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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
-
-
-
?
diacylglycerylphosphoryl monomethylethanolamine + H2O
?
-
-
-
-
?
diheptanoylphosphatidylcholine + H2O
diheptanoylglycerol + phosphorylcholine
-
-
-
?
dihexanoylphosphatidic acid + H2O
?
-
-
-
-
?
dihexanoylphosphatidylcholine + H2O
dihexanoylglycerol + phosphorylcholine
-
-
-
?
dimyristoylphosphatidylcholine + H2O
dimyristoylglycerol + phosphorylcholine
-
substrate in mixed micelles with sodium deoxycholate
-
-
?
glucosaminylphosphatidylglycerol + H2O
?
-
-
-
-
?
p-nitrophenylphosphorylcholine + H2O
p-nitrophenol + phosphorylcholine
-
-
-
-
?
phosphatidic acid + H2O
?
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + choline phosphate
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + phosphorylcholine
phosphatidylcholine + H2O
1,2-diacylglycerol + choline phosphate
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
-
-
-
?
phosphatidylethanolamine + H2O
1,2-sn-diacylglycerol + phosphoethanolamine
-
-
-
-
?
phosphatidylethanolamine + H2O
phosphorylethanolamine + diacylglycerol
phosphatidylglycerol + H2O
1,2-diacylglycerol + sn-glycerol-3-phosphate
-
-
-
?
phosphatidylinositol + H2O
inositol monophosphate + diacylglycerol
phosphatidylserine + H2O
phosphorylserine + diacylglycerol
sphingomyelin + H2O
ceramide + phosphorylcholine
additional information
?
-
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
-
-
-
?
phosphatidylserine + H2O
phosphorylserine + diacylglycerol
-
-
-
?
phosphatidylserine + H2O
phosphorylserine + diacylglycerol
-
-
-
?
phosphatidylserine + H2O
phosphorylserine + diacylglycerol
-
-
-
?
phosphatidylserine + H2O
phosphorylserine + diacylglycerol
-
-
-
-
?
sphingomyelin + H2O
ceramide + phosphorylcholine
-
-
-
?
sphingomyelin + H2O
ceramide + phosphorylcholine
-
-
-
?
sphingomyelin + H2O
ceramide + phosphorylcholine
-
-
-
?
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
-
-
?
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phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + choline phosphate
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + phosphorylcholine
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
-
-
-
?
phosphatidylethanolamine + H2O
1,2-sn-diacylglycerol + phosphoethanolamine
-
-
-
-
?
sphingomyelin + H2O
ceramide + phosphorylcholine
-
-
-
?
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
-
-
-
?
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1-[(benzyloxy)[2-(trimethylammonio)ethyl]amino]-1-oxododecan-2-aminium
-
-
1-[(benzyloxy)[2-(trimethylammonio)ethyl]amino]-1-oxohexadecan-2-aminium
-
-
1-[(benzyloxy)[2-(trimethylammonio)ethyl]amino]-1-oxoicosan-2-aminium
-
-
1-[(benzyloxy)[2-(trimethylammonio)ethyl]amino]-1-oxooctan-2-aminium
-
-
1-[(benzyloxy)[3-(dimethylammonio)propyl]amino]-1-oxododecan-2-aminium
-
-
1-[(benzyloxy)[3-(dimethylammonio)propyl]amino]-1-oxooctan-2-aminium
-
-
1-[(benzyloxy)[3-(trimethylammonio)propyl]amino]-1-oxododecan-2-aminium
-
-
1-[(benzyloxy)[3-(trimethylammonio)propyl]amino]-1-oxooctan-2-aminium
-
-
1-[hydroxy[2-(trimethylammonio)ethyl]amino]-1-oxododecan-2-aminium
-
uncompetitive inhibition
1-[hydroxy[2-(trimethylammonio)ethyl]amino]-1-oxohexadecan-2-aminium
-
-
1-[hydroxy[2-(trimethylammonio)ethyl]amino]-1-oxoicosan-2-aminium
-
-
1-[hydroxy[2-(trimethylammonio)ethyl]amino]-1-oxooctan-2-aminium
-
-
1-[hydroxy[3-(trimethylammonio)propyl]amino]-1-oxododecan-2-aminium
-
mixed type inhibition
1-[hydroxy[3-(trimethylammonio)propyl]amino]-1-oxooctan-2-aminium
-
-
1-[[3-(dimethylammonio)propyl](hydroxy)amino]-1-oxododecan-2-aminium
-
-
1-[[3-(dimethylammonio)propyl](hydroxy)amino]-1-oxooctan-2-aminium
-
-
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
-
-
Cd2+
-
in absence of free Zn2+ in solution
Guanidinium chloride
-
denaturation
Ni2+
-
in absence of free Zn2+ in solution
phosphatidic acid
-
monomeric and micellar, poor substrate, inhibitor
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
-
-
tricyclodecan-9-ylxanthogenate
-
i.e. D609
Tris buffer
-
0.1 M Tris causes 50% inhibition
Cu2+
-
-
Cu2+
-
in absence of free Zn2+ in solution
o-phenanthroline
-
-
o-phenanthroline
-
denaturation
o-phenanthroline
-
inhibits the phospholipase C hydrolytic activity of the enzyme, but not its membrane fusion activity
Urea
-
denaturation
Urea
-
denaturation only in absence of free Zn2+
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
-
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4.5
1,2-dihexanoyl-sn-glycero-3-phospho-L-serine
pH 7.3
2.4
1,2-dihexanoyl-sn-glycero-3-phosphocholine
pH 7.3
1.8
1,2-dihexanoyl-sn-glycero-3-phosphoethanolamine
pH 7.3
0.6
1,2-dipalmitoylphosphatidylcholine
-
-
4.5 - 7
1,2-dipalmitoylphosphatidylethanolamine
-
-
14.8 - 39.5
4-nitrophenylphosphorylcholine
0.03 - 1.09
diheptanoylphosphatidylcholine
4.2 - 9
dihexanoylphosphatidic acid
0.19 - 1.12
dihexanoylphosphatidylcholine
0.38
phosphatidylcholine
-
water-soluble substrate
2 - 3
phosphatidylserine
-
-
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
-
14.8
4-nitrophenylphosphorylcholine
-
mutant enzyme F66W, at pH 7.0 and 50°C
17.4
4-nitrophenylphosphorylcholine
-
mutant enzyme F66Y, at pH 7.0 and 50°C
39.5
4-nitrophenylphosphorylcholine
-
wild type enzyme, at pH 7.0 and 50°C
0.03
diheptanoylphosphatidylcholine
-
micellar substrate, wild-type PLC
1.09
diheptanoylphosphatidylcholine
-
micellar substrate, recombinant PLC
4.2
dihexanoylphosphatidic acid
-
monomeric substrate, recombinant PLC
9
dihexanoylphosphatidic acid
-
monomeric substrate, wild-type PLC
0.19
dihexanoylphosphatidylcholine
-
monomeric substrate, wild-type PLC
1.12
dihexanoylphosphatidylcholine
-
monomeric substrate, recombinant PLC
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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
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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
-
brenda
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
brenda
Little, C.
Phospholipase C from Bacillus cereus
Methods Enzymol.
71
725-730
1981
Bacillus cereus
-
brenda
Bjorklid, E.; Little, C.
The isoelectric point of phospholipase C from Bacillus cereus
FEBS Lett.
113
161-163
1980
Bacillus cereus
brenda
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
brenda
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
brenda
Zwaal, R.F.A.; Roelofsen, B.
Phospholipase C (phosphatidylcholine cholinephosphohydrolase, EC 3.1.4.3) from Bacillus cereus
Methods Enzymol.
32
154-161
1974
Bacillus cereus
brenda
Shiloach, J.; Bauer, S.; Vlodavsky, I.; Selinger, Z.
Phospholipase C from Bacillus cereus: Production, purification, and properties
Biotechnol. Bioeng.
15
551-560
1973
Bacillus cereus, Bacillus cereus 569/H
brenda
Hansen, S.; Hough, E.; Svensson, L.A.; Wong, Y.L.; Martin, S.F.
Crystal structure of phospholipase C from Bacillus cereus complexed with a substrate analogue
J. Mol. Biol.
234
179-189
1993
Bacillus cereus
brenda
Hansen, S.; Hansen, L.K.; Hough, E.
The crystal structure of tris-inhibited phospholipase C from Bacillus cereus at 1.9 A resolution. The nature of the metal ion in site 2
J. Mol. Biol.
231
870-876
1993
Bacillus cereus
brenda
Hansen, S.; Hansen, L.K.; Hough, E.
Crystal structures of phosphate, iodide and iodate-inhibited phospholipase C from Bacillus cereus and structural investigations of the binding of reaction products and a substrate analogue
J. Mol. Biol.
225
543-549
1992
Bacillus cereus
brenda
Haftendorn, R.; Ulbrich-Hofmann, R.
Activity of phospholipase C in two-phase systems
Anal. Biochem.
306
144-147
2002
Bacillus cereus
brenda
Martin, S.F.; Follows, B.C.; Hergenrother, P.J.; Trotter, B.K.
The choline binding site of phospholipase C (Bacillus cereus): insights into substrate specificity
Biochemistry
39
3410-3415
2000
Bacillus cereus (P09598), Bacillus cereus
brenda
Durban, M.A.; Silbersack, J.; Schweder, T.; Schauer, F.; Bornscheuer, U.T.
High level expression of a recombinant phospholipase C from Bacillus cereus in Bacillus subtilis
Appl. Microbiol. Biotechnol.
74
634-639
2007
Bacillus cereus, Bacillus cereus SBUG516, Bacillus cereus SBUG318
brenda
Ranganathan, R.; Tcacenco, C.M.; Rosseto, R.; Hajdu, J.
Characterization of the kinetics of phospholipase C activity toward mixed micelles of sodium deoxycholate and dimyristoylphosphatidylcholine
Biophys. Chem.
122
79-89
2006
Bacillus cereus
brenda
Rose, T.M.; Prestwich, G.D.
Synthesis and evaluation of fluorogenic substrates for phospholipase D and phospholipase C
Org. Lett.
8
2575-2578
2006
Bacillus cereus
brenda
Gonzalez-Bulnes, P.; Gonzalez-Roura, A.; Canals, D.; Delgado, A.; Casas, J.; Llebaria, A.
2-aminohydroxamic acid derivatives as inhibitors of Bacillus cereus phosphatidylcholine preferred phospholipase C PC-PLC(Bc)
Bioorg. Med. Chem.
18
8549-8555
2010
Bacillus cereus
brenda
Liao, R.Z.; Yu, J.G.; Himo, F.
Reaction mechanism of the trinuclear zinc enzyme phospholipase C: a density functional theory study
J. Phys. Chem. B
114
2533-2540
2010
Bacillus cereus
brenda
Shimanouchi, T.; Kawasaki, H.; Fuse, M.; Umakoshi, H.; Kuboi, R.
Membrane fusion mediated by phospholipase C under endosomal pH conditions
Colloids Surf. B Biointerfaces
103
75-83
2013
Bacillus cereus
brenda
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
Prog. Lipid Res.
52
62-79
2013
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)
brenda
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
Process Biochem.
50
432-437
2015
Bacillus cereus
-
brenda
Elena, C.; Ravasi, P.; Cerminati, S.; Peiru, S.; Castelli, M.; Menzella, H.
Pichia pastoris engineering for the production of a modified phospholipase C
Process Biochem.
51
1935-1944
2016
Bacillus cereus
-
brenda
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
Process Biochem.
54
67-72
2017
Bacillus cereus
-
brenda