BRENDA - Enzyme Database
show all sequences of 3.1.1.111

Structure and function of extracellular phospholipase A1 belonging to the pancreatic lipase gene family

Aoki, J.; Inoue, A.; Makide, K.; Saiki, N.; Arai, H.; Biochimie 89, 197-204 (2007) View publication on PubMed

Data extracted from this reference:

Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
extracellular
-
Homo sapiens
-
-
Organism
Organism
UniProt
Commentary
Textmining
Homo sapiens
Q53H76
-
-
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
extracellular
-
Homo sapiens
-
-
General Information
General Information
Commentary
Organism
physiological function
review on extracellular PLA1s including phosphatidylserine-specific PLA1, membrane-associated phosphatidic acid-selective mPA-PLA1alpha and mPA-PLA1beta. The tertiary structures of lipases show two surface loops, the lid and the beta9 loop. The lid and the beta9 loop cover the active site in its closed conformation. Phosphatidylserine-specific PLA1, membrane-associated phosphatidic acid-selective mPA-PLA1alpha and mPA-PLA1beta have short lids and short loops. They specifically hydrolyze phospatidylserine and phosphatidic acid, respectively, producing their corresponding lysophospholipids
Homo sapiens
General Information (protein specific)
General Information
Commentary
Organism
physiological function
review on extracellular PLA1s including phosphatidylserine-specific PLA1, membrane-associated phosphatidic acid-selective mPA-PLA1alpha and mPA-PLA1beta. The tertiary structures of lipases show two surface loops, the lid and the beta9 loop. The lid and the beta9 loop cover the active site in its closed conformation. Phosphatidylserine-specific PLA1, membrane-associated phosphatidic acid-selective mPA-PLA1alpha and mPA-PLA1beta have short lids and short loops. They specifically hydrolyze phospatidylserine and phosphatidic acid, respectively, producing their corresponding lysophospholipids
Homo sapiens
Other publictions for EC 3.1.1.111
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
753940
Sawada
Serum phosphatidylserine-spec ...
Homo sapiens
Int. J. Rheum. Dis.
22
2059-2066
2019
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1
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3
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754543
Guo
Phosphatidylserine-specific p ...
Homo sapiens
J. Virol.
89
2367-2377
2015
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1
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4
-
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1
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753210
Hosono
Expression of phosphatidylser ...
Homo sapiens
Cell Transplant.
19
759-764
2010
-
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-
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1
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2
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2
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753301
Nakamura
A novel enzyme immunoassay fo ...
Homo sapiens
Clin. Chim. Acta
411
1090-1094
2010
-
1
1
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1
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752867
Aoki
Structure and function of ext ...
Homo sapiens
Biochimie
89
197-204
2007
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1
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1
1
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754071
Hiramatsu
Biochemical and molecular cha ...
Homo sapiens
J. Biol. Chem.
278
49438-49447
2003
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1
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1
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1
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1
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1
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1
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650365
oki
Structure and function of phos ...
Rattus norvegicus
Biochim. Biophys. Acta
1582
26-32
2002
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4
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652153
Hosono
Phosphatidylserine-specific ph ...
Rattus norvegicus
J. Biol. Chem.
276
29664-29670
2001
-
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1
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754062
Hosono
Phosphatidylserine-specific p ...
Rattus norvegicus
J. Biol. Chem.
276
29664-29670
2001
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1
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754052
Nagai
An alternative splicing form ...
Homo sapiens
J. Biol. Chem.
274
11053-11059
1999
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6
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754048
Sato
Serine phospholipid-specific ...
Rattus norvegicus
J. Biol. Chem.
272
2192-2198
1997
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1
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1
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6
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