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Information on EC 3.1.1.26 - galactolipase and Organism(s) Homo sapiens
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3.1.1.26 galactolipaseIUBMB Comments
Also acts on 2,3-di-O-acyl-1-O-(6-O-alpha-D-galactosyl-beta-D-galactosyl)-D-glycerol, and phosphatidylcholine and other phospholipids.
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Word Map
- 3.1.1.26
- fabry
- galactose
-
senescence-associated
-
x-linked
- galactolipids
-
lipolytic
- lipases
-
fucosidase
- glycosphingolipids
- globotriaosylceramide
- patatins
- angiokeratomas
-
glucuronidase
- colipase
-
mannosidase
-
exoglycosidase
- anderson-fabry
- monogalactosyldiacylglycerol
- digalactosyldiacylglycerol
-
acroparesthesias
-
patatin-like
- xylosidase
- synthesis
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
galactosidase, galactolipase, plrp1, dongle, lipid acyl hydrolase, pancreatic lipase-related protein 1, vupat1, lipid acyl-hydrolase, galactolipid acyl hydrolase, gplrp2 galactolipase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
pancreatic lipase-related protein 2
PLRP2
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
1,2-diacyl-3-beta-D-galactosyl-sn-glycerol acylhydrolase
Also acts on 2,3-di-O-acyl-1-O-(6-O-alpha-D-galactosyl-beta-D-galactosyl)-D-glycerol, and phosphatidylcholine and other phospholipids.
CAS REGISTRY NUMBER
COMMENTARY
37278-40-3
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,2-di-O-dodecanoyl-3-O-beta-D-galactopyranosyl-sn-glycerol + H2O
2,3-dihydroxypropyl beta-D-galactopyranoside + dodecanoate
1,2-diacyl-3-O-(6-O-alpha-D-galactosyl-beta-D-galactosyl)-sn-glycerol + H2O
2-acyl-3-O-(6-O-alpha-D-galactosyl-beta-D-galactosyl)-sn-glycerol + fatty acid
-
-
-
-
?
3-O-(6-O-alpha-D-galactopyranosyl-beta-D-galactopyranosyl)-1,2-di-O-dodecanoyl-sn-glycerol + H2O
2,3-dihydroxypropyl 6-O-beta-D-galactopyranosyl-beta-D-galactopyranoside + 2 dodecanoate
monogalactosyl dioctanoylglycerol + H2O
galactosylglycerol + 2 octanoate
-
-
-
?
1,2-di-O-dodecanoyl-3-O-beta-D-galactopyranosyl-sn-glycerol + H2O
2,3-dihydroxypropyl beta-D-galactopyranoside + dodecanoate
-
-
-
?
1,2-di-O-dodecanoyl-3-O-beta-D-galactopyranosyl-sn-glycerol + H2O
2,3-dihydroxypropyl beta-D-galactopyranoside + dodecanoate
galactolipase activity of LRP2
-
-
?
3-O-(6-O-alpha-D-galactopyranosyl-beta-D-galactopyranosyl)-1,2-di-O-dodecanoyl-sn-glycerol + H2O
2,3-dihydroxypropyl 6-O-beta-D-galactopyranosyl-beta-D-galactopyranoside + 2 dodecanoate
-
-
-
?
3-O-(6-O-alpha-D-galactopyranosyl-beta-D-galactopyranosyl)-1,2-di-O-dodecanoyl-sn-glycerol + H2O
2,3-dihydroxypropyl 6-O-beta-D-galactopyranosyl-beta-D-galactopyranoside + 2 dodecanoate
galactolipase activity of LRP2
-
-
?
digalactosyldiacylglycerol + H2O
digalactosylglycerol + fatty acid
-
-
-
?
digalactosyldiacylglycerol + H2O
digalactosylglycerol + fatty acid
-
-
-
?
monogalactosyldiacylglycerol + H2O
galactosylglycerol + fatty acid
-
-
-
?
monogalactosyldiacylglycerol + H2O
galactosylglycerol + fatty acid
-
-
-
?
monogalactosyldiacylglycerol + H2O
galactosylglycerol + fatty acid
-
-
-
?
additional information
?
-
-
the main physiological function of the enzyme is the hydrolysis of galactolipids, which are the main lipids present in vegetable food
-
-
?
additional information
?
-
-
the enzyme displays a very low level of activity on phospholipid micelles and monomolecular films. Its activity on monogalactosyldiglyceride monomolecular film is much higher
-
-
?
additional information
?
-
acts preferentially on substrates forming monomers or small aggregates (micelles) dispersed in solution like monoglycerides, phospholipids and galactolipids
-
-
?
additional information
?
-
-
pancreatic lipase-related protein 2 only hydrolyzes one ester bond at the sn-1 position of galactolipids
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
the main physiological function of the enzyme is the hydrolysis of galactolipids, which are the main lipids present in vegetable food
-
-
?
additional information
?
-
acts preferentially on substrates forming monomers or small aggregates (micelles) dispersed in solution like monoglycerides, phospholipids and galactolipids
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
E600
in the absence of bile salts and colipase, the time required to obtain 50% inactivation of PLRP2 by E600 is 3 min, in the presence of 4 mM sodium taurodeoxycholate and colipase, the rate of inhibition of PLRP2 by E600 increases significantly and 50% inhibition is reached within 1 min
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
using the partly soluble short chain tributyrin, the activity of both HPLRP2 N336Q mutant and HPLRP2 is high in the presence of bile salts and in the absence of colipase
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.3
wild type enzyme, using 1,2(2,3)-diolein as substrate, in 1 mM Tris-HCl, at pH 8.0, at 37°C, in the absence of colipase
1756
-
purified enzyme, using natural long chain 1,2-diacyl-3-O-(6-O-alpha-D-galactosyl-beta-D-galactosyl)-sn-glycerol as substrate, at 37°C, pH not specified in the publication
1786
-
purified enzyme, using synthetic medium chain 1,2-diacyl-3-O-beta-D-galactosyl-sn-glycerol as substrate, at 37°C, pH not specified in the publication
212
mutant enzyme N336Q, using tributyrin as substrate, in 1 mM Tris-HCl, at pH 8.0, at 37°C, in the absence of colipase
2441
-
purified enzyme, using natural long chain 1,2-diacyl-3-O-beta-D-galactosyl-sn-glycerol as substrate, at 37°C, pH not specified in the publication
247
mutant enzyme N336Q, using 1(3)-monoolein as substrate, in 1 mM Tris-HCl, at pH 8.0, at 37°C, in the absence of colipase
287
wild type enzyme, using tributyrin as substrate, in 1 mM Tris-HCl, at pH 8.0, at 37°C, in the absence of colipase
2976
-
purified enzyme, using synthetic medium chain 1,2-diacyl-3-O-(6-O-alpha-D-galactosyl-beta-D-galactosyl)-sn-glycerol as substrate, at 37°C, pH not specified in the publication
3.4
mutant enzyme N336Q, using 1,2(2,3)-diolein as substrate, in 1 mM Tris-HCl, at pH 8.0, at 37°C, in the absence of colipase
317
wild type enzyme, using 1(3)-monoolein as substrate, in 1 mM Tris-HCl, at pH 8.0, at 37°C, in the absence of colipase
4.3
mutant enzyme N336Q, using triolein as substrate, in 1 mM Tris-HCl, at pH 8.0, at 37°C, in the absence of colipase
40.2
mutant enzyme N336Q, using trioctanoin as substrate, in 1 mM Tris-HCl, at pH 8.0, at 37°C, in the absence of colipase
43
wild type enzyme, using trioctanoin as substrate, in 1 mM Tris-HCl, at pH 8.0, at 37°C, in the absence of colipase
5
wild type enzyme, using triolein as substrate, in 1 mM Tris-HCl, at pH 8.0, at 37°C, in the absence of colipase
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
pancreatic lipase-related protein 2 is the main enzyme involved in the digestion of these common vegetable lipids in the gastrointestinal tract
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). LIPR2_HUMAN
469
0
51961
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method, using 1.17 M (NH4)2SO4, 0.1 M Na-cacodylate pH 5.5, 0.04 M NaCl for wild type enzyme, and 2.05 M ammonium sulfate, 0.1 M HEPES, pH 6.7 for mutant enzyme N336Q
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
N336Q
the mutant enzyme is not glycosylated and shows identical kinetic properties to the wild type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Superdex 75 gel filtration and Macro-Prep DEAE column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Pichia pastoris
expressed in SF9 insect cells (wild type enzyme) and in Pichia pastoris (mutant enzyme N336Q)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
-
pancreatic lipase-related protein 2 may be used to produce lipid and free fatty acid fractions enriched in either 16:3 n-3 or 18:3 n-3 fatty acids
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sias, B.; Ferrato, F.; Grandval, P.; Lafont, D.; Boullanger, P.; De Caro, A.; Leboeuf, B.; Verger, R.; Carriere, F.
Human pancreatic lipase-related protein 2 is a galactolipase
Biochemistry
43
10138-10148
2004
Homo sapiens
De Caro, J.; Sias, B.; Grandval, P.; Ferrato, F.; Halimi, H.; Carriere, F.; De Caro, A.
Characterization of pancreatic lipase-related protein 2 isolated from human pancreatic juice
Biochim. Biophys. Acta
1701
89-99
2004
Homo sapiens
Eydoux, C.; Spinelli, S.; Davis, T.L.; Walker, J.R.; Seitova, A.; Dhe-Paganon, S.; De Caro, A.; Cambillau, C.; Carriere, F.
Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation
Biochemistry
47
9553-9564
2008
Homo sapiens (P54317)
De Caro, J.; Eydoux, C.; Cherif, S.; Lebrun, R.; Gargouri, Y.; Carriere, F.; De Caro, A.
Occurrence of pancreatic lipase-related protein-2 in various species and its relationship with herbivore diet
Comp. Biochem. Physiol. B
150
1-9
2008
Oryctolagus cuniculus, Felis silvestris, no activity in Bos taurus, no activity in Ovis aries, Myocastor coypus, no activity in Capra hircus, no activity in Struthio camelus, no activity in Meleagris gallopavo, Sus scrofa (B8XY18), Sus scrofa, Canis lupus familiaris (P06857), Homo sapiens (P54315), Homo sapiens (P54317), Homo sapiens, Rattus norvegicus (P54316), Rattus norvegicus (P54318), Cavia porcellus (P81139), Cavia porcellus, Equus caballus (Q95KP4), Equus caballus
Amara, S.; Barouh, N.; Lecomte, J.; Lafont, D.; Robert, S.; Villeneuve, P.; De Caro, A.; Carriere, F.
Lipolysis of natural long chain and synthetic medium chain galactolipids by pancreatic lipase-related protein 2
Biochim. Biophys. Acta
1801
508-516
2010
Cavia porcellus, Homo sapiens
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