Information on EC 3.1.1.32 - phospholipase A1

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
3.1.1.32
-
RECOMMENDED NAME
GeneOntology No.
phospholipase A1
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
phosphatidylcholine + H2O = 2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
-
-
-
-
phosphatidylcholine + H2O = 2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
structure-function relationship
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
alpha-Linolenic acid metabolism
-
-
Biosynthesis of secondary metabolites
-
-
Glycerophospholipid metabolism
-
-
Metabolic pathways
-
-
phosphatidylcholine acyl editing
-
-
phospholipases
-
-
SYSTEMATIC NAME
IUBMB Comments
phosphatidylcholine 1-acylhydrolase
This enzyme has a much broader specificity than EC 3.1.1.4 phospholipase A2. Requires Ca2+.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Allergen Dol m 1.01
-
-
-
-
Allergen Dol m 1.02
-
-
-
-
OM PLA
-
-
-
-
OMPLA
-
-
-
-
Phosphatidylcholine 1-acylhydrolase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9043-29-2
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
expression in Saccharomyces cerevisiae
Swissprot
Manually annotated by BRENDA team
strain 168
-
-
Manually annotated by BRENDA team
Bacillus subtilis 168
strain 168
-
-
Manually annotated by BRENDA team
Bacteroides melaninogenicus
strain 576 and 579
-
-
Manually annotated by BRENDA team
Bacteroides melaninogenicus 576
strain 576 and 579
-
-
Manually annotated by BRENDA team
several isozymes
-
-
Manually annotated by BRENDA team
two cationic phospholipase A1 activities
-
-
Manually annotated by BRENDA team
two cationic phospholipase A1 activities: Ia and Ib
-
-
Manually annotated by BRENDA team
Corticium centrifugum
-
-
-
Manually annotated by BRENDA team
isozyme a; gene CG8552 or papla1
UniProt
Manually annotated by BRENDA team
isozyme b; gene CG8552 or papla1
UniProt
Manually annotated by BRENDA team
isozyme D; gene CG8552 or papla1
UniProt
Manually annotated by BRENDA team
strain IMSS 0989
-
-
Manually annotated by BRENDA team
Giardia intestinalis IMSS 0989
strain IMSS 0989
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
acid phospholipase activity
-
-
Manually annotated by BRENDA team
several isozymes
-
-
Manually annotated by BRENDA team
Linnaeus
-
-
Manually annotated by BRENDA team
skipjack tuna
-
-
Manually annotated by BRENDA team
several isozymes
-
-
Manually annotated by BRENDA team
enzyme precursor
SwissProt
Manually annotated by BRENDA team
precursor; a social wasp
UniProt
Manually annotated by BRENDA team
isolate HFKI0020
-
-
Manually annotated by BRENDA team
one isoenzyme in kidney
-
-
Manually annotated by BRENDA team
several isozymes
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
; strain MK1
SwissProt
Manually annotated by BRENDA team
strain MK1
-
-
Manually annotated by BRENDA team
strain MK1
SwissProt
Manually annotated by BRENDA team
strain MK1
-
-
Manually annotated by BRENDA team
isolated from Japanese soil, gene pla
UniProt
Manually annotated by BRENDA team
Streptomyces albidoflavus NA297
-
UniProt
Manually annotated by BRENDA team
Streptomyces albidoflavus NA297
isolated from Japanese soil, gene pla
UniProt
Manually annotated by BRENDA team
strain NT-1
-
-
Manually annotated by BRENDA team
Tetrahymena pyriformis NT-1
strain NT-1
-
-
Manually annotated by BRENDA team
screen for PLA1 hypersecretory mutants
-
-
Manually annotated by BRENDA team
strain 427, from BALB/c mouse bloodstream
UniProt
Manually annotated by BRENDA team
Trypanosoma brucei 427
strain 427, from BALB/c mouse bloodstream
UniProt
Manually annotated by BRENDA team
Plase A1 may play a role in the pathogenesis of Chagas' disease
-
-
Manually annotated by BRENDA team
strains Cvd and RA (lethal) and K98 (non-lethal)
UniProt
Manually annotated by BRENDA team
4 isoforms, Ves a 1.01-1.04
-
-
Manually annotated by BRENDA team
black-bellied hornet
-
-
Manually annotated by BRENDA team
genes Vesv1 and Vesv5
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
mechanisms of activation of the ExoU family of PLAs may be evolutionarily conserved
evolution
-
evolutionary relationship and phylogenetics of isozymes Ves a 1.01-1.04, overview
evolution
-
the enzyme is a member of the pancreatic lipase family
malfunction
-
knockdown of intracellular PLA1gamma expression by RNAi does not affect the anterograde transport of ts045 vesicular stomatitis virus protein (VSVGts045) but dramatically delays two types of Golgi-to-endoplasmic reticulum retrograde membrane transport, i.e., transfer of the Golgi membrane into the endoplasmic reticulum in the presence of brefeldin A and delivery of cholera toxin B subunit from the Golgi complex to the endoplasmic reticulum. Knockdown of intracellular PLA1gamma does not impair coat protein complex I- and Rab6-dependent retrograde transports represented by ERGIC-53 recycling and endoplasmic reticulum delivery of Shiga toxin, respectively
malfunction
-
Because orientation of seam cell division is randomized relative to the A-P axis in ipla-1 mutants, ipla-1 mutants exhibit aberrant orientation of seam cell divisions. Acl-8 acl-9 acl-10 triple mutations also cause misorientation of seam cell divisions similar to that observed in ipla-1 mutants
malfunction
-
in enzyme mutants, in the absence of transport to the Golgi, rhodopsin 1 is aberrantly glycosylated and is mislocalized. These defects lead to decreased levels of the protein and decreased sensitivity of the photoreceptors to light. Several GPCRs, including other rhodopsins and Bride of sevenless, are similarly affected, phenotypes, overview
malfunction
-
phosphatidic acid-preferring phospholipase A1 depletion causes mitochondrial elongation, leading to a loss of motility
malfunction
-
phosphatidic acid-preferring phospholipase A1 depletion causes mitochondrial elongation. Enzyme knock-out mice have a defect in sperm formation, spermatozoa from PA-PLA1-/- mice possess an annulus that is not attached to the mitochondrial sheath, whereas that in control mice is attached. In enzyme-deficient sperm, the mitochondrial structure is disorganized, and an abnormal gap structure exists between the middle and principal pieces.A flagellum is bent at that position, leading to a loss of motility
physiological function
-
H-Rev107 functions principally as a Ca2+-independent PLA1/2 with a higher PLA1 activity. Transient expression of H-Rev107 in COS-7 cells does not appear to influence cell proliferation
physiological function
P53817
H-Rev107 functions principally as a Ca2+-independent PLA1/2 with a higher PLA1 activity. Transient expression of H-Rev107 in COS-7 cells does not appear to influence cell proliferation
physiological function
-
is capable for activation of human basophils, relevance of Ves v 1 in hymenoptera venom allergy
physiological function
-
mediates a specific retrograde membrane transport pathway between the endoplasmic reticulum and the Golgi complex
physiological function
-
simultaneous purification of plasmalogens and sphingomyelin with PLA1 in human erythrocytes. Relative concentration of the plasmalogens after treatment with PLA1 is 92% of phospholipids in the supernatant fraction, and that of sphingomyelin is 97.7% in the precipitate fraction
physiological function
-
intracellular phospholipase A1 and acyltransferase, which are involved in Caenorhabditis elegans stem cell divisions, determine the sn-1 fatty acyl chain of phosphatidylinositol
physiological function
-
PLA1 is the major allergen for humans in the wasp venom
physiological function
-
the phospholipase A1 activity of lysophospholipase A-I links platelet activation to LPA production during blood coagulation
physiological function
-
classical pancreatic lipase may fulfill in some cases additional biological functions as a phospholipase A1, PLA1, enzyme, compensating pancreatic lipase-related protein 2, PLRP2, deficiency in the digestive tract
physiological function
H2EIY3
lysophospholipase activity in live Tryypanosoma cruzi parasites contributes to self protection against toxic compounds generated by phospholipase A1 activity
physiological function
-
the cytosolic enzyme is necessary for transit of selective transmembrane receptor cargo by the COPII coat for anterograde trafficking in Drosophila melanogaster. The enzme interacts with the coat protein II (COPII), the COPII coated vesicular system transports newly synthesized secretory and membrane proteins from the endoplasmic reticulum to the Golgi complex. The enzyme is required for the transport of rhodopsin 1, an N-glycosylated G protein-coupled receptor, from the endoplasmic reticulum to the Golgi complex, but the active site of PAPLA1 is not necessary for Rh1 maturation. The enzyme acts downstream of the rhodopsin 1 chaperone NinaA and upstream of the Golgi-resident protein dMPPE
physiological function
-
the phosphatidic acid-preferring phospholipase A1 regulates mitochondrial dynamics
physiological function
-
the phosphatidic acid-preferring phospholipase A1 regulates mitochondrial dynamics. When ectopically expressed in HeLa cells, it induces mitochondrial fragmentation, whereas its depletion causes mitochondrial elongation. The effects of the enzyme on mitochondrial morphology appear to counteract those of MitoPLD, a mitochondrion-localized phospholipase D that produces phosphatidic acid from cardiolipin
physiological function
-
the T4SS-translocated effector protein VipD exhibits phospholipase A1 activity that is activated only upon binding to endosomal Rab5 or Rab22, VipD protects Legionella pneumophila from endosomal fusion, that way, the pathogen Legionella pneumophila bypasses the microbicidal endosomal compartment of mammalian macrophages. By catalyzing phosphatidylinositol 3-phosphate depletion in a Rab5-dependent manner, VipD alters the protein composition of endosomes thereby blocking fusion with Legionella-containing vacuoles, implicated molecular mechanism, overview. The enzyme VipD alters the endosomal protein and lipid composition
metabolism
-
intracellular phospholipase A1 and acyltransferase are involved in Caenorhabditis elegans stem cell divisions
additional information
K0J3J2
residue Ser11 is essential for the catalytic function of the enzyme, the active site may include residues Ser216 and His218
additional information
K0J3J2
the enzyme's active site is composed of a Ser-His dyad (Ser11 and His218), whereby stabilization of the imidazole is provided by the main-chain carbonyl oxygen of Ser216, a common variation of the catalytic triad in many serine hydrolases, where this carbonyl maintains the orientation of the active site histidine residue. The hydrophobic pocket and cleft for lipid binding are adjacent to the active site, and are approximately 13-15 A deep and 14-16 A long
additional information
Streptomyces albidoflavus NA297
-
the enzyme's active site is composed of a Ser-His dyad (Ser11 and His218), whereby stabilization of the imidazole is provided by the main-chain carbonyl oxygen of Ser216, a common variation of the catalytic triad in many serine hydrolases, where this carbonyl maintains the orientation of the active site histidine residue. The hydrophobic pocket and cleft for lipid binding are adjacent to the active site, and are approximately 13-15 A deep and 14-16 A long, residue Ser11 is essential for the catalytic function of the enzyme, the active site may include residues Ser216 and His218
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1(3)-monoolein + H2O
?
show the reaction diagram
-
-
-
-
?
1,2-didocosahexaenoyl-phosphatidylcholine + H2O
2-docosahexaenoyl-lysophosphatidylcholine + docosahexaenoic acid
show the reaction diagram
-
19% of activity with 1-oleoyl-2-palmitoyl-phosphatidylcholine
-
?
1,2-dimyristoyl-sn-glycero-3-phosphate + H2O
?
show the reaction diagram
Streptomyces albidoflavus, Streptomyces albidoflavus NA297
K0J3J2
-
-
-
?
1,2-dimyristoyl-sn-glycero-3-phosphocholine + H2O
2-myristoyl-sn-glycero-3-phosphocholine + myristic acid
show the reaction diagram
Q9X9D8
-
-
?
1,2-dioctadecenoylthio-sn-glycero-3-phosphocholine + H2O
1-thio-2-octadecenoylthio-sn-glycero-3-phosphocholine + octadecenoate
show the reaction diagram
-
-
-
?
1,2-dioctadecenoylthio-sn-glycero-3-phosphoethanolamine + H2O
1-thio-2-octadecenoylthio-sn-glycero-3-phosphoethanolamine + octadecenoate
show the reaction diagram
-
-
-
?
1,2-dioctadecenoylthio-sn-glycero-3-phosphoglycerol + H2O
1-thio-2-octadecenoylthio-sn-glycero-3-phosphoglycerol + octadecenoate
show the reaction diagram
-
-
-
?
1,2-dioleoyl-sn-glycero-3-phosphoethanolamine + H2O
?
show the reaction diagram
Streptomyces albidoflavus, Streptomyces albidoflavus NA297
K0J3J2
-
-
-
?
1,2-dioleoylphosphatidylcholine + H2O
oleic acid + 2-oleoylglycerophosphocholine
show the reaction diagram
-
-
-
?
1,2-dipalmitoyl-phosphatidylcholine + H2O
2-palmitoyl-sn-glycerophosphocholine + palmitate
show the reaction diagram
H2EIY3
substrate from Glycine max
-
-
?
1,2-dipalmitoyl-sn-glycero-3-phosphocholine + H2O
?
show the reaction diagram
Streptomyces albidoflavus, Streptomyces albidoflavus NA297
K0J3J2
-
-
-
?
1- palmitoyl-2-oleoyl-phosphatidylcholine + H2O
2-oleoyl-lysophosphatidylcholine + palmitic acid
show the reaction diagram
-
-
-
?
1-acyl-2-lysophosphatidylserine + H2O
sn-glycerol-phosphoserine + a carboxylate
show the reaction diagram
-
-
-
?
1-acyl-2-oleoyl-sn-glycerophosphocholine + H2O
acyl-glycerophosphocholine + oleic acid
show the reaction diagram
-
labeled at the sn-2 position with [14C]oleic acid
-
-
?
1-acyl-lysophosphtidic acid + H2O
glycerol-3-phosphate + a carboxylate
show the reaction diagram
-
7% of activity with phosphatidic acid
-
?
1-acyl-sn-glycero-3-phosphocholine + H2O
fatty acid + glycero-3-phosphocholine
show the reaction diagram
-
-
-
-
?
1-myristoyl 2-oleyl phosphatidylcholine + H2O
2-oleylglycerophosphocholine + myristoate
show the reaction diagram
Q93V61
-
-
-
-
1-oleoyl-2-palmitoyl-phosphatidylcholine + H2O
2-palmitoyl-lysophosphatidylcholine + oleic acid
show the reaction diagram
-
-
-
?
1-oleoyl-2-stearoyl-3-sn-glycerophosphorylcholine + H2O
?
show the reaction diagram
A2VBC4
-
-
-
?
1-palmitoyl-2-arachidonoyl-glycero-3-phosphoethanolamine + H2O
2-arachidonoyl-lysophosphatidylethanolamine + H2O
show the reaction diagram
-
-
-
?
1-palmitoyl-2-arachidonoyl-glycero-3-phosphoethanolamine + H2O
2-arachidonoyl-lysophosphatidylethanolamine + H2O
show the reaction diagram
-
-
-
-
?
1-palmitoyl-2-arachidonylglycerophosphocholine + H2O
palmitic acid + 2-arachidonylglycerophosphocholine
show the reaction diagram
-
-
-
-
?
1-palmitoyl-2-arachidonylglycerophosphocholine + H2O
palmitic acid + 2-arachidonylglycerophosphocholine
show the reaction diagram
-
-
-
-
?
1-palmitoyl-2-arachidonylglycerophosphocholine + H2O
palmitic acid + 2-arachidonylglycerophosphocholine
show the reaction diagram
-
-
-
-
?
1-palmitoyl-2-docosahexaenoyl-phosphatidylcholine + H2O
2-docosahexaenoyl-lysophosphatidylcholine + palmitic acid
show the reaction diagram
-
-
-
?
1-palmitoyl-2-linoleoyl phosphatidylcholine + H2O
?
show the reaction diagram
-
the enzyme is responsible for about two-thirds of plasma 1-palmitoyl-2-linoleoyl phosphatidylcholine disappearance
-
-
-
1-palmitoyl-2-linoleoyl-phosphatidyl choline + H2O
2-linoleoyl-lysophosphatidyl choline + palmitic acid
show the reaction diagram
Q948R1
-
-
?
1-palmitoyl-2-linoleoyl-phosphorylcholine + H2O
palmitic acid + 2-linoleoyl-1-lysophosphoryl choline
show the reaction diagram
A5YW95
-
-
-
?
1-palmitoyl-2-linoleoyl-sn-3-glycerophosphorylethanolamine + H2O
palmitic acid + 2-linoleoyl-sn-3-glycerophosphorylethanolamine
show the reaction diagram
-
-
-
-
?
1-palmitoyl-2-linoleoylglycerophosphocholine + H2O
?
show the reaction diagram
-
-
-
-
?
1-palmitoyl-2-linoleoylglycerophosphocholine + H2O
?
show the reaction diagram
-
-
-
-
-
1-palmitoyl-2-linoleoylglycerophosphocholine + H2O
?
show the reaction diagram
-
-
-
-
?
1-palmitoyl-2-linoleoylphosphatidylethanolamine + H2O
?
show the reaction diagram
-
-
-
-
?
1-palmitoyl-2-oleoyl-phosphatidylcholine + H2O
2-oleoyl-lysophosphatidylcholine + palmitic acid
show the reaction diagram
-
-
-
?
1-palmitoyl-2-oleoylglycerophosphocholine + H2O
palmitic acid + 2-oleoylglycerophosphocholine
show the reaction diagram
-
-
-
-
?
1-palmitoyl-2-oleoylglycerophosphocholine + H2O
palmitic acid + 2-oleoylglycerophosphocholine
show the reaction diagram
Bacteroides melaninogenicus, Bacteroides melaninogenicus 576
-
-
-
-
?
1-palmitoyl-2-palmitoylglycerophosphocholine + H2O
palmitic acid + 2-palmitoylglycerophosphocholine
show the reaction diagram
-
-
-
-
?
1-palmitoyllysophosphatidylcholine + H2O
palmitic acid + lysophosphatidylcholine
show the reaction diagram
-
weak activity
-
-
?
1-stearoyl-2-arachidonyl-sn-glycero-3-phosphoinositol + H2O
2-arachidonylglycero-3-phosphoinositol + ?
show the reaction diagram
-
-
no release of free arachidonate
?
1-stearoyl-2-arachidonylglycerophosphocholine + H2O
stearic acid + 2-arachidonylglycerophosphocholine
show the reaction diagram
-
-
-
-
?
1-stearoyl-2-arachidonylglycerophosphocholine + H2O
stearic acid + 2-arachidonylglycerophosphocholine
show the reaction diagram
-
-
-
-
?
1-stearoyl-2-arachidonylglycerophosphoinositol + H2O
stearic acid + 2-arachidonylglycerophosphoinositol
show the reaction diagram
-
-
-
-
?
1-stearoyl-2-arachidonylglycerophosphoinositol + H2O
stearic acid + 2-arachidonylglycerophosphoinositol
show the reaction diagram
-
-
-
-
?
1-stearoyl-2-oleoyl-3-sn-glycerophosphorylcholine + H2O
?
show the reaction diagram
A2VBC4
-
-
-
?
2-acyl-sn-glycero-3-phosphocholine + H2O
fatty acid + glycerophosphocholine
show the reaction diagram
-
-
-
-
?
2-hexadecanoylthio-ethane-1-phosphocholine + H2O
thio-ethane-1-phosphocholine + hexadecanoate
show the reaction diagram
-
-
-
?
2-monoolein + H2O
?
show the reaction diagram
-
-
-
-
?
2-oleoylphosphatidylcholine + H2O
oleic acid + glycerophosphocholine
show the reaction diagram
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
A5YW95
-
-
-
?
cardiolipin + H2O
?
show the reaction diagram
-
-
-
-
?
diacyl-sn-glycero-3-phosphorylcholine + H2O
fatty acid + lysophosphatidylcholine
show the reaction diagram
-
-
-
-
?
diacyl-sn-glycero-3-phosphorylethanolamine + H2O
fatty acid + lysophosphatidylethanolamine
show the reaction diagram
-
-
-
-
?
diacyl-sn-glycero-3-phosphorylserine + H2O
fatty acid + lysophosphatidylserine
show the reaction diagram
-
-
-
-
?
diolein + H2O
?
show the reaction diagram
-
-
-
-
?
dipalmitoylphosphatidylcholine + H2O
?
show the reaction diagram
-
-
-
-
?
dipalmitoylphosphatidylcholine + H2O
palmitic acid + 1-lyso-2-palmitoylphosphatidylcholine
show the reaction diagram
-
-
-
-
?
dipalmitoylphosphatidylcholine + H2O
palmitic acid + 1-lyso-2-palmitoylphosphatidylcholine
show the reaction diagram
P53817
-
-
-
?
hexadecanoylthioethane-1-phosphocholine + H2O
hexadecanoate + thioethane-1-phosphocholine
show the reaction diagram
-
-
-
?
high-density lipoprotein + H2O
fatty acid + ?
show the reaction diagram
-
-
-
-
?
L-alpha-phosphatidyl-L-serine + H2O
2-acyl-1-glycerophosphoserine + a carboxylate
show the reaction diagram
K0J3J2
substrate from Glycine max
-
-
?
L-alpha-phosphatidylcholine + H2O
2-acyl-1-glycerophosphocholine + a carboxylate
show the reaction diagram
K0J3J2
PLA1 activity for egg yolk lecithin hydrolysis, substrate from egg yolk or Glycine max
-
-
?
L-alpha-phosphatidylglycerol + H2O
?
show the reaction diagram
K0J3J2
-
-
-
?
L-alpha-phosphatidylinositol + H2O
2-acyl-1-glycerophosphoinositol + a carboxylate
show the reaction diagram
K0J3J2
-
-
-
?
lecithin + H2O
?
show the reaction diagram
K0J3J2
from Glycine max
-
-
?
lysophosphatidylcholine + H2O
?
show the reaction diagram
Q93V61
weak substrate
-
-
-
phosphatidic acid + H2O
?
show the reaction diagram
-
phosphatidic acid-specific isozymes mPA-PLA1alpha and mPA-PLA1beta
-
-
?
phosphatidic acid + H2O
2-acyl-lysophosphatidic acid + a carboxylate
show the reaction diagram
-
-
-
-
?
phosphatidic acid + H2O
2-acyl-lysophosphatidic acid + a carboxylate
show the reaction diagram
-
-
-
?
phosphatidic acid + H2O
2-acyl-lysophosphatidic acid + a carboxylate
show the reaction diagram
-
-
-
-
?
phosphatidic acid + H2O
2-acyl-lysophosphatidic acid + a carboxylate
show the reaction diagram
Q6XZB0
-
-
?
phosphatidic acid + H2O
2-acyl-lysophosphatidic acid + a carboxylate
show the reaction diagram
Q8WWY8
-
-
?
phosphatidic acid + H2O
2-acyl-lysophosphatidic acid + a carboxylate
show the reaction diagram
K0J3J2
-
-
-
?
phosphatidic acid + H2O
2-acyl-lysophosphatidic acid + a carboxylate
show the reaction diagram
-
best substrate
-
?
phosphatidic acid + H2O
2-acyl-lysophosphatidic acid + a carboxylate
show the reaction diagram
-
preferred substrate in vitro
-
-
?
phosphatidic acid + H2O
2-acyl-lysophosphatidic acid + a carboxylate
show the reaction diagram
Streptomyces albidoflavus NA297
K0J3J2
-
-
-
?
phosphatidic acid + H2O
2-acylglycerophosphatidic acid + a carboxylate
show the reaction diagram
-
the catalytic preference for phosphatidic acid increases in the presence of membranes containing cholesterol, diacylglycerol, sn-1-stearoyl-2-arachidonoylphosphatidylethanolamine instead of sn-1-palmitoyl-2-oleeoylphosphatidylethanolamine and 10 mol% phosphatidic acid per 100 mol% total phosphoglycerides
-
?
phosphatidic acid + H2O
lysophosphatidic acid + a carboxylate
show the reaction diagram
-
-
-
?
phosphatidic acid + H2O
2-acylglycerol-3-phosphate + a carboxylate
show the reaction diagram
Q93V61
-
-
-
?
phosphatidic acid + H2O
2-acyllysophosphatidic acid + a carboxylate
show the reaction diagram
-
phosphatidic acid-specific isozymes mPA-PLA1alpha and mPA-PLA1beta
-
-
?
phosphatidylcholine + 2-acylglycerophosphocholine
2-acylglycerophosphocholine + phosphatidylcholine
show the reaction diagram
-
regiospecific transacylation activity, PLA1 transfers a fatty acid at the sn-1 position of a donor phosphatidylcholine to the sn-1 position of an acceptor 2-acyl-lysophosphatidylcholine
-
?
phosphatidylcholine + H2O
?
show the reaction diagram
-
-
-
-
?
phosphatidylcholine + H2O
?
show the reaction diagram
-
-
-
-
?
phosphatidylcholine + H2O
?
show the reaction diagram
-
-
-
-
?
phosphatidylcholine + H2O
?
show the reaction diagram
-
-
-
-
?
phosphatidylcholine + H2O
?
show the reaction diagram
Bacteroides melaninogenicus
-
-
-
-
?
phosphatidylcholine + H2O
?
show the reaction diagram
-
no activity
-
-
-
phosphatidylcholine + H2O
?
show the reaction diagram
-
hydrolysis of L-phosphatidylcholine and not D-phosphatidylcholine
-
-
?
phosphatidylcholine + H2O
?
show the reaction diagram
-
hydrolysis only if phosphatidylserine, phosphatidylethanolamine or phosphatidic acid is present
-
-
?
phosphatidylcholine + H2O
?
show the reaction diagram
Bacteroides melaninogenicus 576
-
-
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
-
-
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
-
-
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
-
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
-
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
-
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
-
-
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
-
-
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
P53817
-
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
-
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
-
-
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
-
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
-
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
-
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
-
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
Q9X9D8
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
Q9X9D8
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
Q948R1
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
A2VBC4
-
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
-
-
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
-
very low activity
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
-
18fold lower initial rate than with phosphatidic acid
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
-
7% of activity with phosphatidic acid, at 0.1% Triton X-100
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
-
trivial name lecithin
trivial name lysolecithin
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
-
phosphatidylcholine from shark liver
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
Q9X9D8
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + eicosapentaenoic acid + docosapentaenoic acid + docosahexaenoic acid
show the reaction diagram
-
acidolysis, substrate from fish oil, fatty acid residue composition, overview, Thermomyces lanuginosus/Fusarium oxysporum enzyme mixture
-
-
?
phosphatidylcholine + H2O
lysophosphocholine + a carboxylate
show the reaction diagram
Q6KBS7
-
-
-
?
phosphatidylcholine + H2O
lysophosphocholine + a carboxylate
show the reaction diagram
-
milk, whey, and soy bean substrates
-
-
?
phosphatidylcholine + H2O
lysophosphocholine + a carboxylate
show the reaction diagram
Q6KBS7
TbPLA1 possesses an active-site serine residue, but is relatively insensitive to serine-modifying reagents such as di-isopropyl fluorophosphate and PMSF
-
-
?
phosphatidylcholine + H2O
lysophosphocholine + a carboxylate
show the reaction diagram
Trypanosoma brucei 427
Q6KBS7
TbPLA1 possesses an active-site serine residue, but is relatively insensitive to serine-modifying reagents such as di-isopropyl fluorophosphate and PMSF
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a fatty acid anion
show the reaction diagram
-
-
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a fatty acid anion
show the reaction diagram
-
-
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a fatty acid anion
show the reaction diagram
A9X3M0
-
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a fatty acid anion
show the reaction diagram
-
phosphatidylcholine is more easily hydrolyzed than phosphatidylethanolamine
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a fatty acid anion
show the reaction diagram
A5YW95
PLA1 displays a strong preference for phosphatidylcholine as a substrate
-
-
?
phosphatidylcholine + H2O
lysophosphatidylcholine + fatty acid
show the reaction diagram
-
-
-
-
?
phosphatidylcholine + H2O
lysophosphatidylcholine + fatty acid
show the reaction diagram
-
intracellular phospholipase A1
-
-
?
phosphatidylcholine + H2O
1-acyl-2-oleoyl-sn-glycerophosphocholine + arachidonic acid
show the reaction diagram
-
labeled at the sn-2 position with [14C]arachadonic acid
-
-
?
phosphatidylcholine + H2O
2-acyl-1-glycerophosphocholine + a carboxylate
show the reaction diagram
-
substrate from egg yolk
-
-
?
phosphatidylcholine + H2O
2-acyl-1-glycerophosphocholine + a carboxylate
show the reaction diagram
-
substrate from egg yolk, the regiospecificity and hydrolysis profile of the enzyme is typical of a PLA1 enzyme generating lysophosphatidic acid, but not hydrolyzing the ester bond at the sn-2 position
-
-
?
phosphatidylethanolamine + H2O
?
show the reaction diagram
-
-
-
-
?
phosphatidylethanolamine + H2O
?
show the reaction diagram
-
-
-
-
?
phosphatidylethanolamine + H2O
?
show the reaction diagram
-
-
-
-
?
phosphatidylethanolamine + H2O
?
show the reaction diagram
-
-
-
-
?
phosphatidylethanolamine + H2O
?
show the reaction diagram
-
-
-
-
?
phosphatidylethanolamine + H2O
?
show the reaction diagram
-
-
-
-
?
phosphatidylethanolamine + H2O
?
show the reaction diagram
-
-
-
-
?
phosphatidylethanolamine + H2O
?
show the reaction diagram
-
-
-
-
?
phosphatidylethanolamine + H2O
?
show the reaction diagram
-
no activity
-
-
-
phosphatidylethanolamine + H2O
?
show the reaction diagram
-
no activity
-
-
-
phosphatidylethanolamine + H2O
?
show the reaction diagram
-
docosahexaenoic acid-enriched phosphatidylethanolamine vesicles
-
-
?
phosphatidylethanolamine + H2O
2-acylglycerophosphoethanolamine + a carboxylate
show the reaction diagram
-
-
-
-
?
phosphatidylethanolamine + H2O
2-acylglycerophosphoethanolamine + a carboxylate
show the reaction diagram
-
-
-
-
?
phosphatidylethanolamine + H2O
2-acylglycerophosphoethanolamine + a carboxylate
show the reaction diagram
P53817
-
-
-
?
phosphatidylethanolamine + H2O
2-acylglycerophosphoethanolamine + a carboxylate
show the reaction diagram
Q93V61
-
-
-
?
phosphatidylethanolamine + H2O
2-acylglycerophosphoethanolamine + a carboxylate
show the reaction diagram
-
similar activity as with phosphatidic acid
-
?
phosphatidylethanolamine + H2O
lysophosphatidylethanolamine + a carboxylate
show the reaction diagram
-
milk, whey, and soy bean substrates
-
-
?
phosphatidylethanolamine + H2O
lysophosphatidylethanolamine + a fatty acid anion
show the reaction diagram
-
-
-
-
?
phosphatidylethanolamine + H2O
lysophosphatidylethanolamine + a fatty acid anion
show the reaction diagram
-
-
-
-
?
phosphatidylglycerol + H2O
?
show the reaction diagram
-
-
-
-
?
phosphatidylglycerol + H2O
?
show the reaction diagram
-
-
-
-
?
phosphatidylglycerol + H2O
?
show the reaction diagram
-
-
-
-
?
phosphatidylglycerol + H2O
?
show the reaction diagram
-
-
-
-
?
phosphatidylinositol + H2O
?
show the reaction diagram
-
-
-
-
?
phosphatidylinositol + H2O
?
show the reaction diagram
-
hydrolysis only if phosphatidylserine, phosphatidylethanolamine or phosphatidic acid is present
-
-
?
phosphatidylinositol + H2O
?
show the reaction diagram
-
highly specific for phosphatidylinositol
-
-
?
phosphatidylinositol + H2O
?
show the reaction diagram
-
intracellular phospholipase A1 recognizes the sn-1 position of phosphatidylinositol as its substrate, recombinant IPLA-1 hydrolyzes a fatty acid attached to phosphatidylinositol
-
-
?
phosphatidylinositol + H2O
lysophosphatidylinositol + a carboxylate
show the reaction diagram
-
1% of activity with phosphatidic acid, at 0.1% Triton X-100
-
?
phosphatidylserine + H2O
?
show the reaction diagram
-
in short incubation, 1-3 h, 2-acyllysophosphatidylserine is produced, in longer incubations the cis-unsaturated fatty acid is also released
-
-
?
phosphatidylserine + H2O
?
show the reaction diagram
-
docosahexaenoic acid-enriched phosphatidylserine vesicles
-
-
?
phosphatidylserine + H2O
?
show the reaction diagram
-
phosphatidylserine-specific PLA1 isozyme PS-PLA1 or PLA1A
-
-
?
phosphatidylserine + H2O
2-acyl-1-glycerophosphoserine + a carboxylate
show the reaction diagram
-
PS-PLA1 stimulates histamine release from peritoneal mast cells through production of 2-acyl-1-glycerophosphoserine
-
?
phosphatidylserine + H2O
2-acylglycerophosphoserine + a carboxylate
show the reaction diagram
-
-
-
?
phosphatidylserine + H2O
2-acylglycerophosphoserine + a carboxylate
show the reaction diagram
-
low activity
-
?
phosphatidylserine + H2O
lysophosphatidylserine + fatty acid
show the reaction diagram
-
-
-
-
?
phosphatidylserine + H2O
lysophosphatidylserine + fatty acid
show the reaction diagram
-
intracellular phospholipase A1
-
-
?
sphingomyelin + H2O
?
show the reaction diagram
-
-
-
-
?
triacetin + H2O
?
show the reaction diagram
-
-
-
-
?
tributyrin + H2O
?
show the reaction diagram
-
-
-
-
?
triolein + H2O
?
show the reaction diagram
-
-
-
-
?
triolein + H2O
oleic acid + 1,2-dioleoylglycerol
show the reaction diagram
A5YW95
-
-
-
?
monogalactosyldiacylglycerol + H2O
1-lyso-2-acyl-3-galactosyl-sn-glycerol + a fatty acid anion
show the reaction diagram
A5YW95
-
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
the enzyme hydrolyzes sn-1 ester bonds about 2000 times more efficiently than sn-2 ones, the enzyme exhibits weak, but significant sn-1 lysophospholipase activity
-
-
-
additional information
?
-
-
natural glycerophospholipids carrying a 1-acyl-bond are degraded in the following decreasing order of decreasing activity: phosphatidylcholine, phosphatidylinositol, 1-acyl-sn-glycero-3-phosphocholine, phosphatidylethanolamine, phosphatidylglycerol
-
-
-
additional information
?
-
-
transacylase activity
-
-
-
additional information
?
-
-
the enzyme exhibits both phospholipase A1 and phospholipase A2 activity
-
-
-
additional information
?
-
-
the enzyme exhibits both phospholipase A1 and phospholipase A2 activity
-
-
-
additional information
?
-
-
no activity with phosphatidylcholine or triolein
-
-
-
additional information
?
-
-
no activity with 1-alkyl-2-acyl-sn-glycero-3-phosphocholine
-
-
-
additional information
?
-
-
the enzyme also has lysophospholipase activity
-
-
-
additional information
?
-
Corticium centrifugum
-
the enzyme also has lysophospholipase activity
-
-
-
additional information
?
-
-
substrate specificity, overview
-
-
-
additional information
?
-
-
the enzyme is supposed to be responsible for the accumulation of lysophosphatidylcholine
-
-
-
additional information
?
-
-
the enzyme is activated by the binding of isoprenaline to beta2-adrenergic receptors
-
-
-
additional information
?
-
-
the enzyme is important in phospholipid catabolism and the remodeling of the acyl groups of phospholipids
-
-
-
additional information
?
-
Q93V61
no substrate: tripalmitoylglycerol, cholesteryl oleate. Enzyme is sn-1 specific
-
-
-
additional information
?
-
-
isozyme mPA-PLA1beta is identical to the lipid defect locus lipase LPDL, encoded by gene lpd, homozygous insertion mutation leads to high levels of triacylglycerols in the plasma and hepatic steatosis
-
-
-
additional information
?
-
-
isozyme mPA-PLA1beta might plays a role in tumor progression
-
-
-
additional information
?
-
-
release of lysophospholipids from the fat globule membrane decreasing the surface tension of skim milk and whey, overview, the enzyme improves foaming stability and properties of skim milk and whey, overview
-
-
-
additional information
?
-
-
the enzyme plays an important role in the metabolism of high density lipoproteins, it may be responsible for the generation of docosahexaenoic acid DHA lysophospholipids in plasma, DHA is important in brain development and neurological function, the endothelial lipase is important in the delivery of DHA lysophospholipid carriers to the brain, overview
-
-
-
additional information
?
-
-
the parasite enzyme of the infective stages generates lipid messengers that activate host cell protein kinase C, infection of Vero cells with the pathogen leads to an altered lipid composition with the appearance of free fatty acids, diacylglycerol, and lysophosphatidylcholine, overview, the enzyme might play an important role in host cell-parasite interaction preceding invasion
-
-
-
additional information
?
-
-
distribution of phospholipids and lysophospholipids between fat globules and skim milk, foaming and surface properties, overview
-
-
-
additional information
?
-
-
several isozymes with different substrate specificities, overview, endothelial lipase hepatic lipase, and PLRP2 also exhibit triacylglycerol-hydrolyzing activity
-
-
-
additional information
?
-
A5YW95
catalyzes the hydrolysis of phospholipids at the sn-1 position
-
-
-
additional information
?
-
P53817
His21 and Cys111 of H-Rev107 form a catalytic dyad. The N-terminal proline-rich and C-terminal hydrophobic domains are involved in the catalytic activity and/or proper folding
-
-
-
additional information
?
-
-
hydrolysis of diacylphospholipids
-
-
-
additional information
?
-
-
monoglyceride lipase does exhibit PLA1 activity
-
-
-
additional information
?
-
-
RP534 is a bona fide PLA enzyme
-
-
-
additional information
?
-
-
no activity with phosphatidylethanolamine and phosphatidic acid by intracellular phospholipase A1
-
-
-
additional information
?
-
-
the Rickettsia prowazekii RP534 protein possesses phospholipase A1, i.e. PLA1, PLA2, and Lyso-PLA2 activities and can function in the absence of any eukaryotic cofactors in vitro, overview. RP534 protein is a homologue of the Pseudomonas aeruginosa ExoU phospholipase A secreted cytotoxin
-
-
-
additional information
?
-
-
the enzyme is a triacylglycerol lipase, EC 3.1.1.3, that is a carboxylester hydrolases catalyzing the hydrolysis of long-chain acylglycerols, but it is also active on phosphatidylcholine to a lesser extent
-
-
-
additional information
?
-
-
the enzyme VipD possesses phospholipase A1 but not phospholipase A2 activity, EC 3.1.1.4
-
-
-
additional information
?
-
K0J3J2
the enzyme preferentially hydrolyzes the sn-1 acyl ester in glycerophospholipids, yielding a fatty acid and 2-acyl-lysophospholipid, molecular mechanism underlying the substrate binding by the enzyme, overview
-
-
-
additional information
?
-
K0J3J2
the substrate specificity is pH-dependent, the enzyme preferably hydrolyzes phosphatidic acid and phosphatidylserine at pH 7.2, it is active with lysophosphatidylcholine, but not with triglyceride and the 4-nitrophenyl ester of fatty acids, substrate specificity, overview. At the reaction equilibrium, the molar ratio of released free fatty acids (sn-1:sn-2) is 63:37
-
-
-
additional information
?
-
-
Val260 residue in enzyme's lid is critical for the interaction with lipid substrate, molecular dynamics calculations of lipase-phospholipid transition-state complexes in substrate binding determining the substrate specificity with phospholipids, molecular dynamics simulations, overview. Hydrolysis of egg yolk phosphatidylcholine by the enzyme shows a triphasic kinetic pattern
-
-
-
additional information
?
-
Streptomyces albidoflavus NA297
K0J3J2
the enzyme preferentially hydrolyzes the sn-1 acyl ester in glycerophospholipids, yielding a fatty acid and 2-acyl-lysophospholipid, molecular mechanism underlying the substrate binding by the enzyme, overview
-
-
-
additional information
?
-
Streptomyces albidoflavus NA297
K0J3J2
the substrate specificity is pH-dependent, the enzyme preferably hydrolyzes phosphatidic acid and phosphatidylserine at pH 7.2, it is active with lysophosphatidylcholine, but not with triglyceride and the 4-nitrophenyl ester of fatty acids, substrate specificity, overview. At the reaction equilibrium, the molar ratio of released free fatty acids (sn-1:sn-2) is 63:37
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1-palmitoyl-2-linoleoyl phosphatidylcholine + H2O
?
show the reaction diagram
-
the enzyme is responsible for about two-thirds of plasma 1-palmitoyl-2-linoleoyl phosphatidylcholine disappearance
-
-
-
phosphatidic acid + H2O
2-acyl-lysophosphatidic acid + a carboxylate
show the reaction diagram
-
-
-
-
?
phosphatidic acid + H2O
2-acyl-lysophosphatidic acid + a carboxylate
show the reaction diagram
-
-
-
?
phosphatidic acid + H2O
2-acyl-lysophosphatidic acid + a carboxylate
show the reaction diagram
-
-
-
-
?
phosphatidic acid + H2O
2-acyl-lysophosphatidic acid + a carboxylate
show the reaction diagram
Q6XZB0
-
-
?
phosphatidic acid + H2O
2-acyl-lysophosphatidic acid + a carboxylate
show the reaction diagram
Q8WWY8
-
-
?
phosphatidic acid + H2O
2-acylglycerophosphatidic acid + a carboxylate
show the reaction diagram
-
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
-
-
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
-
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
-
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
-
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
-
-
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
-
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
-
-
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
-
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
-
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
-
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
-
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
Q9X9D8
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
Q9X9D8
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
Q948R1
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
A2VBC4
-
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
-
-
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + eicosapentaenoic acid + docosapentaenoic acid + docosahexaenoic acid
show the reaction diagram
-
acidolysis, substrate from fish oil, fatty acid residue composition, overview, Thermomyces lanuginosus/Fusarium oxysporum enzyme mixture
-
-
?
phosphatidylcholine + H2O
lysophosphocholine + a carboxylate
show the reaction diagram
Q6KBS7
-
-
-
?
phosphatidylcholine + H2O
2-acylglycerophosphocholine + a carboxylate
show the reaction diagram
Q9X9D8
-
-
?
phosphatidylcholine + H2O
lysophosphocholine + a carboxylate
show the reaction diagram
Trypanosoma brucei 427
Q6KBS7
-
-
-
?
phosphatidylserine + H2O
2-acyl-1-glycerophosphoserine + a carboxylate
show the reaction diagram
-
PS-PLA1 stimulates histamine release from peritoneal mast cells through production of 2-acyl-1-glycerophosphoserine
-
?
phosphatidylserine + H2O
2-acylglycerophosphoserine + a carboxylate
show the reaction diagram
-
-
-
?
1-palmitoyl-2-oleoyl-phosphatidylcholine + H2O
2-oleoyl-lysophosphatidylcholine + palmitic acid
show the reaction diagram
-
-
-
?
additional information
?
-
-
the enzyme is supposed to be responsible for the accumulation of lysophosphatidylcholine
-
-
-
additional information
?
-
-
the enzyme is activated by the binding of isoprenaline to beta2-adrenergic receptors
-
-
-
additional information
?
-
-
the enzyme is important in phospholipid catabolism and the remodeling of the acyl groups of phospholipids
-
-
-
additional information
?
-
-
isozyme mPA-PLA1beta is identical to the lipid defect locus lipase LPDL, encoded by gene lpd, homozygous insertion mutation leads to high levels of triacylglycerols in the plasma and hepatic steatosis
-
-
-
additional information
?
-
-
isozyme mPA-PLA1beta might plays a role in tumor progression
-
-
-
additional information
?
-
-
release of lysophospholipids from the fat globule membrane decreasing the surface tension of skim milk and whey, overview, the enzyme improves foaming stability and properties of skim milk and whey, overview
-
-
-
additional information
?
-
-
the enzyme plays an important role in the metabolism of high density lipoproteins, it may be responsible for the generation of docosahexaenoic acid DHA lysophospholipids in plasma, DHA is important in brain development and neurological function, the endothelial lipase is important in the delivery of DHA lysophospholipid carriers to the brain, overview
-
-
-
additional information
?
-
-
the parasite enzyme of the infective stages generates lipid messengers that activate host cell protein kinase C, infection of Vero cells with the pathogen leads to an altered lipid composition with the appearance of free fatty acids, diacylglycerol, and lysophosphatidylcholine, overview, the enzyme might play an important role in host cell-parasite interaction preceding invasion
-
-
-
additional information
?
-
A5YW95
catalyzes the hydrolysis of phospholipids at the sn-1 position
-
-
-
additional information
?
-
-
monoglyceride lipase does exhibit PLA1 activity
-
-
-
additional information
?
-
-
RP534 is a bona fide PLA enzyme
-
-
-
additional information
?
-
-
the enzyme is a triacylglycerol lipase, EC 3.1.1.3, that is a carboxylester hydrolases catalyzing the hydrolysis of long-chain acylglycerols, but it is also active on phosphatidylcholine to a lesser extent
-
-
-
additional information
?
-
-
the enzyme VipD possesses phospholipase A1 but not phospholipase A2 activity, EC 3.1.1.4
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
-
divalent cation required
Ca2+
-
10 mM, 10% activation
Ca2+
-
required for actiivty, one Ca2+ per monomer bound at the dimer interface; required for activity, only in dimeric OMPLA high affinity Ca2+-sites are formed that are essential for catalysis
Ca2+
-
required for activity
Ca2+
-
dependent on
Ca2+
A9X3M0
111.5% relative activity at 5 mM Ca2+
Ca2+
-
required
Ca2+
K0J3J2
activates at 10 mM
Ca2+
-
divalent cation required, Ca2+ being most effective, maximal activity at 10 mM
Ca2+
-
slight stimulation of solubilized enzyme from plasmalemma
Ca2+
-
required
Ca2+
-
no requirement
Ca2+
-
independent of Ca2+ at pHs below 7.4, striking pH dependence at alkaline pH
Ca2+
-
no requirement
Hg2+
-
2.0 mM, stimulates; not required
Hg2+
-
not required
Hg2+
-
not required; stimulates
Hg2+
Bacteroides melaninogenicus
-
not required
Mg2+
-
divalent cation required
Mg2+
-
required
Mg2+
-
maximal stimulation at 1 mM
Sr2+
-
divalent cation required
Mn2+
-
divalent cation required
additional information
Q93V61
independent of Ca2+
additional information
Q6KBS7
TbPLA1 does not require metal co-factors for activity
additional information
-
H-Rev107 functions as a cytosolic Ca2+-independent PLA1/2
additional information
P53817
H-Rev107 functions as a cytosolic Ca2+-independent PLA1/2
additional information
K0J3J2
metal ion-independent phospholipase A1
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
K0J3J2
weak inhibition
Al3+
Corticium centrifugum
-
inhibition of phospholipase A1 activity and lysophospholipase activity
arachidonyl trifluoromethyl ketone analogue
Q6KBS7
-
-
Ca2+
Q6KBS7
slight inhibition at 2 mM
Ca2+
K0J3J2
up to 0.1 mM
Ca2+
-
CaCl2, slight
Ca2+
-
-
Ca2+
-
10 mM CaCl2, 50-60% inhibition of lysosomal enzyme
Ca2+
-
10 mM, 20-60% increase in activity
Cationic amphiphilic drugs
-
-
-
Cd2+
Q6KBS7
complete inhibition at 2 mM
CHAPS
-
-
chlorpromazine
-
1 mM, 50% inhibition
choline plasmalogen
-
inhibits hydrolysis of phosphatidylethanolamine
Co2+
Q6KBS7
43% inhibition at 2 mM
cocaine
-
10 mM, below 10% residual activity
Cr3+
A9X3M0
51.4% relative activity at 5 mM
Cu2+
Q6KBS7
complete inhibition at 2 mM
Cu2+
A9X3M0
56.8% relative activity at 5 mM
DFP
-
-
di-isopropyl fluorophosphate
Q6KBS7
TbPLA1 possesses an active-site serine residue, but is relatively insensitive to serine-modifying reagents such as di-isopropyl fluorophosphate and PMSF
diethyl-p-nitrophenyl phosphate
Q6KBS7
-
diisopropyl fluorophosphate
-
IC50: 8 mM
dithiothreitol
-
1 mM, complete inhibition
DNA containing thymine glycol
-
0.05 mM, 50% inhibition
-
DNA containing thymine glycol
-
-
-
E-600
Q6KBS7
-
EDTA
-
no activity in the presence of EDTA
EDTA
A9X3M0
complete inhibition at 5 mM
EDTA
-
10 mM, 30-40% inhibition
ethanolamine plasmalogen
-
inhibits hydrolysis of phosphatidylethanolamine
-
Fe2+
Q6KBS7
complete inhibition at 2 mM
Fe2+
A9X3M0
89.2% relative activity at 5 mM
Fe2+
Corticium centrifugum
-
inhibition of phospholipase A1 activity and lysophospholipase activity
Fe3+
Corticium centrifugum
-
inhibition of phospholipase A1 activity and lysophospholipase activity
Fe3+
-
1 mM, almost complete inhibition
gentamycin
-
the inhibition by aminoglycosides appears to be due to substrate depletion caused by binding of aminoglycosides to the negatively charged phospholipid and can be overcome by raising the substrate concentration
GSK264220A
-
-
guanosine 5'-[gamma-thio]triphosphate
-
-
Insulin
-
significantly reduces endothelial lipase mRNA and protein expression in a dose dependent manner
-
iodoacetic acid
-
-
iodoacetic acid
P53817
-
KCl
-
2 M, inactivation of the soluble enzyme, no inactivation of the membrane-bound enzyme
lauryldimethylbenzyl ammonium chloride
-
-
liponox DCH
-
1%, i.e. polyoxyethylene alkylether
-
methyl arachidonyl fluorophosphonate
-
blocks phospholipase A1 as well as phospholipase A2 activity
Mg2+
A9X3M0
13.5% relative activity at 5 mM
MgCl2
-
slight
Mn2+
Q6KBS7
slight inhibition at 2 mM
N-bromosuccinimide
Corticium centrifugum
-
-
Na+
A9X3M0
54.7% relative activity at 5 mM
NaCl
-
100 mM, 20-30% inhibition of lysosomal enzyme
Ni2+
Q6KBS7
57% inhibition at 2 mM
octyl-beta-glucoside
-
-
p-Diazobenzenesulfonic acid
Corticium centrifugum
-
-
palmitoyl trifluoromethyl ketone analogue
Q6KBS7
-
-
PMSF
Q6KBS7
TbPLA1 possesses an active-site serine residue, but is relatively insensitive to serine-modifying reagents such as di-isopropyl fluorophosphate and PMSF
PMSF
K0J3J2
weak inhibition
rabbit anti-phospholipase A antibodies
-
-
-
Rosenthal's inhibitor
-
-
SDS
A9X3M0
20.9% relative activity at 5 mM
SDS
Corticium centrifugum
-
-
SDS
-
Triton enhances the inhibitory effect
Sodium deoxycholate
-
-
Sodium vanadate
Q6XZB0
0.01 mM, 50% inhibition
taurodeoxycholate
-
-
tetrahydrolipstatin
-
-
thiol reagents
-
protected by 2-mercaptoethanol
tobramycin
-
the inhibition by aminoglycosides appears to be due to substrate depletion caused by binding of aminoglycosides to the negatively charged phospholipid and can be overcome by raising the substrate concentration
Triton X-100
-
-
Triton X-100
A9X3M0
complete inhibition at 5 mM
Triton X-100
K0J3J2
weak inhibition at up to 0.23% w/v
Triton X-100
-
-
Triton X-100
-
at high concentration
Zn2+
Q6KBS7
66% inhibition at 2 mM
Zn2+
A9X3M0
52% relative activity at 5 mM
Mn2+
A9X3M0
complete inhibition at 5 mM
additional information
Q6KBS7
PLA1 is not affected by Mg2+, Cs2+, and EDTA
-
additional information
-
inhibition of RP534 PLA2 activity by nanomolar amounts of the potent, irreversible inhibitor methyl arachidonoyl fluorophosphonate and by the reversible inhibitor arachidonoyl trifluoromethylketone
-
additional information
K0J3J2
the enzyme is not inhibited by EDTA and DTT
-
additional information
-
naturally occuring inhibitors of lysosomal phospholipase A are present in two of the lysosomal-soluble protein fractions obtained in the purification
-
additional information
-
a protein found in Bacillus subtilis specifically inhibits the phospholipase
-
additional information
-
protease inhibitors, e.g. pepstatin, E 64, leupeptin or chymostatin reduce lysosomal acid phospholipase A1 activity in cultured rat hepatocytes
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-propanol
Corticium centrifugum
-
stimulates phospholipase A1 activity and inhibits lysophospholipase 1 activity
dithiothreitol
-
-
Rab22
-
a guanine nucleotide binding protein, activates the VipD phospholipase A1, C-terminal binding
-
Rab5
-
a guanine nucleotide binding protein, activates the VipD phospholipase A1, C-terminal binding, enzyme activity with constitutively active conformation of Rab5, Rab5a Q79L or Rab5c Q80L, is compared with the constitutively inactive forms Rab5a S34N or Rab5c S35N. Active Rab5 stimulates phospholipase activity only in full-length VipD, not in the truncated enzyme comprising residues 2-621
-
sn-1-alkyl-2-oleoyl phosphatidic acid
-
activates
-
Sodium deoxycholate
-
activates
Sodium deoxycholate
-
required for maximal activity
Sodium deoxycholate
-
phospholipase A1 activity is greatly stimulated, lysophospholipase activity is inhibited
Sodium deoxycholate
-
increases the activity against diolein
Triton X-100
-
1%, 12.4fold increase in activity
Triton X-100
-
maximal activity at 0.025%
Triton X-100
-
stimulates
Triton X-100
Corticium centrifugum
-
stimulates phospholipase A1 activity and inhibits lysophospholipase 1 activity
Triton X-100
-
0.05% w/v causes maximal enhancement of activity; increases activity
tumor necrosis factor-alpha
-
stimulates secretion of endothelial lipase, the stimulation can be inhibited by adiponectin
-
dithiothreitol
P53817
required for full activity. Addition of 2 mM increases PLA1/2 activity 167fold
additional information
Q6KBS7
TbPLA1 does not require metal cofactors for activity, but it does require interfacial activation prior to catalysis, activation by Triton X-100/glycerophosphatidylcholine mixed micelle surfaces is not specific and does not require the preformation of a specific enzyme-substrate complex to achieve surface binding, activation kinetics and mechanism, overview
-
additional information
-
endothelial lipase is upregulated by inflammation
-
additional information
P53817
purified H-Rev107 exhibits an 88fold higher PLA1/2 activity than the cytosolic fraction
-
additional information
-
addition of bovine liver superoxide dismutase 1, SOD1, resultes in an increased rate of RP534-catalyzed phospholipid hydrolysis, mechanism, overview
-
additional information
-
the enzyme is activated by the binding of isoprenaline to beta2-adrenergic receptors
-
additional information
-
NO2 specifically reacts with the plasma membrane component of pulmonary artery endothelial cells, causing specific activation of the enzyme
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.5
1-palmitoyl-2-arachidonylglycerophosphocholine
-
-
0.6
diacyl-sn-glycero-3-phosphorylcholine
-
-
0.92
diacyl-sn-glycero-3-phosphorylethanolamine
-
-
2.38
phosphatidic acid
K0J3J2
pH 7.2, 50C, recombinant enzyme
0.11
phosphatidylcholine
Q9X9D8
37C, pH 8.0
1.5
phosphatidylcholine
-
native vesicles, pH 5.4, 37C
4
phosphatidylcholine
-
delipidated vesicles, pH 5.4, 37C
0.0003
phosphatidylglycerol
-
-
1.19
diacyl-sn-glycero-3-phosphorylserine
-
-
additional information
additional information
Q6KBS7
kinetic analysis of enzyme activation
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.1
high-density lipoprotein
-
-
-
630
phosphatidic acid
K0J3J2
pH 7.2, 50C, recombinant enzyme
0.057 - 0.65
phosphatidylcholine
Q9X9D8
37C, pH 8.0
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
265
phosphatidic acid
K0J3J2
pH 7.2, 50C, recombinant enzyme
491
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
8
diisopropyl fluorophosphate
-
IC50: 8 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.42
-
-
1.8
-
-
2.6
-
phosphatidylserine hydrolysis
2.8
-
recombinant PS-PLA1
2.95
-
-
3 - 8
Q6KBS7
recombinant enzyme
3.1
-
1-acyl-2-lysophosphatidylserine hydrolysis
6.383
-
lysosomal enzyme
8.72
-
-
20.6
-
enzyme from plasmalemma
80.2
-
native vesicles, pH 5.4, 37C
84
-
substrate hexadecanoylthioethane-1-phosphocholine
155
-
delipidated vesicles, pH 5.4, 37C
202.3
A9X3M0
recombinant enzyme, after 8.5fold purification, at pH 9.0 and 35C
588 - 2873
K0J3J2
pH 7.2, 50C, purified recombinant enzyme
1192
-
pH 8.0, 37C
2898
A2VBC4
purified enzyme
additional information
-
enzyme activity is markedly enhanced when the amount of negatively-charged lipids included in the vesicles is increased from 10 to around 30% of total phospholipids and the intensity of this effect depends on the nature of the acidic lipids used, ganglioside GM1
additional information
-
lipid-specfic in vivo activity, overview
additional information
-
-
additional information
-
-
additional information
-
-
additional information
Corticium centrifugum
-
-
additional information
-
-
additional information
-
-
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.2 - 4
-
-
3.6 - 3.8
-
-
3.7
-
hydrolysis of cardiolipin
4 - 4.5
Corticium centrifugum
-
-
4 - 5
-
-
4
-
lysosomal enzyme
4.5
-
hydrolysis of phosphatidylglycerol
4.7
H2EIY3
assay at
6 - 6.5
Q93V61
-
6.5 - 7
-
substrate phosphatidylcholine
6.5 - 7
-
hydrolysis of phosphatidylcholine
7
Q6KBS7
assay at
7
-
hydrolysis of 1-palmitoyl-2-arachidonoyl-glycero-3-phosphoethanolamine, in absence of Mg2+
7.5 - 8.5
-
hydrolysis of 1-palmitoyl-2-arachidonoyl-glycero-3-phosphoethanolamine, in presence of Mg2+
7.5
-
assay at
7.6
-
phosphatidylglycerol
7.9
A2VBC4
assay at
7.9
-
phosphatidylethanolamine
8 - 9
-
enzyme from plasmalemma
8
-
assay at
8
-
assay at
8.5 - 9.5
-
-
8.8
-
-
9 - 9.5
-
hydrolysis of diolein
9
Bacteroides melaninogenicus
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.6 - 5.2
-
pH 2.6: 83% of maximal activity, pH 4.5: 50% of maximal activity, pH 5.2: 10% of maximal activity
2.7 - 4.8
-
pH 2.7: 40-60% of maximal activity, pH 4.8: 20-40% of maximal activity
3 - 5
-
50% of maximal activity at pH 3.0 and at pH 5.0, lysosomal enzyme
3 - 7
-
approx. 50% of maximal activity at pH 3.0, approx. 20% of maximal activity at pH 6.0
3.5 - 4.5
-
pH 3.5: about 30% of maximal activity, pH 4.5: about 25% of maximal activity
4 - 11
K0J3J2
activity range, profile overview
5 - 10
-
activity range
5.2 - 8.4
-
pH 5.2: 10% of maximal activity, pH 6.5: about 50% of maximal activity, pH 8.4: optimum
6 - 8
-
about 25% of maximal activity at pH 6.0 and at pH 8.0
6.2 - 9.5
-
approx. 6% of maximal activity at pH 6.2, approx. 23% of maximal activity at pH 9.5
7.8 - 9.3
-
pH 7.8: about 55% of maximal activity, pH 9.3: 90% of maximal activity
8 - 10
-
pH 8.0: about 50% of maximal activity, pH 10.0: about 45% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
Q6KBS7
assay at
35
A9X3M0
recombinant enzyme
36.5
-
assay at
37
A2VBC4
assay at
37
-
assay at
37
-
assay at
37
H2EIY3
assay at
40
-
assay at
50
Bacteroides melaninogenicus
-
-
60 - 65
Q93V61
-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 40
-
4C: about 50% of maximal activity, 40C: 35% of maximal activity
4
-
50% of maximal activity
20 - 70
K0J3J2
activity range, profile overview
27 - 60
Bacteroides melaninogenicus
-
27C: about 25% of maximal activity, 60C: about 55% of maximal activity, strain 576. About 35% of maximal activity at 27C and at 60C, strain 579
35 - 65
-
activity range, immobilized enzyme
additional information
-
temperature profile
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.1
A5YW95
calculated from amino acid sequence
8.85
-
isozme Ves a 1.04, sequence calculation
9.58
-
isozyme Ves a 1.02, sequence calculation
9.96
-
isozyme Ves a 1.03, sequence calculation
10
-
isozyme Ves a 1.01, sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
infective stage, high enzyme activity
Manually annotated by BRENDA team
-
isozyme mPA-PLA1alpha
Manually annotated by BRENDA team
-
isozyme PS-PLA1 or PLA1A
Manually annotated by BRENDA team
-
high expression level
Manually annotated by BRENDA team
Q8WWY8
low mRNA levels
Manually annotated by BRENDA team
-
northern analysis
Manually annotated by BRENDA team
-
isozyme mPA-PLA1alpha
Manually annotated by BRENDA team
-
the enzyme is secreted by the cells of the blood-brain barrier
Manually annotated by BRENDA team
-
low expression in fetal brain
Manually annotated by BRENDA team
Q8WWY8
high mRNA levels
Manually annotated by BRENDA team
-
isozyme mPA-PLA1alpha
Manually annotated by BRENDA team
Tetrahymena pyriformis NT-1
-
-
-
Manually annotated by BRENDA team
-
non-infective stage, low enzyme activity
Manually annotated by BRENDA team
Q948R1
upper parts of stamen filaments in middle-stage flower buds
Manually annotated by BRENDA team
Q8WWY8
low mRNA levels
Manually annotated by BRENDA team
-
northern analysis
Manually annotated by BRENDA team
-
isozyme mPA-PLA1alpha
Manually annotated by BRENDA team
-
isozyme PS-PLA1 or PLA1A
Manually annotated by BRENDA team
-
cortex, only one isoenzyme
Manually annotated by BRENDA team
Q8WWY8
high mRNA levels
Manually annotated by BRENDA team
-
northern analysis
Manually annotated by BRENDA team
-
isozyme mPA-PLA1alpha
Manually annotated by BRENDA team
-
northern analysis
Manually annotated by BRENDA team
Q8WWY8
high mRNA levels
Manually annotated by BRENDA team
-
northern analysis
Manually annotated by BRENDA team
-
isozyme mPA-PLA1alpha
Manually annotated by BRENDA team
-
isozyme PS-PLA1 or PLA1A
Manually annotated by BRENDA team
Q8WWY8
high mRNA levels
Manually annotated by BRENDA team
-
isozyme mPA-PLA1alpha
Manually annotated by BRENDA team
-
PLA1 activity is predominant in the ovaries
Manually annotated by BRENDA team
-
enzyme is the major phospholipase activity present in oviductal fluid
Manually annotated by BRENDA team
Q8WWY8
high mRNA levels
Manually annotated by BRENDA team
-
northern analysis
Manually annotated by BRENDA team
-
pancreatic lipase-related protein 2
Manually annotated by BRENDA team
-
pancreatic lipase-related protein 2, isozyme mPA-PLA1alpha
Manually annotated by BRENDA team
-
northern analysis
Manually annotated by BRENDA team
-
isozyme mPA-PLA1beta
Manually annotated by BRENDA team
Q8WWY8
high mRNA levels
Manually annotated by BRENDA team
-
isozyme mPA-PLA1alpha
Manually annotated by BRENDA team
A5YW95
the enzyme is selectively expressed in young roots at days 4-5 after germination and rapidly declines thereafter
Manually annotated by BRENDA team
-
seminal plasma, containing several phospholipase activities
Manually annotated by BRENDA team
-
northern analysis
Manually annotated by BRENDA team
-
isozyme mPA-PLA1beta
Manually annotated by BRENDA team
-
contains several phospholipase activities
Manually annotated by BRENDA team
-
low expression
Manually annotated by BRENDA team
Q8WWY8
low mRNA levels
Manually annotated by BRENDA team
-
isozyme mPA-PLA1alpha
Manually annotated by BRENDA team
-
high expression
Manually annotated by BRENDA team
-
high expression level
Manually annotated by BRENDA team
Q8WWY8
high mRNA levels
Manually annotated by BRENDA team
-
isozyme mPA-PLA1alpha and isozyme mPA-PLA1beta
Manually annotated by BRENDA team
-
high expression
Manually annotated by BRENDA team
Giardia intestinalis IMSS 0989
-
-
-
Manually annotated by BRENDA team
Q6KBS7
from insect and bloodstream, the latter enzyme form shows a 3fold higher activity
Manually annotated by BRENDA team
-
infective stage, high enzyme activity
Manually annotated by BRENDA team
Trypanosoma brucei 427
-
from insect and bloodstream, the latter enzyme form shows a 3fold higher activity
-
Manually annotated by BRENDA team
-
peritoneal, isozyme PS-PLA1 or PLA1A
Manually annotated by BRENDA team
additional information
-
not expressed in SIMA cell, SH-SY5Y cell, IMR-5 cell, KELLY cell, NB-1 cell, NB-2 cell, NB-3 cell, Nb-4 cell, ERMS-7 cell, ERMS-8 cell, ERMS-10 cell, ARMS-7 cell, ARMS-8 cell, ARMS-9 cell, ARMS-10 cell, adrenal gland, prostate gland, uterus, salivary gland, skeletal muscle, thymus, adult brain, cerebellum, fetal liver kidney, bone marrow, liver, lung, heart, and placenta
Manually annotated by BRENDA team
additional information
-
broad expression of LIPI and LIPH, expression profiles, overview
Manually annotated by BRENDA team
additional information
-
the enzyme protein shows strong colocalization with the Sec23 protein in a number of tissues, including oocyte and male accessory gland
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
predominantly
Manually annotated by BRENDA team
-
secretion by the infective stages, secretion in enhanced by formation of metacyclic forms
-
Manually annotated by BRENDA team
-
the enzyme is secreted by the cells of the blood-brain barrier
-
Manually annotated by BRENDA team
Serratia sp. MK1, Tetrahymena pyriformis NT-1
-
-
-
-
Manually annotated by BRENDA team
-
cis-Golgi and endoplasmic reticulum-Golgi intermediate compartment (ERGIC). Endogenous intracellular PLA1gamma does not appear to be localized to the ERGIC at 37C. At 15C, intracellular PLA1gamma shows marked colocalization with ERGIC-53
-
Manually annotated by BRENDA team
Giardia intestinalis IMSS 0989
-
-
-
Manually annotated by BRENDA team
-
whole-soluble lysosomal fraction
Manually annotated by BRENDA team
Tetrahymena pyriformis NT-1
-
-
-
Manually annotated by BRENDA team
-
associated, phosphatidic acid-specific isozymes mPA-PLA1alpha and mPA-PLA1beta
Manually annotated by BRENDA team
-
associated, phosphatidic acid-specific isozymes mPA-PLA1alpha or lipase H, and mPA-PLA1beta or lacrimal lipase
Manually annotated by BRENDA team
H2EIY3
the enzyme is a membrane-bound/secreted enzyme in the infective stages of Trypanosoma cruzi
Manually annotated by BRENDA team
Q93V61
associated with microsomal membrane
-
Manually annotated by BRENDA team
Bacillus subtilis 168
-
-
-
-
Manually annotated by BRENDA team
additional information
Bacteroides melaninogenicus
-
the activity in a growing bacterial culture increases from the end of the lag phase to the late exponential phase of the growth
-
Manually annotated by BRENDA team
additional information
-
particulate subcellular fraction P30, hemolytic activity correlates with phospholipase activity
-
Manually annotated by BRENDA team
additional information
-
subcellular localization, overview
-
Manually annotated by BRENDA team
additional information
H2EIY3
immunohistochemic analysis of subcellular localization
-
Manually annotated by BRENDA team
additional information
K0J3J2
the enzyme possesses a 33-residue N-terminal signal secretion sequence
-
Manually annotated by BRENDA team
additional information
Bacteroides melaninogenicus 576
-
the activity in a growing bacterial culture increases from the end of the lag phase to the late exponential phase of the growth
-
-
Manually annotated by BRENDA team
additional information
Streptomyces albidoflavus NA297
-
the enzyme possesses a 33-residue N-terminal signal secretion sequence
-
-
Manually annotated by BRENDA team
additional information
Giardia intestinalis IMSS 0989
-
subcellular localization, overview
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
26800
Corticium centrifugum
-
gel filtration
94317
28000
K0J3J2
DLS analysis
729743
29700
Q6KBS7
soluble free enzyme, gel filtration
678064
30000
-
gel filtration
94307
32000
-
SDS-PAGE
690253
33800
A9X3M0
calculated from amino acid sequence
692119
35000
A9X3M0
SDS-PAGE
692119
37000
-
phospholipase A1 Ia, gel filtration
94304
40000
-
gel filtration
649705
42000
-
phospholipase A1 Ib, gel filtration
94304
45000
-
gel filtration
94308
45100
A5YW95
calculated from amino acid sequence
694672
60000
-
sucrose density gradient sedimentation
94324
71500
-
matrix-assisted laser desorption/ionizazion time-of-flight mass spectrometry
650319
137000
Q6KBS7
Triton X-100 micelle-bound PLA1, gel filtration
678064
140000
-
gel filtration
133898
155000
-
gel filtration
94311
230000
-
gel filtration
94332
365000
-
gel filtration
94338
440000
-
gel filtration
94334
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
P53817
x * 19000, SDS-PAGE
?
H2EIY3
x * 38000, SDS-PAGE
?
-
x * 36000, SDS-PAGE
?
-
x * 34000, SDS-PAGE
?
-
x * 29000, SDS-PAGE
?
-
x * 14000, at least six subunits of the native enzyme can be cross-linked, SDS-PAGE
?
-
x * 32000, lysosomal enzyme, SDS-PAGE, x * 75000, enzyme from plasmalemma, SDS-PAGE
?
-
x * 37000, recombinant enzyme, SDS-PAGE
?
Q6XZB0
x * 52991, deduced from nucleotide sequence, x * 55000, SDS-PAGE, immunoblot
?
-
x * 90000, SDS-PAGE, immunoblot
?
Q6Q252
x * 33502, calculated
?
A2VBC4
x * 33961, PLA1, mass spectrometry
?
-
x * 33442-33474, isozymes, mass spectrometry
dimer
-
2 * 27000, SDS-PAGE, OMPLA is only active in the dimeric state, 2 * 31000, OMPLA is only active as a dimer
monomer
-
1 * 38000, SDS-PAGE
monomer
-
1* 67000, SDS-PAGE
monomer
K0J3J2
1 * 27199, mature protein, seuence calculation, 1 * 28000, recombinant extracellular enzyme, SDS-PAGE
tetramer
-
4 * 110000, SDS-PAGE
monomer
Streptomyces albidoflavus NA297
-
1 * 27199, mature protein, seuence calculation, 1 * 28000, recombinant extracellular enzyme, SDS-PAGE
-
additional information
-
amino acid sequence comparison
additional information
Q6Q252
partial amino acid sequence
additional information
-
isozyme tertiary structure analysis, amino acid sequence comparison
additional information
-
isozyme tertiary structure analysis, amino acid sequence comparison, overview
additional information
-
isozyme tertiary structure analysis, overview
additional information
A2VBC4
three-dimensional structure determination and anaylsis, PLA1 shows an alpha/beta fold common to lipases, structure comparison and molecular modeling, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
side-chain modification
-
glycoprotein
glycoprotein
-
indicated by binding to ConA-Sepharose
no glycoprotein
-
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N156A mutant OMPLA is crystallized by hanging drop vapor-diffusion, drops consisting of 0.003 ml of protein solution and 0.002 ml reservoir solution are suspended over a 1 ml reservoir containing 27% 2-methyl-2,4-pentanediol, 0.4-1 mM CaCl2 and 100 mM Bis-Tris buffer, pH 6.0-6.3, the initial protein solution contained 10 mg/ml N156A OMPLA, 10 mM KCl, 1% 1-O-n-octyl-beta-D-glucopyranoside and 0.2 mM Tris-HCl at pH 6.6, crystals diffract to 2.5-3 A
-
purified recombinant enzyme, hanging drop vapour diffusion method, by equilibrating a mixture containing 0.001 ml of 1.0 mg/ml protein solution containing 20 mM Tris-HCl, pH 9.0, and 20 mM NaCl, and 0.001 ml of reservoir solution containing 1.8 M ammonium sulfate, 3% PEG monomethyl ether 2000, and 0.1 M HEPES, pH 7.5, a few days, X-ray diffraction structure determination and analysis at 1.75 A resolution, molecular replacement
K0J3J2
sitting drop vapour diffusion method, at 4C, in 0.1 M Tris-HCl pH 8.0, using PEG 4000 as precipitant
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 10
A9X3M0
the enzyme is stable between pH 6 and 10 at the indicated pH range when incubated at 35C for 3 h, but the enzyme loses about 50% of its activity at pHs below 5.5
692119
5.6 - 9
K0J3J2
recombinant enzyme, stable at
729743
6 - 8
Corticium centrifugum
-
stable
94317
7.2 - 9
K0J3J2
native enzyme, stable at
729743
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0
-
approximately half of the activity remains at 0C
692411
10 - 55
A9X3M0
the enzyme loses most of its activity at 55C but retains about 70% of its maximum activity at 10C, heat treatment at 60C for 10 min results in an 86% decrease in enzyme activity
692119
30
Corticium centrifugum
-
stable up to
94317
37
-
75% loss of activity after 1 h, only little loss of activity in the presence of sn-1-alkyl-2-oleoyl or lysophosphatidic acid containing membranes
650008
37
-
2 h, 20% loss of activity
94308
37
-
5 d, less than 50% loss of activity
94336
40
K0J3J2
native and recombinant enzymes, stable at
729743
45
Corticium centrifugum
-
pH 7.0, rapid loss of activity
94317
50
-
about 50% loss of activity after 2 min
94321
55
Bacteroides melaninogenicus
-
stable up to
94316
60
-
15 min, stable
94336
60
-
5 min, more than 90% loss of activity
94338
70
Q9X9D8
loss of 50% activity after 20 min
649360
70
-
5 min, 50% loss of activity
94308
100
-
5 min, the isozymes show still some activity
731003
100
-
5 min, more than 60% of the activity is recovered
94336
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
membrane lipids increase stability
-
stable in 3% SDS
-
freezing and thawing results in 98% loss of activity of the soluble enzyme and 3% loss of activity of the membrane-bound enzyme
-
treatment with trypsin results in 35% loss of activity of the soluble enzyme and 67% loss of activity of the membrane-bound enzyme
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
acetonitril
Q9X9D8
50%, approx. 90% loss of activity after 10 h
butyl acetate
Q9X9D8
50%, approx. 80% loss of activity after 10 h
butyl acetate
-
50%, approx. 80% loss of activity after 10 h
-
dimethyl sulfoxide
Q9X9D8
50%, almost complete loss of activity after 10 h, approx. 90 min half-life
dimethyl sulfoxide
-
50%, almost complete loss of activity after 10 h, approx. 90 min half-life
-
hexane
Q9X9D8
50%, approx. 85% loss of activity after 10 h
hexane
-
50%, approx. 85% loss of activity after 10 h
-
N,N-dimethylformamide
Q9X9D8
50%, almost complete loss of activity after 10 h
octane
Q9X9D8
50%, approx. 82% loss of activity after 10 h
octane
-
50%, approx. 82% loss of activity after 10 h
-
toluene
Q9X9D8
50%, approx. 80% loss of activity after 10 h
toluene
-
50%, approx. 80% loss of activity after 10 h
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, indefinitely stable
-
4C, stable for at least 2 months
-
-20C, Tris-HCl buffer, pH 9.0, complete loss of activity after 1 month
-
-20C, 50 mM Hepes, 5 mM EDTA, pH 7.4, stable for 48 h, 25% loss of activity after 1 week
-
-20C, stable for at least 1 year
-
-70C, 50% glycerol, stable for 1 year
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant DAD1
Q948R1
recombinant PLA1 expressed in Saccharomyces cerevisiae
-
Superdex 200, partially purified
-
recombinant IPLA-1 from HEK-293 cells
-
-
Corticium centrifugum
-
N156A mutant
-
recombinant OMPLA; recombinant phospholipase A
-
heparin-Sepharose column chromatography and Superdex 200 gel filtration
-
native enzyme 1500fold from thrombin-activated platelets by anion exchange, hydrophobic interaction, and affinity chromatography
-
partial
-
ammonium sulfate, DEAE-cellulofine, ether-Toyopearl, hydroxylapatite, Toyopearl HW 50S
-
native PLA1 21fold from venom by gel filtration and cation exchange chromatography
A2VBC4
DEAE-Sepharose, heparin-Sepharose, Blue-sepharose, partially purified
-
FLAG-tagged H-Rev107 by immunoprecipitation
P53817
recombinant PS-PLA1
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain C41[DE3] by nickel affinity chromatography
-
recombinant His-tagged phospholipase A1; recombinant phospholipase A1
Q9X9D8
recombinant PAL
Q9X9D8
Q sepharose column chromatography
A9X3M0
recombinant enzyme by ammonium sulfate fractionation, hydrophobic interaction and cation exchange chromatography, followed by anion exchange chromatography
K0J3J2
recombinant extracellular enzyme to homogeneity from the culture supernatant by ammonium sulfate precipitation, hydrophobic interaction chromatography, and anion exchange chromatography
K0J3J2
Triton X-100, Blue-Toyopearl, Red-Toyopearl, DEAE-Toyopearl, Green-agarose, Brown-agarose, Polylysine-agarose, Palmitoyl-CoA-agarose, Blue-5PW
-
rapid method, suitable for large-scale production
-
purified from epimastogote homogenate supernatants, DEAE-Trisacryl, ConA-Sepharose 4B, CM-Sepharose
-
soluble portion of recombinant His-tagged enzyme from Escherichia coli strain BL21 (DE3) pLysS by nickel affinity chromatography
H2EIY3
CM cation-exchange column chromatography and C4 reverse-phase HPLC column chromatography
-
by nickel-chelating affinity chromatography
-
recombinant His-tagged Vesv5 and Vesv1 wild-type and His-tagged Vesv1 mutant enzymes from Pichia pastoris strains X33 and KM71H from culture supernatant
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
Q948R1
expression in Saccharomyces cerevisiae and Aspergillus oryzae
-
expression of IPLA-1 in HEK-293 cells
-
expressed in Arabidopsis thaliana
A5YW95
phylogenetic tree, overview
-
gene CG8552, expression of a 31-kb genomic enzyme fragment modified to carry a V5 epitope at the N-terminus, i.e. V5-N-PAPLA1, the recombinant protein is transiently expressed and fully functional in the Drosophila S2 cell line and rescues all the phenotype of a null mutant; gene CG8552, expression of a 31-kb genomic enzyme fragment modified to carry a V5 epitope at the N-terminus, i.e. V5-N-PAPLA1, the recombinant protein is transiently expressed and fully functional in the Drosophila S2 cell line and rescues all the phenotype of a null mutant; gene CG8552, expression of a 31-kb genomic enzyme fragment modified to carry a V5 epitope at the N-terminus, i.e. V5-N-PAPLA1, the recombinant protein is transiently expressed and fully functional in the Drosophila S2 cell line and rescues all the phenotype of a null mutant
M9MRD9, Q9VLS7, X2JDJ3
phylogenetic tree, overview
-
; expression in Escherichia coli
-
expression of N156A mutant
-
LIPH and LIPI, DNA and amino acid sequence determination and analysis, conserved genomic organization of LIPI and LIPH, the LIPI locus is neighbored by a member of the RNA binding motif, RBM, family, RBM11
-
cDNA encoding C-terminally FLAG-tagged H-Rev107. Subcloned into the HindIII and EcoRI sites of pcDNA3.1 (+). Expression vector harboring H-Rev107 cDNA introduced into COS-7 cells
-
cloning of cDNA, transient expression in 293 T cells
-
DNA and amino acid sequence analysis of isozymes, isozyme genetic structures, location of isozyme PS-PLA1 or PLA1A encoding gene on chromosome 3q13.2-q13.3, phylogenetic analysis of isozymes, overview
-
expressed in CHO cells
-
expressed in HEK-293 cells
-
expression HeLa, CHO-K1 and Sf9 cells
Q6XZB0
expression in Sf9 insect cells
Q8WWY8
expression of FLAG-tagged wild-type and mutant enzymes in HeLa cells and in siRNA-treated knockout mutant HeLa cells. Upon overexpression of wild-type enzyme, the tubular structures become fragmented, expression of the mutant S537A has no effect
-
polypeptide (amino acid number 368-486 of intracellular PLA1gamma) expressed as a glutathione S-transferase fusion protein in Escherichia coli. Purified protein used to immunize rats. The cDNA encoding intracellular PLA1gamma cloned into pEGFP-C3 vector and stably expressed in CHO cells
-
recombinant expression in COS-1 cells, recombinant expression in Saccharomyces cerevisiae strain INVSc1, Rab5 enhances the growth defect of yeast cells producing VipD
-
cDNA encoding C-terminally FLAG-tagged H-Rev107. Subcloned into the HindIII and EcoRI sites of pcDNA3.1 (+). Expression vector harboring H-Rev107 cDNA introduced into COS-7 cells
-
DNA and amino acid sequence analysis of isozymes, location of isozyme PS-PLA1 or PLA1A encoding gene on chromosome 16
-
DNA and amino acid sequence analysis
-
expression in Sf9 insect cells
-
expression vector harboring H-Rev107 with a FLAG tag at the N terminus. Expression vector harboring H-Rev107 cDNA introduced into COS-7 cells
P53817
expresssion of His-tagged wild-type and mutant enzymes in Escherichia coli strain C41[DE3]
-
expression in Escherichia coli
-
expression in Escherichia coli; expression of wild-type and PCR evolved phospholipase A1 variants in Escherichia coli
Q9X9D8
expressed in Pichia pastoris
A9X3M0
gene pla, DNA and amino acid sequence determination and analysis, expression and extracellular production of the recombinant enzyme in Streptomyces lividans from expression vector pUC702/pla
K0J3J2
recombinant enzyme expression
K0J3J2
DNA and amino acid equence determination and analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21 (DE3) pLysS, the enzyme is mainly localized in inclusion bodies
H2EIY3
4 isozymes Ves a 1.01-1.04, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, isozyme peptide mapping and sequence comparisons
-
genes Vesv1 and Vesv5, subcloning in Escherichia coli strain Dh5alpha, recombinant expression of His-tagged Vesv5 and Vesv1 wild-type and His-tagged Vesv1 mutant enzymes in Pichia pastoris strains X33 and KM71H as secreted proteins, method optimization, overview
-
PCR product subcloned into the pAcGP67-B baculovirus transfer vector, expressed as wild-type and enzymatically inactivated mutant in Sf9-insect cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of intracellular PLA1gamma is suppressed by transfecting cells with siRNA against intracellular PLA1gamma. Expression of intracellular PLA1gamma protein is decreased to less than 10% that of control siRNA-treated cells
-
increased levels of PLA1 expression in the infective amastigotes and trypomastigotes compared to the non-infective epimastigotes of lethal RA strain
H2EIY3
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D384A
Q93V61
less than 10% of wild-type activity
H409L
Q93V61
less than 10% of wild-type activity
S177A
Q93V61
less than 10% of wild-type activity
T352A
Q93V61
about 70% of wild-type activity
D148N
-
100% of wild-type activity
D149A
-
100% of wild-type activity
D149N
-
approx. 85% of wild-type activity
D184A
-
approx. 30% of wild-type activity
H26C
-
introduced cysteine covalently links 2 OMPLA monomers to an active dimer via disulfide bond
N336Q
-
the mutant shows a significant phospholipase A1 activity on mixed phospholipid-bile salt micelles
S149A
-
catalytically inactive
S537A
-
site-directed mutagenesis, inactive mutant
D286A
-
site-directed mutagenesis, the active site mutant shows highly reduced activity compared to the wild-type enzyme VipD
G288A
-
site-directed mutagenesis, the active site mutant shows highly reduced activity compared to the wild-type enzyme VipD
G43S
-
site-directed mutagenesis, the active site mutant shows highly reduced activity compared to the wild-type enzyme VipD
D264A
-
site-directed mutagenesis, substrate specificity compared to the wild-type enzyme, overview
H218A
K0J3J2
site-directed mutagenesis, inactive mutant
H218R
K0J3J2
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
S11A
K0J3J2
site-directed mutagenesis, inactive mutant
S11D
K0J3J2
site-directed mutagenesis, inactive mutant
S11E
K0J3J2
site-directed mutagenesis, inactive mutant
S11T
K0J3J2
site-directed mutagenesis, inactive mutant
S11Y
K0J3J2
site-directed mutagenesis, inactive mutant
S216A
K0J3J2
site-directed mutagenesis, inactive mutant
S216D
K0J3J2
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
S216E
K0J3J2
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
S216T
K0J3J2
site-directed mutagenesis, the mutant shows 80-90% reduced activity compared to the wild-type enzyme
S216Y
K0J3J2
site-directed mutagenesis, the mutant shows 80-90% reduced activity compared to the wild-type enzyme
H218A
Streptomyces albidoflavus NA297
-
site-directed mutagenesis, inactive mutant
-
S11A
Streptomyces albidoflavus NA297
-
site-directed mutagenesis, inactive mutant
-
S11D
Streptomyces albidoflavus NA297
-
site-directed mutagenesis, inactive mutant
-
S11E
Streptomyces albidoflavus NA297
-
site-directed mutagenesis, inactive mutant
-
S216A
Streptomyces albidoflavus NA297
-
site-directed mutagenesis, inactive mutant
-
D165A
-
site-directed mutagenesis of gene Vesv1
H229A
-
site-directed mutagenesis of gene Vesv1, inactive mutant, that binds IgE antibodies from wasp venom allergic patients and inhibits the binding of wasp venom to IgE antibodies specific for phospholipase A1. The recombinant mutant protein is allergenic in a biological assay as demonstrated by its capability to induce histamine release of wasp venom-sensitive basophils
S137A
-
site-directed mutagenesis of gene Vesv1
S137G/N165A
-
lacks phospholipase activity
Y346F
Q93V61
about 30% of wild-type activity
additional information
-
acl-8 acl-9 acl-10 triple mutations cause misorientation of seam cell divisions similar to that observed in ipla-1 mutants
additional information
-
construction of a gene CG8552 null mutant
S152N
-
approx. 6% of wild-type activity
additional information
-
enzyme immobilization using Lewatit VP OC 1600 as immobilization carrier, method optimization, n-3 polyunsaturated fatty acids-enriched phosphatidylcholine is successfully produced with fatty acid from fish oil and phosphatidylcholine from soybean by immobilized phospholipase A1-catalyzed acidolysis, best at ratio of fatty acid to phophatidylcholine of 8:1 mol/mol, overview. The yield of phosphatidylcholine increases significantly by application of vacuum, even though a slight decrease of n-3 polyunsaturated fatty acid incorporation is observed
additional information
-
gene lpd encoding isozyme mPA-PLA1beta, i.e. the lipid defect locus lipase LPDL, homozygous insertion mutation leads to high levels of triacylglycerols in the plasma and hepatic steatosis
additional information
-
construction of enzyme knockout mutant HeLa cells by treatment with specific siRNA, phenotype, overview
G75A
-
site-directed mutagenesis, the active site mutant shows highly reduced activity compared to the wild-type enzyme VipD
additional information
-
truncated enzyme mutant VipD2-621 is inactive with a primarily cytosolic localization, the loss of enzyme activity is likely not because of a folding defect of the VipD2621 point mutants because they still interact with Rab5c(Q80L)
S73A
-
site-directed mutagenesis, the active site mutant shows highly reduced activity compared to the wild-type enzyme VipD
additional information
-
generation of phosphatidic acid-preferring phospholipase A1 knock-out mice using targeting vector clone PGS00049_B_D06 and specific siRNA, phenotype, overview
additional information
P53817
deletion mutant of H-Rev107 lacking either N-terminal 8 or N-terminal 16 amino acids (DELTAN1, DELTAN2) or C-terminal 25 amino acids (DELTAC1). Expression of the mutants with the expected molecular masses. As for PLA1/2 activity, DELTAN1 shows very low activity (about 3% that of the wild-type), and DELTAN2 and DELTAC1 are entirely inactive
S100A
-
site-directed mutagenesis, substrate specificity compared to the wild-type enzyme, overview
additional information
Q9X9D8
mutants generated by mutagenic and unidirectional reassembly show lipase activity
additional information
Q9X9D8
stability and catalytic activity of phospholipase A1 in the presence of an organic solvent is enhanced by error-prone polymerase chanin reaction and DNA shuffling followed by a filter-based visual screening, thermal stability and catalytic activity of phospholipase A1 are improved by evolutionary molecular engineering
additional information
-
stability and catalytic activity of phospholipase A1 in the presence of an organic solvent is enhanced by error-prone polymerase chanin reaction and DNA shuffling followed by a filter-based visual screening, thermal stability and catalytic activity of phospholipase A1 are improved by evolutionary molecular engineering
-
V260A
-
site-directed mutagenesis, the mutation affects the enzyme's substrate specificity
additional information
-
enzyme immobilization using Lewatit VP OC 1600 as immobilization carrier, method, n-3 polyunsaturated fatty acids-enriched phosphatidylcholine is successfully produced with fatty acid from fish oil and phosphatidylcholine from soybean by immobilized phospholipase A1-catalyzed acidolysis, overview. The yield of phosphatidylcholine increases significantly by application of vacuum, even though a slight decrease of n-3 polyunsaturated fatty acid incorporation is observed
additional information
Q6KBS7
construction of the PLA1 deletion mutant cell line BSF lacking enzyme activity, overview
additional information
Trypanosoma brucei 427
-
construction of the PLA1 deletion mutant cell line BSF lacking enzyme activity, overview
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
-
PLA1 may be used in lysolecithin production
synthesis
-
the enzyme mixture from Thermomyces lanuginosus/Fusarium oxysporum acts as biocatalyst in a solvent-free system containing PLA1 for the modification of phosphatidylcholine from fatty acid saponification of fish oil, overview
food industry
-
the enzyme improves foaming stability and properties of skim milk and whey, implying that phospholipases can be useful tools for modifying the functionality of dairy products and ingredients
nutrition
-
the enzyme improves foaming stability and properties of skim milk and whey, implying that phospholipases can be useful tools for modifying the functionality of dairy products and ingredients
medicine
-
acidotropic accumulation of cocaine in lysosomes inhibits acid phospholipase A1 and inactivates acid sphingomyelinase, inducing a mixed lysosomal lipidosis
synthesis
-
the enzyme mixture from Thermomyces lanuginosus/Fusarium oxysporum acts as biocatalyst in a solvent-free system containing PLA1 for the modification of phosphatidylcholine from fatty acid saponification of fish oil, overview
medicine
-
may provide a valuable tool for diagnostic and therapeutic approaches in hymenoptera venom allergy. Recombinant Ves v 1 is an essential component to assess the sensitisation of individuals to yellow jacket venom and its recombinant availability complemented with Ves v 5 and phospholipase A2 from honeybee venom (Api m 1) allows for clear assignment of sensitisation patterns
pharmacology
-
the recombinant protein is allergenic in a biological assay as demonstrated by its capability to induce histamine release of wasp venom-sensitive basophils. The recombinant phospholipase A1 presents a good candidate for wasp venom immunotherapy