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Information on EC 3.1.4.3 - phospholipase C and Organism(s) Bacillus cereus and UniProt Accession P09598
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3.1.4.3 phospholipase CIUBMB Comments
The bacterial enzyme, which is a zinc protein, also acts on sphingomyelin and phosphatidylinositol; that from seminal plasma does not act on phosphatidylinositol.
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Word Map
- 3.1.4.3
- inositol
- agonist
- phosphatidylinositol
- pkc
- phospholipid
- diacylglycerol
- phosphoinositide
- cyclase
- pertussis
- camp
-
phorbol
- g-proteins
- platelet
-
arachidonic
- 1,4,5-trisphosphate
- 4,5-bisphosphate
-
receptor-mediated
- vibrio
- thapsigargin
- trisphosphate
- adenylate
-
protein-coupled
-
blocker
-
adenylyl
- phospholipases
-
muscarinic
-
phosphatidic
- cereus
- carbachol
- perfringens
- pip2
-
fura-2
- neomycin
-
ca2+-free
-
phosphatidylinositol-specific
-
metabotropic
-
13-acetate
-
thromboxane
- nifedipine
- parahaemolyticus
- staurosporine
- bradykinin
- enterotoxin
-
desensitization
-
ryanodine
-
prelabeled
-
toxin-sensitive
-
store-operated
- chelerythrine
-
agonist-induced
- analysis
- drug development
- medicine
- food industry
- pharmacology
The taxonomic range for the selected organisms is: Bacillus cereus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
phospholipase c, plc, hemolysin, pc-plc, lecithinase, phosphatidylcholine-specific phospholipase c, plcbeta, plcg2, beta toxin, plcg1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-toxin
-
-
-
-
Beta toxin
-
-
-
-
Beta-hemolysin
-
-
-
-
Beta-toxin
-
-
-
-
Cbp
-
-
-
-
Clostridium oedematiens beta- and gamma-toxins
-
-
-
-
Clostridium welchii alpha-toxin
-
-
-
-
Gamma-toxin
-
-
-
-
Heat labile-hemolysin
-
-
-
-
heat-labile hemolysin
-
-
-
-
Hemolysin
-
-
-
-
Lecithinase
-
-
-
-
lecithinase C
-
-
-
-
lipophosphodiesterase C
-
-
-
-
lipophosphodiesterase I
-
-
-
-
MTP40 antigen
-
-
-
-
PC-PLC
phosphatidase C
-
-
-
-
Phosphatidylcholine cholinephosphohydrolase
-
-
-
-
PLC
SMase
-
-
-
-
sphingomyelinase
-
-
-
-
PC-PLC
-
-
-
-
PLC
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
phosphatidylcholine cholinephosphohydrolase
The bacterial enzyme, which is a zinc protein, also acts on sphingomyelin and phosphatidylinositol; that from seminal plasma does not act on phosphatidylinositol.
CAS REGISTRY NUMBER
COMMENTARY
9001-86-9
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,2-dihexanoyl-sn-glycero-3-phospho-L-serine + H2O
1,2-dihexanoyl-sn-glycerol + phosphorylserine
-
-
?
1,2-dihexanoyl-sn-glycero-3-phosphocholine + H2O
1,2-dihexanoyl-sn-glycerol + phosphorylcholine
-
-
?
1,2-dihexanoyl-sn-glycero-3-phosphoethanolamine + H2O
1,2-dihexanoyl-sn-glycerol + phosphoethanolamine
-
-
?
1,2-dicaproylphosphatidylcholine + H2O
1,2-dicaproylglycerol + phosphorylcholine
-
-
-
?
1,2-dihexanoyl-sn-glycero-3-phosphoethanolamine + H2O
1,2-dihexanoyl-sn-glycerol + phosphoethanolamine
-
less efficient substrate
-
-
?
1,2-dimyristoylphosphatidylcholine + H2O
1,2-dimyristoylglycerol + phosphorylcholine
-
-
-
?
1,2-dipalmitoylphosphatidylcholine + H2O
1,2-dipalmitoylglycerol + phosphorylcholine
-
-
-
?
1,2-dipalmitoylphosphatidylethanolamine + H2O
1,2-dipalmitoylglycerol + phosphorylethanolamine
-
-
-
?
1-O-(6-(p-methyl red)-amino-hexanoyl)-2-O-(12-(p-methyl red)-amino-dodecanoyl)-sn-glyceryl-N-(3-(5-BODIPY-pentanoyl)-amino-propyl)-N,Ndimethyl-phosphatidylethanolamine + H2O
?
-
fluorogenic analogue of phosphatidylcholine, direct substrate for real-time measurement of enzyme activity
-
-
?
4-nitrophenylphosphorylcholine + H2O
4-nitrophenol + phosphorylcholine
-
-
-
-
?
cardiolipin + H2O
phosphatidylglycerophosphate + 1,2-diacylglycerol
-
-
-
?
diheptanoylphosphatidylcholine + H2O
diheptanoylglycerol + phosphorylcholine
-
-
-
?
dihexanoylphosphatidylcholine + H2O
dihexanoylglycerol + phosphorylcholine
-
-
-
?
dimyristoylphosphatidylcholine + H2O
dimyristoylglycerol + phosphorylcholine
-
substrate in mixed micelles with sodium deoxycholate
-
-
?
p-nitrophenylphosphorylcholine + H2O
p-nitrophenol + phosphorylcholine
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + choline phosphate
-
-
-
-
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
-
-
-
?
phosphatidylethanolamine + H2O
1,2-sn-diacylglycerol + phosphoethanolamine
-
-
-
-
?
phosphatidylglycerol + H2O
1,2-diacylglycerol + sn-glycerol-3-phosphate
-
-
-
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + phosphorylcholine
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + phosphorylcholine
-
preferred substrate
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylethanolamine + H2O
phosphorylethanolamine + diacylglycerol
-
-
-
?
phosphatidylethanolamine + H2O
phosphorylethanolamine + diacylglycerol
-
-
-
?
phosphatidylethanolamine + H2O
phosphorylethanolamine + diacylglycerol
-
-
-
?
phosphatidylethanolamine + H2O
phosphorylethanolamine + diacylglycerol
-
-
-
?
phosphatidylethanolamine + H2O
phosphorylethanolamine + diacylglycerol
-
-
-
-
?
phosphatidylinositol + H2O
inositol monophosphate + diacylglycerol
-
-
-
?
phosphatidylinositol + H2O
inositol monophosphate + diacylglycerol
-
-
-
?
sphingomyelin + H2O
ceramide + phosphorylcholine
-
when substrate is presented in a biological membrane, for example in the human red cell membrane or myelin sheath
-
?
additional information
?
-
-
PLCBC also catalyzes the hydrolysis of phosphatidylethanolamine and phosphatidylserine but with lower efficiency
-
-
?
additional information
?
-
-
modeling of active site and reaction mechanism, development of two different reaction mechanism models, overview
-
-
?
additional information
?
-
-
phospholipase C can catalyze the membrane fusion between cell membranes and phospholipid vehicles (liposomes) at pH 4.0-7.5, highest activity at pH 5.0, 37°C. The liposomes are composed of 1,2-dioleoyl-sn-glycero-3-phosphocholine, 1,2-dipalmitoyl-sn-glycero-3-phosphocholine, and cholesterol in a 1:1:1 molar ratio, membrane fusion is dependent of the lipid composition, overview. The enzyme takes a molten-globule state, with a large fluctuation at acidic pH, mechanism of enzyme-induced membrane fusion
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + choline phosphate
-
-
-
-
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
-
-
-
?
phosphatidylethanolamine + H2O
1,2-sn-diacylglycerol + phosphoethanolamine
-
-
-
-
?
additional information
?
-
-
PLCBC also catalyzes the hydrolysis of phosphatidylethanolamine and phosphatidylserine but with lower efficiency
-
-
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + phosphorylcholine
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + phosphorylcholine
-
preferred substrate
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
Zn2+
-
phospholipase C is a trinuclear zinc enzyme, structure analysis, using also the crystal structure from PDB entry 1AH7, overview
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-[hydroxy[2-(trimethylammonio)ethyl]amino]-1-oxododecan-2-aminium
-
uncompetitive inhibition
1-[hydroxy[3-(trimethylammonio)propyl]amino]-1-oxododecan-2-aminium
-
mixed type inhibition
2-[(benzyloxy)[2-[(tert-butoxycarbonyl)amino]dodecanoyl]amino]-N,N,N-trimethylethanaminium
-
-
2-[(benzyloxy)[2-[(tert-butoxycarbonyl)amino]hexadecanoyl]amino]-N,N,N-trimethylethanaminium
-
-
2-[(benzyloxy)[2-[(tert-butoxycarbonyl)amino]icosanoyl]amino]-N,N,N-trimethylethanaminium
-
-
2-[(benzyloxy)[2-[(tert-butoxycarbonyl)amino]octanoyl]amino]-N,N,N-trimethylethanaminium
-
-
3(S),4-dihexanoylbutyl-1-phosphonycholine
-
non-hydrolyzable, competitive inhibitor of bacterial PLC, analog of the natural phospholipid substrate, binds with its phosphonyl group to the three Zn-ions in the active site of the enzyme
3-[(benzyloxy)[2-[(tert-butoxycarbonyl)amino]dodecanoyl]amino]-N,N,N-trimethylpropan-1-aminium
-
mixed type inhibition
3-[(benzyloxy)[2-[(tert-butoxycarbonyl)amino]octanoyl]amino]-N,N,N-trimethylpropan-1-aminium
-
-
tert-butyl (1-[(benzyloxy)[3-(dimethylamino)propyl]amino]-1-oxododecan-2-yl)carbamate
-
noncompetitive inhibition
tert-butyl (1-[(benzyloxy)[3-(dimethylamino)propyl]amino]-1-oxooctan-2-yl)carbamate
-
-
o-phenanthroline
-
inhibits the phospholipase C hydrolytic activity of the enzyme, but not its membrane fusion activity
additional information
-
PC-PLCBc inhibition is not due to the interaction of compounds with the phospholipase catalytic zinc atoms, but rather results from the inhibitor cationic group recognition by the PCPLCBc amino acids involved in choline lipid binding. Inhibitor design based on 2-aminohydroxamic acid PC-PLCBc inhibitors that block the enzyme by coordination of the zinc active site atoms present in PC-PLCBc, overview
-
additional information
-
excess diacylglycerol at pH 7.5 at approximately 12% inhibits the membrane fusion activity of the enzyme
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetic parameters depend on the physicochemical properties of substrate aggregates. Larger micelles with a ratio bile salt/lipid smaller than 5 show higher activity and shorter steady state duration of less than 4 min, smaller micelles with a ratio bile salt/lipid greater than 5 show lower activity and longer steady state of about 10 min
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.012
1-[hydroxy[2-(trimethylammonio)ethyl]amino]-1-oxododecan-2-aminium
-
pH and temperature not specified in the publication
0.026
1-[hydroxy[3-(trimethylammonio)propyl]amino]-1-oxododecan-2-aminium
-
pH and temperature not specified in the publication
0.0025
3-[(benzyloxy)[2-[(tert-butoxycarbonyl)amino]dodecanoyl]amino]-N,N,N-trimethylpropan-1-aminium
-
pH and temperature not specified in the publication
0.0025
tert-butyl (1-[(benzyloxy)[3-(dimethylamino)propyl]amino]-1-oxododecan-2-yl)carbamate
-
pH and temperature not specified in the publication
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01
1-[(benzyloxy)[2-(trimethylammonio)ethyl]amino]-1-oxododecan-2-aminium
Bacillus cereus
-
pH and temperature not specified in the publication
0.004
1-[(benzyloxy)[2-(trimethylammonio)ethyl]amino]-1-oxohexadecan-2-aminium
Bacillus cereus
-
pH and temperature not specified in the publication
0.004
1-[(benzyloxy)[2-(trimethylammonio)ethyl]amino]-1-oxoicosan-2-aminium
Bacillus cereus
-
pH and temperature not specified in the publication
0.032
1-[(benzyloxy)[3-(dimethylammonio)propyl]amino]-1-oxododecan-2-aminium
Bacillus cereus
-
pH and temperature not specified in the publication
0.05
1-[(benzyloxy)[3-(trimethylammonio)propyl]amino]-1-oxododecan-2-aminium
Bacillus cereus
-
pH and temperature not specified in the publication
0.1
1-[(benzyloxy)[3-(trimethylammonio)propyl]amino]-1-oxooctan-2-aminium
Bacillus cereus
-
pH and temperature not specified in the publication
0.04
1-[hydroxy[2-(trimethylammonio)ethyl]amino]-1-oxododecan-2-aminium
Bacillus cereus
-
pH and temperature not specified in the publication
0.002
1-[hydroxy[2-(trimethylammonio)ethyl]amino]-1-oxohexadecan-2-aminium
Bacillus cereus
-
pH and temperature not specified in the publication
0.004
1-[hydroxy[2-(trimethylammonio)ethyl]amino]-1-oxoicosan-2-aminium
Bacillus cereus
-
pH and temperature not specified in the publication
0.5
1-[hydroxy[2-(trimethylammonio)ethyl]amino]-1-oxooctan-2-aminium
Bacillus cereus
-
pH and temperature not specified in the publication
0.058
1-[hydroxy[3-(trimethylammonio)propyl]amino]-1-oxododecan-2-aminium
Bacillus cereus
-
pH and temperature not specified in the publication
0.1
1-[[3-(dimethylammonio)propyl](hydroxy)amino]-1-oxododecan-2-aminium
Bacillus cereus
-
pH and temperature not specified in the publication
0.005
2-[(benzyloxy)[2-[(tert-butoxycarbonyl)amino]dodecanoyl]amino]-N,N,N-trimethylethanaminium
Bacillus cereus
-
pH and temperature not specified in the publication
0.002
2-[(benzyloxy)[2-[(tert-butoxycarbonyl)amino]hexadecanoyl]amino]-N,N,N-trimethylethanaminium
Bacillus cereus
-
pH and temperature not specified in the publication
0.003
2-[(benzyloxy)[2-[(tert-butoxycarbonyl)amino]icosanoyl]amino]-N,N,N-trimethylethanaminium
Bacillus cereus
-
pH and temperature not specified in the publication
0.056
2-[(benzyloxy)[2-[(tert-butoxycarbonyl)amino]octanoyl]amino]-N,N,N-trimethylethanaminium
Bacillus cereus
-
pH and temperature not specified in the publication
0.004
3-[(benzyloxy)[2-[(tert-butoxycarbonyl)amino]dodecanoyl]amino]-N,N,N-trimethylpropan-1-aminium
Bacillus cereus
-
pH and temperature not specified in the publication
0.078
3-[(benzyloxy)[2-[(tert-butoxycarbonyl)amino]octanoyl]amino]-N,N,N-trimethylpropan-1-aminium
Bacillus cereus
-
pH and temperature not specified in the publication
0.008
tert-butyl (1-[(benzyloxy)[3-(dimethylamino)propyl]amino]-1-oxododecan-2-yl)carbamate
Bacillus cereus
-
pH and temperature not specified in the publication
0.077
tert-butyl (1-[(benzyloxy)[3-(dimethylamino)propyl]amino]-1-oxooctan-2-yl)carbamate
Bacillus cereus
-
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
assay of enzyme in presence of organic solvent, two-phase-system
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
additional information
-
secondary and tertiary structure analysis of the enzyme at different pH values from pH 2.0-7.5, overview
physiological function
-
PC-PLC is an important enzyme that plays a key role in a variety of cellular events and lipid homoeostases
physiological function
-
the enzyme inhibits the formation of cAMP by adenylate cyclase and is involved in the defence mechanism of bacteria to phagocytosis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
-
secondary and tertiary structure analysis of the enzyme at different pH values from pH 2.0-7.5, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
2.1 A resolution for phosphate inhibited PLC, 2.8 A resolution for iodide and iodate-inhibited PLC, R-factor of 20.3%
-
crystal structure of a complex between the enzyme and a competitive inhibitor. 1.9 A resolution, R-factor of 15.7%
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F66W
-
the mutant enzyme can remove up to 90% of phosphatidylethanolamine while retaining its efficiency at hydrolyzing phosphatidylcholine
F66Y
-
the mutant enzyme can remove up to 90% of phosphatidylethanolamine while retaining its efficiency at hydrolyzing phosphatidylcholine
additional information
additional information
-
amino acid sequence differs from that of strain SBUG516 by substitution D173E
additional information
-
amino acid sequence differs from that of strain SBUG516 by substitution E173D
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
-
for 5 min, in 2 M guanidinium chloride, no loss of activity after dialysis against Zn2+-containing buffer
76
-
for 6 min, with 0.1 mM free Zn2+: loss of 21% of activity, without Zn2+: loss of 63% of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
guanidinium chloride, denaturation at a concentration of 1-2 M, reversible by free Zn2+
-
sodium dodecyl sulfate, enzyme resistant to denaturation in presence of 1 mM Zn2+
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
chloroform
-
assay of enzyme in presence of organic solvent, two-phase-system
diethyl ether
-
assay of enzyme in presence of organic solvent, two-phase-system
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, in barbital-buffered saline, pH 7.4, 1 mM ZnSO4, stable for more than one year
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, ethanol precipitate, protamine sulfate supernatant, gel filtration, ion-exchange chromatography, 450fold, approximately 98% pure
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
guanidinium chloride causes denaturation at a concentration of 1-2 M, reversible by free Zn2+
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
synthesis of fluorogenic analogue of phosphatidylcholine 1-O-(6-(p-methyl red)-amino-hexanoyl)-2-O-(12-(p-methyl red)-amino-dodecanoyl)-sn-glyceryl-N-(3-(5-BODIPY-pentanoyl)-amino-propyl)-N,Ndimethyl-phosphatidylethanolamine, and use as direct substrate for real-time measurement of enzyme activity. Substrate for both phospholipases C and D and lysophospholipase D, no substrate for Bacillus cereus PI-PLC or Clostridium perfringens PC-PLC
food industry
-
the enzyme is used in vegetable oil refining by enzymatic phospholipid removal (degumming )
medicine
-
inactivation of thromboplastin, potential therapeutic value in cases of intravascular coagulation
pharmacology
-
phospholipase C is considered to be one of key enzymes for the design of drug delivery system using the endocytosis route, because PLC can catalyze the membrane fusion between cell membranes and phospholipid vehicles (liposomes)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hanahan, D.J.
Phospholipases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
5
71-85
1971
Bacillus cereus, Clostridium perfringens, Clostridium welchii, Bacillus cereus 7004
-
Tan, C.A.; Roberts, M.F.
Engineering of the nonspecific phospholipase C from Bacillus cereus: Replacement of glutamic acid-4 by alanine results in loss of interfacial catalysis and enhanced phosphomonoesterase activity
Biochemistry
37
4275-4279
1998
Bacillus cereus
Little, C.
Phospholipase C from Bacillus cereus
Methods Enzymol.
71
725-730
1981
Bacillus cereus
-
Bjorklid, E.; Little, C.
The isoelectric point of phospholipase C from Bacillus cereus
FEBS Lett.
113
161-163
1980
Bacillus cereus
Little, C.; Johansen, S.
Unfolding and refolding of phospholipase C from Bacillus cereus in solutions of guanidinium chloride
Biochem. J.
179
509-514
1979
Bacillus cereus
Otnaess, A.B.; Little, C.; Sletten, K.; Wallin, R.; Johnsen, S.; Flengsrud, R.; Prydz, H.
Some characteristics of phospholipase C from Bacillus cereus
Eur. J. Biochem.
79
459-468
1977
Bacillus cereus
Zwaal, R.F.A.; Roelofsen, B.
Phospholipase C (phosphatidylcholine cholinephosphohydrolase, EC 3.1.4.3) from Bacillus cereus
Methods Enzymol.
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Bacillus cereus, Bacillus cereus 569/H
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Biochemistry
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Bacillus cereus (P09598), Bacillus cereus
Durban, M.A.; Silbersack, J.; Schweder, T.; Schauer, F.; Bornscheuer, U.T.
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Bacillus cereus, Bacillus cereus SBUG516, Bacillus cereus SBUG318
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Bacillus cereus
Liao, R.Z.; Yu, J.G.; Himo, F.
Reaction mechanism of the trinuclear zinc enzyme phospholipase C: a density functional theory study
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Bacillus cereus
Shimanouchi, T.; Kawasaki, H.; Fuse, M.; Umakoshi, H.; Kuboi, R.
Membrane fusion mediated by phospholipase C under endosomal pH conditions
Colloids Surf. B Biointerfaces
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Bacillus cereus
Pokotylo, I.; Pejchar, P.; Potocky, M.; Kocourkova, D.; Krckova, Z.; Ruelland, E.; Kravets, V.; Martinec, J.
The plant non-specific phospholipase C gene family. Novel competitors in lipid signalling
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Bacillus cereus, Clostridium perfringens, Glycine max, Nicotiana tabacum, Oryza sativa, Petunia x hybrida, Physcomitrium patens, Populus trichocarpa, Pseudomonas fluorescens, Sorghum bicolor, Ureaplasma urealyticum, Vitis vinifera, Picea sitchensis, Selaginella moellendorffii, Arabidopsis thaliana (O81020), Arabidopsis thaliana (Q8H965), Arabidopsis thaliana (Q8L7Y9), Arabidopsis thaliana (Q9S816), Arabidopsis thaliana (Q9SRQ6), Arabidopsis thaliana (Q9SRQ7)
Jiang, X.; Chang, M.; Jin, Q.; Wang, X.
Application of phospholipase A1 and phospholipase C in the degumming process of different kinds of crude oils
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Bacillus cereus
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Elena, C.; Ravasi, P.; Cerminati, S.; Peiru, S.; Castelli, M.; Menzella, H.
Pichia pastoris engineering for the production of a modified phospholipase C
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Elena, C.; Cerminati, S.; Ravasi, P.; Rasia, R.; Peiru, S.; Menzella, H.; Castelli, M.
B. cereus phospholipase C engineering for efficient degumming of vegetable oil
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Bacillus cereus
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