4.6.1.13: phosphatidylinositol diacylglycerol-lyase

This is an abbreviated version!
For detailed information about phosphatidylinositol diacylglycerol-lyase, go to the full flat file.

Reaction

Synonyms

1-phosphatidyl-D-myo-inositol inositolphosphohydrolase (cyclic-phosphate-forming), 1-phosphatidylinositol phosphodiesterase, EC 3.1.4.10, monophosphatidylinositol phosphodiesterase, More, Phosphatidylinositol diacylglycerol-lyase, phosphatidylinositol phosphodiesterase, phosphatidylinositol phospholipase C, phosphatidylinositol-specific phospholipase C, phosphatidylinositol-specific PLC, phosphatidylinositolphospholipase C, PI-phospholipase C, PI-PLC, PLC, PLC1, PLC2, PLC3, PLC4, PLC5, PLC6

ECTree

     4 Lyases

         4.6 Phosphorus-oxygen lyases

             4.6.1 Phosphorus-oxygen lyases (only sub-subclass identified to date)

                4.6.1.13 phosphatidylinositol diacylglycerol-lyase

Advanced search results

Do not include text mining results

Include results (more...)

Include results (more...)

Results	in table
35	Activating Compound
2774	AA Sequence
6	Application
2	CAS Registry Number
18	Cloned(Commentary)
8	Crystallization (Commentary)
4	Expression
10	General Information
1	General Stability
26	Inhibitors
4	Ki Value [mM]
9	KM Value [mM]
8	Localization
15	Metals/Ions
12	Molecular Weight [Da]
13	Natural Substrates/ Products (Substrates)
2	Organic Solvent Stability
50	Organism
2	Pathway
27	PDB ID
14	pH Optimum
2	pH Range
1	pI Value
98	Protein Variants
20	Purification (Commentary)
7	Reaction
1	Reaction Type
47	Reference
2	Source Tissue
40	Specific Activity [micromol/min/mg]
1	Storage Stability
63	Substrates and Products (Substrate)
8	Subunits
57	Synonyms
1	Systematic Name
7	Temperature Optimum [°C]
1	Temperature Range [°C]
11	Temperature Stability [°C]
2	Turnover Number [1/s]

Crystallization

print visible entries

print all entries

Go back to the abbreviated version
of the Enzyme Summary Page.

Crystallization on EC 4.6.1.13 - phosphatidylinositol diacylglycerol-lyase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

top print hide Go to Crystallization (commentary) Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

-

Bacillus cereus

-

285236

in complex with myo-inositol

Bacillus cereus

-

285242

X-ray crystal structure

Bacillus cereus

-

650093

mutant Y247S/Y251S in the absence and presence of myo-inositol as well as mutant Y246S/Y247S/Y248S/Y251S, both mutant proteins crystallize as monomers, are very similar to one another, and have no change in the active site region

Bacillus thuringiensis

P08954

709019

wild-type and D274N mutant PI-PLC

Bacillus thuringiensis

-

652552

-

Listeria monocytogenes

-

285241

recombinant PI-PLC

Listeria monocytogenes

-

650573

purified recombinant wild-type enzyme and mutant Y253S complexed with 1,2-dibutyroyl-sn-glycero-3-phosphocholine, hanging drop vapour diffusion method, mixing of 0.0015 ml of 10 mg/ml protein, 50 mM myo-inositol and 2.5 mM 1,2-dibutyroyl-sn-glycero-3-phosphocholine, with 0.0015 ml of reservoir solution containing 150 mM ammonium acetate, 100 mM sodium acetate, pH 4.6, with 1 mM Mg(NO3)2 (100 mM for the mutant enzymes), and 16-20% PEG 4000, 20°C, 2 weeks, X-ray diffraction structure determination and analysis at 2.16-2.3 A resolution

Staphylococcus aureus

P45723

730001