoinositide metabolism. Naturally occurring B lymphoblasts contain a Mg2(+)-regulated phosphatidylinositol-specific phospholipase C.
references: A chromogenic substrate for phosphatidylinositol-specific phospholipase C: 4-nitrophenyl myo-inositol-1-phosphate.
references: Phospholipase stereospecificity at phosphorus.
references: Phospholipids chiral at phosphorus. Stereochemical mechanism for the formation of inositol 1-phosphate catalyzed by phosphatidylinositol-specific phospholipase C.
references: Substrate requirements of bacterial phosphatidylinositol-specific phospholipase C.
references: Crystallization of phosphatidylinositol-specific phospholipase C from Bacillus cereus.
references: Phosphatidylinositol-specific phospholipase C from Bacillus cereus at the lipid-water interface: interfacial binding, catalysis, and activation.
references: src-homology 2 (SH2) domain ligation as an allosteric regulator: modulation of phosphoinositide-specific phospholipase C gamma 1 structure and activity.
references: Crystal structure of the phosphatidylinositol-specific phospholipase C from Bacillus cereus in complex with myo-inositol.
references: Mechanism and structure based inhibitors of phospholipase C enzymes.
references: Crystal structure of phosphatidylinositol-specific phospholipase C from Bacillus cereus in complex with glucosaminyl(alpha 1-->6)-D-myo-inositol, an essential fragment of GPI anchors.
references: Synthesis, structure-activity relationships, and the effect of polyethylene glycol on inhibitors of phosphatidylinositol-specific phospholipase C from Bacillus cereus.
references: Inhibition of phosphatidylinositol-specific phospholipase C: studies on synthetic substrates, inhibitors and a synthetic enzyme.
references: Phospholipid signalling. Taking stock of PI-PLC.
references: Structural views of phosphoinositide-specific phospholipase C: signalling the way ahead.
references: Probing the roles of active site residues in phosphatidylinositol-specific phospholipase C from Bacillus cereus by site-directed mutagenesis.
references: Phosphatidylinositol-specific phospholipase C: kinetic and stereochemical evidence for an interaction between arginine-69 and the phosphate group of phosphatidylinositol.
references: Short-chain phosphatidylinositol conformation and its relevance to phosphatidylinositol-specific phospholipase C.
references: Allosteric activation of phosphatidylinositol-specific phospholipase C: specific phospholipid binding anchors the enzyme to the interface.
references: Activation of phosphatidylinositol-specific phospholipase C toward inositol 1,2-(cyclic)-phosphate.
references: Crystal structure of the phosphatidylinositol-specific phospholipase C from the human pathogen Listeria monocytogenes.
references: Determination of pKa values of the histidine side chains of phosphatidylinositol-specific phospholipase C from Bacillus cereus by NMR spectroscopy and site-directed mutagenesis.
references: Mechanism of phosphatidylinositol-specific phospholipase C: a unified view of the mechanism of catalysis.
references: Structural and mechanistic comparison of prokaryotic and eukaryotic phosphoinositide-specific phospholipases C.
references: Bacterial phosphatidylinositol-specific phospholipase C: structure, function, and interaction with lipids.
references: Mutagenesis of active-site histidines of Listeria monocytogenes phosphatidylinositol-specific phospholipase C: effects on enzyme activity and biological function.
references: Involvement of the Arg-Asp-His catalytic triad in enzymatic cleavage of the phosphodiester bond.
references: A catalytic diad involved in substrate-assisted catalysis: NMR study of hydrogen bonding and dynamics at the active site of phosphatidylinositol-specific phospholipase C.
references: N-terminal EF-hand-like domain is required for phosphoinositide-specific phospholipase C activity in Arabidopsis thaliana.
references: Role of tryptophan residues in interfacial binding of phosphatidylinositol-specific phospholipase C.
references: Engineering a catalytic metal binding site into a calcium-independent phosphatidylinositol-specific phospholipase C leads to enhanced stereoselectivity.
references: Water-miscible organic cosolvents enhance phosphatidylinositol-specific phospholipase C phosphotransferase as well as phosphodiesterase activity.
references: Application of Bronsted-type LFER in the study of the phospholipase C mechanism.
references: X-ray structure of the R69D phosphatidylinositol-specific phospholipase C enzyme: insight into the role of calcium and surrounding amino acids in active site geometry and catalysis.
references: Dimer structure of an interfacially impaired phosphatidylinositol-specific phospholipase C.
comment: This enzyme was transferred from E.C. 3.1.4.10 to 4.6.1.13. This enzyme catalyzes the following reactions: (A) Intramolecular phosphotransfer reaction: (B) Hydrolysis: However, the activity of hydrolysis reaction is very low, according to the literature [25], [26]. The first reaction of this enzyme proceeds as follows: (1) Asp274 modulates the activity of a general base, His32. (2) His32 acts as a general base to deprotonate and activate 2-OH group of 1-Phosphatidyl-D-myo-inositol. (3) The activated hydroxyl group makes a nucleophilic attack on the phosphate group of the substrate, forming a pentacovalent transition state. (4) The negatively charged transition-state is stabilized by Arg69, which is modulated and oriented by Asp33. (5) Asp33 also modulates the activity of the general acid, His82. (6) His32 acts as a general acid to protonate the leaving group, completing the reaction.

TIM Barrel
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.20.20.190
catalytic domain: index.html

Inositol phosphate metabolism
type: KeggPathway
references: KEGG:MAP00562

1-Phosphatidyl-D-myo-inositol
type: KeggSubstrate
references: KEGG:C01194
compound type: carbohydrate
compound type: lipid
compound type: phosphate group/phosphate ion

D-myo-Inositol 1,2-cyclic phosphate
type: KeggProduct
references: KEGG:C04299
compound type: carbohydrate
compound type: phosphate group/phosphate ion
references: CHEBI:18426
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Diacylglycerol
type: KeggProduct
references: KEGG:C00165
compound type: carbohydrate
compound type: lipid

1aodA
type: Pdb
references: 1aod
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aod
catalytic residue: HIS 45;ASP 46;ARG 84;HIS 93;ASP 278

2plcA
type: Pdb
references: 2plc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2plc
catalytic residue: HIS 45;ASP 46;ARG 84;HIS 93;ASP 278

1gymA
type: Pdb
references: 1gym
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gym
catalytic residue: HIS 32;ASP 33;ARG 69;HIS 82;ASP 274

1ptdA
type: Pdb
references: 1ptd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ptd
catalytic residue: HIS 32;ASP 33;ARG 69;HIS 82;ASP 274

1ptgA
type: Pdb
references: 1ptg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ptg
catalytic residue: HIS 32;ASP 33;ARG 69;HIS 82;ASP 274

2ptdA
type: Pdb
references: 2ptd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2ptd
catalytic residue: HIS 32;ASP 33;ARG 69;HIS 82;ASP 274

3ptdA
type: Pdb
references: 3ptd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3ptd
catalytic residue: HIS 32;ASP 33;ARG 69;HIS 82;
comment: mutant D274S

4ptdA
type: Pdb
references: 4ptd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4ptd
catalytic residue: HIS 32;ASP 33;ARG 69;HIS 82;
comment: mutant D274N

5ptdA
type: Pdb
references: 5ptd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:5ptd
catalytic residue: ;ASP 33;ARG 69;HIS 82;ASP 274
comment: mutant H32A

6ptdA
type: Pdb
references: 6ptd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:6ptd
catalytic residue: ;ASP 33;ARG 69;HIS 82;ASP 274
comment: mutant H32L

7ptdA
type: Pdb
references: 7ptd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:7ptd
catalytic residue: HIS 32;ASP 33;ARG 69;HIS 82;ASP 274
comment: mutant R163K

1t6mA
type: Pdb
references: 1t6m
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1t6m
catalytic residue: HIS 36;ASP 37; ;HIS 86;ASP 278
comment: mutant R73D

1t6mB
type: Pdb
references: 1t6m
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1t6m
catalytic residue: HIS 36;ASP 37; ;HIS 86;ASP 278
comment: mutant R73D

2or2A
type: Pdb
references: 2or2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2or2
catalytic residue: HIS 32;ASP 33;ARG 69;HIS 82;ASP 274

2or2B
type: Pdb
references: 2or2
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2or2
catalytic residue: HIS 32;ASP 33;ARG 69;HIS 82;ASP 274

Phospholipids chiral at phosphorus. Stereochemical mechanism of reactions catalyzed by phosphatidylinositide-specific phospholipase C from Bacillus cereus and guinea pig uterus.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2161255
journal: Biochemistry
volume: 29
pages: 2747-57
published year: 1990
authors:
  item: Lin GL
  item: Bennett CF
  item: Tsai MD

Divalent cation regulation of phosphoinositide metabolism. Naturally occurring B lymphoblasts contain a Mg2(+)-regulated phosphatidylinositol-specific phospholipase C.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2160965
journal: J Biol Chem
volume: 265
pages: 9201-7
published year: 1990
authors:
  item: Chien MM
  item: Cambier JC

A chromogenic substrate for phosphatidylinositol-specific phospholipase C: 4-nitrophenyl myo-inositol-1-phosphate.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1814635
journal: Chem Phys Lipids
volume: 60
pages: 101-10
published year: 1991
authors:
  item: Shashidhar MS
  item: Volwerk JJ
  item: Griffith OH
  item: Keana JF

Phospholipase stereospecificity at phosphorus.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1646930
journal: Methods Enzymol
volume: 197
pages: 258-69
published year: 1991
authors:
  item: Bruzik KS
  item: Tsai MD

Phospholipids chiral at phosphorus. Stereochemical mechanism for the formation of inositol 1-phosphate catalyzed by phosphatidylinositol-specific phospholipase C.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1318746
journal: Biochemistry
volume: 31
pages: 5183-93
published year: 1992
authors:
  item: Bruzik KS
  item: Morocho AM
  item: Jhon DY
  item: Rhee SG
  item: Tsai MD

Substrate requirements of bacterial phosphatidylinositol-specific phospholipase C.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8395883
journal: Biochemistry
volume: 32
pages: 8836-41
published year: 1993
authors:
  item: Lewis KA
  item: Garigapati VR
  item: Zhou C
  item: Roberts MF

Crystallization of phosphatidylinositol-specific phospholipase C from Bacillus cereus.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8386017
journal: Biophys J
volume: 64
pages: 784-91
published year: 1993
authors:
  item: Bullock TL
  item: Ryan M
  item: Kim SL
  item: Remington SJ
  item: Griffith OH

Phosphatidylinositol-specific phospholipase C from Bacillus cereus at the lipid-water interface: interfacial binding, catalysis, and activation.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8142343
journal: Biochemistry
volume: 33
pages: 3464-74
published year: 1994
authors:
  item: Volwerk JJ
  item: Filthuth E
  item: Griffith OH
  item: Jain MK

src-homology 2 (SH2) domain ligation as an allosteric regulator: modulation of phosphoinositide-specific phospholipase C gamma 1 structure and activity.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7531435
journal: Biochem J
volume: 305
pages: 745-51
published year: 1995
authors:
  item: Koblan KS
  item: Schaber MD
  item: Edwards G
  item: Gibbs JB
  item: Pompliano DL

Crystal structure of the phosphatidylinositol-specific phospholipase C from Bacillus cereus in complex with myo-inositol.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
medline id: 95393962
references: http://www.ncbi.nlm.nih.gov/pubmed/7664726
journal: EMBO J
volume: 14
pages: 3855-63
published year: 1995
authors:
  item: Heinz DW
  item: Ryan M
  item: Bullock TL
  item: Griffith OH
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P14262

Mechanism and structure based inhibitors of phospholipase C enzymes.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8869740
journal: Adv Enzyme Regul
volume: 36
pages: 57-71
published year: 1996
authors:
  item: Roberts MF
  item: Wu Y
  item: Zhou C
  item: Geng D
  item: Tan C

Crystal structure of phosphatidylinositol-specific phospholipase C from Bacillus cereus in complex with glucosaminyl(alpha 1-->6)-D-myo-inositol, an essential fragment of GPI anchors.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
medline id: 96302248
references: http://www.ncbi.nlm.nih.gov/pubmed/8755729
journal: Biochemistry
volume: 35
pages: 9496-504
published year: 1996
authors:
  item: Heinz DW
  item: Ryan M
  item: Smith MP
  item: Weaver LH
  item: Keana JF
  item: Griffith OH
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P14262

Synthesis, structure-activity relationships, and the effect of polyethylene glycol on inhibitors of phosphatidylinositol-specific phospholipase C from Bacillus cereus.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8893831
journal: J Med Chem
volume: 39
pages: 4366-76
published year: 1996
authors:
  item: Ryan M
  item: Smith MP
  item: Vinod TK
  item: Lau WL
  item: Keana JF
  item: Griffith OH

Inhibition of phosphatidylinositol-specific phospholipase C: studies on synthetic substrates, inhibitors and a synthetic enzyme.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8877813
journal: J Mol Recognit
volume: 9
pages: 197-209
published year: 1996
authors:
  item: Vizitiu D
  item: Kriste AG
  item: Campbell AS
  item: Thatcher GR

Phospholipid signalling. Taking stock of PI-PLC.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8602254
journal: Nature
volume: 380
pages: 581-3
published year: 1996
authors:
  item: Irvine R

Structural views of phosphoinositide-specific phospholipase C: signalling the way ahead.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8994965
journal: Structure
volume: 4
pages: 1387-94
published year: 1996
authors:
  item: Williams RL
  item: Katan M

Probing the roles of active site residues in phosphatidylinositol-specific phospholipase C from Bacillus cereus by site-directed mutagenesis.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
medline id: 97477327
references: http://www.ncbi.nlm.nih.gov/pubmed/9335537
journal: Biochemistry
volume: 36
pages: 12802-13
published year: 1997
authors:
  item: Gassler CS
  item: Ryan M
  item: Liu T
  item: Griffith OH
  item: Heinz DW
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P14262

Phosphatidylinositol-specific phospholipase C: kinetic and stereochemical evidence for an interaction between arginine-69 and the phosphate group of phosphatidylinositol.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9184143
journal: Biochemistry
volume: 36
pages: 6633-42
published year: 1997
authors:
  item: Hondal RJ
  item: Riddle SR
  item: Kravchuk AV
  item: Zhao Z
  item: Liao H
  item: Bruzik KS
  item: Tsai MD

Short-chain phosphatidylinositol conformation and its relevance to phosphatidylinositol-specific phospholipase C.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9398326
journal: Biochemistry
volume: 36
pages: 15925-31
published year: 1997
authors:
  item: Zhou C
  item: Garigapati V
  item: Roberts MF

Allosteric activation of phosphatidylinositol-specific phospholipase C: specific phospholipid binding anchors the enzyme to the interface.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9254604
journal: Biochemistry
volume: 36
pages: 10089-97
published year: 1997
authors:
  item: Zhou C
  item: Qian X
  item: Roberts MF

Activation of phosphatidylinositol-specific phospholipase C toward inositol 1,2-(cyclic)-phosphate.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9003187
journal: Biochemistry
volume: 36
pages: 347-55
published year: 1997
authors:
  item: Zhou C
  item: Wu Y
  item: Roberts MF

Crystal structure of the phosphatidylinositol-specific phospholipase C from the human pathogen Listeria monocytogenes.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 43-317.
medline id: 98035056
references: http://www.ncbi.nlm.nih.gov/pubmed/9367761
journal: J Mol Biol
volume: 273
pages: 269-82
published year: 1997
authors:
  item: Moser J
  item: Gerstel B
  item: Meyer JE
  item: Chakraborty T
  item: Wehland J
  item: Heinz DW
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P34024

Determination of pKa values of the histidine side chains of phosphatidylinositol-specific phospholipase C from Bacillus cereus by NMR spectroscopy and site-directed mutagenesis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9300493
journal: Protein Sci
volume: 6
pages: 1937-44
published year: 1997
authors:
  item: Liu T
  item: Ryan M
  item: Dahlquist FW
  item: Griffith OH

Mechanism of phosphatidylinositol-specific phospholipase C: a unified view of the mechanism of catalysis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9521777
journal: Biochemistry
volume: 37
pages: 4568-80
published year: 1998
authors:
  item: Hondal RJ
  item: Zhao Z
  item: Kravchuk AV
  item: Liao H
  item: Riddle SR
  item: Yue X
  item: Bruzik KS
  item: Tsai MD

Structural and mechanistic comparison of prokaryotic and eukaryotic phosphoinositide-specific phospholipases C.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9466937
journal: J Mol Biol
volume: 275
pages: 635-50
published year: 1998
authors:
  item: Heinz DW
  item: Essen LO
  item: Williams RL

Bacterial phosphatidylinositol-specific phospholipase C: structure, function, and interaction with lipids.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10570252
journal: Biochim Biophys Acta
volume: 1441
pages: 237-54
published year: 1999
authors:
  item: Griffith OH
  item: Ryan M

Mutagenesis of active-site histidines of Listeria monocytogenes phosphatidylinositol-specific phospholipase C: effects on enzyme activity and biological function.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9864213
journal: Infect Immun
volume: 67
pages: 182-6
published year: 1999
authors:
  item: Bannam T
  item: Goldfine H

Involvement of the Arg-Asp-His catalytic triad in enzymatic cleavage of the phosphodiester bond.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11331006
journal: Biochemistry
volume: 40
pages: 5422-32
published year: 2001
authors:
  item: Kubiak RJ
  item: Yue X
  item: Hondal RJ
  item: Mihai C
  item: Tsai MD
  item: Bruzik KS

A catalytic diad involved in substrate-assisted catalysis: NMR study of hydrogen bonding and dynamics at the active site of phosphatidylinositol-specific phospholipase C.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11583175
journal: Biochemistry
volume: 40
pages: 9743-50
published year: 2001
authors:
  item: Ryan M
  item: Liu T
  item: Dahlquist FW
  item: Griffith OH

N-terminal EF-hand-like domain is required for phosphoinositide-specific phospholipase C activity in Arabidopsis thaliana.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11377433
journal: FEBS Lett
volume: 497
pages: 165-70
published year: 2001
authors:
  item: Otterhag L
  item: Sommarin M
  item: Pical C

Role of tryptophan residues in interfacial binding of phosphatidylinositol-specific phospholipase C.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11912206
journal: J Biol Chem
volume: 277
pages: 19867-75
published year: 2002
authors:
  item: Feng J
  item: Wehbi H
  item: Roberts MF

Engineering a catalytic metal binding site into a calcium-independent phosphatidylinositol-specific phospholipase C leads to enhanced stereoselectivity.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12600209
journal: Biochemistry
volume: 42
pages: 2422-30
published year: 2003
authors:
  item: Kravchuk AV
  item: Zhao L
  item: Bruzik KS
  item: Tsai MD

Water-miscible organic cosolvents enhance phosphatidylinositol-specific phospholipase C phosphotransferase as well as phosphodiesterase activity.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12832083
journal: Biochim Biophys Acta
volume: 1613
pages: 15-27
published year: 2003
authors:
  item: Wehbi H
  item: Feng J
  item: Roberts MF

Application of Bronsted-type LFER in the study of the phospholipase C mechanism.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12630878
journal: J Am Chem Soc
volume: 125
pages: 3236-42
published year: 2003
authors:
  item: Mihai C
  item: Kravchuk AV
  item: Tsai MD
  item: Bruzik KS

X-ray structure of the R69D phosphatidylinositol-specific phospholipase C enzyme: insight into the role of calcium and surrounding amino acids in active site geometry and catalysis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/16042375
journal: Biochemistry
volume: 44
pages: 9980-9
published year: 2005
authors:
  item: Apiyo D
  item: Zhao L
  item: Tsai MD
  item: Selby TL

Dimer structure of an interfacially impaired phosphatidylinositol-specific phospholipase C.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/17213187
journal: J Biol Chem
volume: 282
pages: 9228-35
published year: 2007
authors:
  item: Shao C
  item: Shi X
  item: Wehbi H
  item: Zambonelli C
  item: Head JF
  item: Seaton BA
  item: Roberts MF

Analogue
compound: 1-Phosphatidyl-D-myo-inositol
pdb: 1gymA
ligand het code: MYG

Analogue
compound: D-myo-Inositol 1,2-cyclic phosphate
pdb: 1aodA
ligand het code: INS

Analogue
compound: D-myo-Inositol 1,2-cyclic phosphate
pdb: 1ptgA
ligand het code: INS

ReferenceForCatalyticMechanism
reference index: 1
reference section: Scheme III, Scheme IV, p.2755
reference step: 1

ReferenceForCatalyticMechanism
reference index: 4
reference section: p.5189-5192

ReferenceForCatalyticMechanism
reference index: 5
reference section: Scheme VIII, p.5191
reference step: 2

ReferenceForCatalyticMechanism
reference index: 10
reference section: Fig. 8, p.3860
reference step: 4

ReferenceForCatalyticMechanism
reference index: 12
reference section: p.9502

ReferenceForCatalyticMechanism
reference index: 14
reference section: Fig. 1

ReferenceForCatalyticMechanism
reference index: 16
reference section: p.1391

ReferenceForCatalyticMechanism
reference index: 17
reference section: Fig.8, p.12810-12812
reference step: 2

ReferenceForCatalyticMechanism
reference index: 18
reference section: Fig.1, p.6641
reference step: 2

ReferenceForCatalyticMechanism
reference index: 22
reference section: Fig. 1, p.277-278
reference step: 2

ReferenceForCatalyticMechanism
reference index: 23
reference section: Fig. 1, p.1940-1943
reference step: 2

ReferenceForCatalyticMechanism
reference index: 24
reference section: Fig. 1, Fig. 2, Fig. 9, p.4577-4578

ReferenceForCatalyticMechanism
reference index: 25
reference section: Fig. 7, p.644-645

ReferenceForCatalyticMechanism
reference index: 26
reference section: Fig. 7, p.245-249
reference step: 2

ReferenceForCatalyticMechanism
reference index: 28
reference section: Scheme I, Fig. 1, Fig. 4, p.5428-5431
reference step: 2

ReferenceForCatalyticMechanism
reference index: 29
reference section: Fig. 5, Fig. 6, p.9749-9750
reference step: 2

ReferenceForCatalyticMechanism
reference index: 32
reference section: Fig. 1, Fig. 2, p.2426-2429
reference step: 2

ReferenceForCatalyticMechanism
reference index: 34
reference section: Fig. 7, p.3242

ReferenceForCatalyticMechanism
reference index: 35
reference section: Scheme 1, p.9984-9988