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Information on EC 3.1.1.26 - galactolipase
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EC Tree
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 enzyme appears in 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, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
chGL
ckGL
DGL
-
shows strong galactolipase and weak phospholipase A1 activities and plays a role in the early phase of jasmonic acid production
FSL
galactolipase
glp1
LAH
lipid acyl hydrolase
NECHADRAFT_49364
pancreatic lipase-related protein 1
pancreatic lipase-related protein 2
PLRP1
PLRP2
Talaromyces thermophilus lipase
TTL
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1,2-diacyl-3-beta-D-galactosyl-sn-glycerol + 2 H2O = 3-beta-D-galactosyl-sn-glycerol + 2 carboxylates
also acts on 2,3-di-O-acyl-1-O-(6-O-alpha-D-galactosyl)-D-glycerol, and phosphatidylcholine and other phospholipids
-
-
-
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PATHWAY SOURCE
PATHWAYS
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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.
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CAS REGISTRY NUMBER
COMMENTARY
37278-40-3
-
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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-alpha-eleostearoyl-3-O-beta-D-galactopyranosyl-sn-glycerol + H2O
? + alpha-eleostearic acid
best substrate
-
-
?
1,2-di-O-dodecanoyl-3-O-beta-D-galactopyranosyl-sn-glycerol + H2O
2,3-dihydroxypropyl beta-D-galactopyranoside + dodecanoate
1,2-diacyl-3-(6-O-alpha-D-Gal-beta-D-Gal)glycerol + H2O
2,3-dihydroxypropyl 6-O-alpha-D-galactopyranosyl-beta-D-galactopyranoside + 2 fatty acid
-
-
-
-
?
1,2-diacyl-3-beta-D-galactosyl-sn-glycerol + H2O
2-acyl-3-beta-D-galactosyl-sn-glycerol + fatty acid
-
-
-
?
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
1,2-diacyl-3-O-alpha-D-galactosyl-(1->6)-beta-D-galactosyl-sn-glycerol + H2O
2-acyl-3-O-alpha-D-galactosyl-(1->6)-beta-D-galactosyl-sn-glycerol + fatty acid
-
-
-
?
1,2-didodecanoyl phosphatidylglycerol + 2 H2O
2 dodecanoate + sn-glycerol 3-phosphate
-
-
-
-
?
1,2-dimyristoyl-sn-glycero-3-phosphate + H2O
2-myristoyl-sn-glycero-3-phosphate + myristate
-
-
-
?
1,2-octanoyl-3-O-alpha-D-galactosyl-(1->6)-beta-D-galactosyl-sn-glycerol + H2O
2-octanoyl-3-O-alpha-D-galactosyl-(1->6)-beta-D-galactosyl-sn-glycerol + octanoate
1,2-octanoyl-3-O-alpha-D-galactosyl-sn-glycerol + H2O
2-octanoyl-3-O-alpha-D-galactosyl-sn-glycerol + octanoate
1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-(1'-rac-)glycerol + H2O
2-oleoyl-sn-glycero-3-phospho-(1'-rac-)glycerol + palmitate
-
-
-
?
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine + H2O
2-oleoyl-sn-glycero-3-phosphocholine + palmitate
low activity
-
-
?
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine + H2O
?
low activity
-
-
?
3-O-(6-O-alpha-D-galactopyranosyl-beta-D-galactopyranosyl)-1,2-di-O-dodecanoyl-sn-glycerol + 2 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
3-O-(6-O-alpha-D-galactopyranosyl-beta-D-galactopyranosyl)-1,2-di-O-octanoyl-sn-glycerol + H2O
?
-
-
-
?
3-O-beta-D-galactopyranosyl-1,2-di-O-dodecanoyl-sn-glycerol + fatty acid + H2O
2,3-dihydroxypropyl-beta-D-galactopyranoside + dodecanoate
-
-
-
-
?
acylsterylglucoside + H2O
?
-
500% of the activity with monogalactosyldiacylglycerol
-
-
?
digalactosyldilinolenin + H2O
digalactosylglycerol + linolenic acid
-
-
-
-
?
monogalactosyl dioctanoylglycerol + H2O
galactosylglycerol + 2 octanoate
-
-
-
?
monogalactosyldilinolenin + H2O
monogalactosylglycerol + linolenic acid
-
-
-
-
?
phosphatidylcholine + H2O
lysophosphatidylcholine + fatty acid
-
-
-
-
?
phosphatidylinositol + H2O
?
-
36% of the activity with monogalactosyldiacylglycerol
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
1,2-di-O-dodecanoyl-3-O-beta-D-galactopyranosyl-sn-glycerol + H2O
2,3-dihydroxypropyl beta-D-galactopyranoside + dodecanoate
galactolipase activity of LRP2
-
-
?
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
-
-
-
-
?
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
-
-
-
?
1,2-diacyl-3-beta-D-galactosyl-sn-glycerol + H2O
?
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
1,2-diacyl-3-O-alpha-D-galactosyl-(1->6)-beta-D-galactosyl-sn-glycerol + H2O
?
-
-
-
?
1,2-diacyl-3-O-alpha-D-galactosyl-(1->6)-beta-D-galactosyl-sn-glycerol + H2O
?
-
-
-
?
1,2-octanoyl-3-O-alpha-D-galactosyl-(1->6)-beta-D-galactosyl-sn-glycerol + H2O
2-octanoyl-3-O-alpha-D-galactosyl-(1->6)-beta-D-galactosyl-sn-glycerol + octanoate
-
-
-
?
1,2-octanoyl-3-O-alpha-D-galactosyl-(1->6)-beta-D-galactosyl-sn-glycerol + H2O
2-octanoyl-3-O-alpha-D-galactosyl-(1->6)-beta-D-galactosyl-sn-glycerol + octanoate
-
-
-
?
1,2-octanoyl-3-O-alpha-D-galactosyl-(1->6)-beta-D-galactosyl-sn-glycerol + H2O
2-octanoyl-3-O-alpha-D-galactosyl-(1->6)-beta-D-galactosyl-sn-glycerol + octanoate
-
-
-
?
1,2-octanoyl-3-O-alpha-D-galactosyl-(1->6)-beta-D-galactosyl-sn-glycerol + H2O
2-octanoyl-3-O-alpha-D-galactosyl-(1->6)-beta-D-galactosyl-sn-glycerol + octanoate
-
-
-
?
1,2-octanoyl-3-O-alpha-D-galactosyl-(1->6)-beta-D-galactosyl-sn-glycerol + H2O
2-octanoyl-3-O-alpha-D-galactosyl-(1->6)-beta-D-galactosyl-sn-glycerol + octanoate
-
-
-
?
1,2-octanoyl-3-O-alpha-D-galactosyl-sn-glycerol + H2O
2-octanoyl-3-O-alpha-D-galactosyl-sn-glycerol + octanoate
-
-
-
?
1,2-octanoyl-3-O-alpha-D-galactosyl-sn-glycerol + H2O
2-octanoyl-3-O-alpha-D-galactosyl-sn-glycerol + octanoate
-
-
-
?
1,2-octanoyl-3-O-alpha-D-galactosyl-sn-glycerol + H2O
2-octanoyl-3-O-alpha-D-galactosyl-sn-glycerol + octanoate
-
-
-
?
1,2-octanoyl-3-O-alpha-D-galactosyl-sn-glycerol + H2O
2-octanoyl-3-O-alpha-D-galactosyl-sn-glycerol + octanoate
-
-
-
?
1,2-octanoyl-3-O-alpha-D-galactosyl-sn-glycerol + H2O
2-octanoyl-3-O-alpha-D-galactosyl-sn-glycerol + octanoate
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
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
-
-
?
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
-
-
-
-
?
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
-
-
-
?
digalactosyldiacylglycerol + H2O
digalactosylglycerol + fatty acid
-
-
-
-
?
digalactosyldiacylglycerol + H2O
digalactosylglycerol + fatty acid
-
-
-
-
?
digalactosyldiacylglycerol + H2O
digalactosylglycerol + fatty acid
-
-
-
-
?
digalactosyldiacylglycerol + H2O
digalactosylglycerol + fatty acid
-
-
-
?
digalactosyldiacylglycerol + H2O
digalactosylglycerol + fatty acid
-
-
-
?
digalactosyldiacylglycerol + H2O
digalactosylglycerol + fatty acid
-
hydrolyzes both the saturated and unsaturated acyl groups
-
?
digalactosyldiacylglycerol + H2O
digalactosylglycerol + fatty acid
-
-
-
?
digalactosyldiacylglycerol + H2O
digalactosylglycerol + fatty acid
-
-
-
?
digalactosyldiacylglycerol + H2O
digalactosylglycerol + fatty acid
-
-
-
-
?
digalactosyldiacylglycerol + H2O
digalactosylglycerol + fatty acid
-
-
-
?
digalactosyldiacylglycerol + H2O
digalactosylglycerol + fatty acid
-
-
-
?
digalactosyldiacylglycerol + H2O
digalactosylglycerol + fatty acid
-
-
-
-
?
digalactosyldiacylglycerol + H2O
digalactosylglycerol + fatty acid
-
-
-
-
?
digalactosyldiacylglycerol + H2O
digalactosylglycerol + fatty acid
-
-
-
-
?
digalactosyldiacylglycerol + H2O
digalactosylglycerol + fatty acid
-
-
-
-
?
digalactosyldiacylglycerol + H2O
digalactosylglycerol + fatty acid
-
-
-
-
?
digalactosyldiacylglycerol + H2O
digalactosylglycerol + fatty acid
-
169% of the activity with monogalactosyldiacylglycerol
-
-
?
digalactosyldiacylglycerol + H2O
digalactosylglycerol + fatty acid
-
-
-
-
?
digalactosyldiacylglycerol + H2O
digalactosylglycerol + fatty acid
-
-
-
-
?
digalactosyldiacylglycerol + H2O
digalactosylglycerol + fatty acid
-
39% of the activity with monogalactosyldiacylglycerol
-
-
?
digalactosyldiacylglycerol + H2O
digalactosylglycerol + fatty acid
Pisum arvense
-
-
-
-
?
digalactosyldiacylglycerol + H2O
digalactosylglycerol + fatty acid
-
-
-
-
?
digalactosyldiacylglycerol + H2O
digalactosylglycerol + fatty acid
-
-
-
-
?
digalactosyldiacylglycerol + H2O
digalactosylglycerol + fatty acid
-
-
-
?
digalactosyldiacylglycerol + H2O
digalactosylglycerol + fatty acid
-
-
-
-
?
digalactosyldiacylglycerol + H2O
digalactosylglycerol + fatty acid
-
-
-
-
?
digalactosyldiacylglycerol + H2O
digalactosylglycerol + fatty acid
-
-
-
-
?
digalactosyldiacylglycerol + H2O
digalactosylglycerol + fatty acid
-
44% of the activity with monogalactosyldiacylglycerol
-
-
?
digalactosyldiacylglycerol + H2O
digalactosylglycerol + fatty acid
-
62% of the activity with monogalactosyldiacylglycerol
-
-
?
digalactosyldiacylglycerol + H2O
digalactosylglycerol + fatty acid
-
-
-
-
?
digalactosyldiacylglycerol + H2O
digalactosylglycerol + fatty acid
-
-
-
?
digalactosyldiacylglycerol + H2O
digalactosylglycerol + fatty acid
-
-
?
digalactosyldiacylglycerol + H2O
digalactosylglycerol + fatty acid
-
-
?
digalactosyldiacylglycerol + H2O
digalactosylglycerol + fatty acid
-
fatty acid with chain lengths of C16:0, C16:1, C18:1, C18:2, C18:3, the polyunsaturated substrates are preferentially hydrolyzed
-
-
?
digalactosyldiacylglycerol + H2O
digalactosylglycerol + fatty acid
-
-
-
-
?
digalactosylmonoacylglycerol + H2O
digalactosylglycerol + fatty acid
-
49% of the activity with monogalactosyldiacylglycerol
-
-
?
digalactosylmonoacylglycerol + H2O
digalactosylglycerol + fatty acid
-
146% of the activity with monogalactosyldiacylglycerol
-
-
?
digalactosylmonoacylglycerol + H2O
digalactosylglycerol + fatty acid
-
26% of the activity with monogalactosyldiacylglycerol
-
-
?
lysophosphatidylcholine + H2O
?
-
33% of the activity with monogalactosyldiacylglycerol
-
-
?
lysophosphatidylcholine + H2O
?
-
89% of the activity with monogalactosyldiacylglycerol
-
-
?
lysophosphatidylcholine + H2O
?
-
26% of the activity with monogalactosyldiacylglycerol
-
-
?
lysophosphatidylcholine + H2O
?
-
304% of the activity with monogalactosyldiacylglycerol
-
-
?
lysophosphatidylethanolamine + H2O
?
-
32% of the activity with monogalactosyldiacylglycerol
-
-
?
lysophosphatidylethanolamine + H2O
?
-
6% of the activity with monogalactosyldiacylglycerol
-
-
?
lysophosphatidylethanolamine + H2O
?
-
71% of the activity with monogalactosyldiacylglycerol
-
-
?
lysophosphatidylglycerol + H2O
?
-
93% of the activity with monogalactosyldiacylglycerol
-
-
?
lysophosphatidylglycerol + H2O
?
-
89% of the activity with monogalactosyldiacylglycerol
-
-
?
lysophosphatidylglycerol + H2O
?
-
20% of the activity with monogalactosyldiacylglycerol
-
-
?
monogalactosyldiacylglycerol + H2O
?
-
extent of polar lipids breakdown in chill-sensitive and chill-tolerant inbreeds during chilling and post-chilling rewarming is correlated with galactolipase activity in chloroplast
-
-
?
monogalactosyldiacylglycerol + H2O
galactosylglycerol + fatty acid
-
high activity
-
-
?
monogalactosyldiacylglycerol + H2O
galactosylglycerol + fatty acid
-
-
-
-
?
monogalactosyldiacylglycerol + H2O
galactosylglycerol + fatty acid
-
-
-
-
?
monogalactosyldiacylglycerol + H2O
galactosylglycerol + fatty acid
-
-
-
?
monogalactosyldiacylglycerol + H2O
galactosylglycerol + fatty acid
-
-
-
-
?
monogalactosyldiacylglycerol + H2O
galactosylglycerol + fatty acid
-
-
-
?
monogalactosyldiacylglycerol + H2O
galactosylglycerol + fatty acid
-
best substrate, hydrolyzes both the saturated and unsaturated acyl groups
-
?
monogalactosyldiacylglycerol + H2O
galactosylglycerol + fatty acid
-
-
-
?
monogalactosyldiacylglycerol + H2O
galactosylglycerol + fatty acid
-
-
-
-
?
monogalactosyldiacylglycerol + H2O
galactosylglycerol + fatty acid
-
-
-
?
monogalactosyldiacylglycerol + H2O
galactosylglycerol + fatty acid
-
-
-
?
monogalactosyldiacylglycerol + H2O
galactosylglycerol + fatty acid
-
-
-
?
monogalactosyldiacylglycerol + H2O
galactosylglycerol + fatty acid
-
-
-
-
?
monogalactosyldiacylglycerol + H2O
galactosylglycerol + fatty acid
-
-
-
-
?
monogalactosyldiacylglycerol + H2O
galactosylglycerol + fatty acid
-
-
-
-
?
monogalactosyldiacylglycerol + H2O
galactosylglycerol + fatty acid
-
-
-
-
?
monogalactosyldiacylglycerol + H2O
galactosylglycerol + fatty acid
-
-
-
-
?
monogalactosyldiacylglycerol + H2O
galactosylglycerol + fatty acid
-
best substrate
-
-
?
monogalactosyldiacylglycerol + H2O
galactosylglycerol + fatty acid
-
-
-
-
?
monogalactosyldiacylglycerol + H2O
galactosylglycerol + fatty acid
-
-
-
-
?
monogalactosyldiacylglycerol + H2O
galactosylglycerol + fatty acid
-
best substrate
-
-
?
monogalactosyldiacylglycerol + H2O
galactosylglycerol + fatty acid
Pisum arvense
-
-
-
-
?
monogalactosyldiacylglycerol + H2O
galactosylglycerol + fatty acid
-
-
-
-
?
monogalactosyldiacylglycerol + H2O
galactosylglycerol + fatty acid
-
-
-
-
?
monogalactosyldiacylglycerol + H2O
galactosylglycerol + fatty acid
-
-
-
?
monogalactosyldiacylglycerol + H2O
galactosylglycerol + fatty acid
-
-
-
-
?
monogalactosyldiacylglycerol + H2O
galactosylglycerol + fatty acid
-
-
-
-
?
monogalactosyldiacylglycerol + H2O
galactosylglycerol + fatty acid
-
-
-
-
?
monogalactosyldiacylglycerol + H2O
galactosylglycerol + fatty acid
-
-
-
-
?
monogalactosyldiacylglycerol + H2O
galactosylglycerol + fatty acid
-
-
-
-
?
monogalactosyldiacylglycerol + H2O
galactosylglycerol + fatty acid
-
-
-
-
?
monogalactosyldiacylglycerol + H2O
galactosylglycerol + fatty acid
-
-
-
-
?
monogalactosyldiacylglycerol + H2O
galactosylglycerol + fatty acid
-
-
?
monogalactosyldiacylglycerol + H2O
galactosylglycerol + fatty acid
-
-
?
monogalactosyldiacylglycerol + H2O
galactosylglycerol + fatty acid
-
substrates with chain lengths of C16:0, C16:1, C18:1, C18:2, C18:3, the polyunsaturated substrates are preferentially hydrolyzed
-
-
?
monogalactosyldiacylglycerol + H2O
galactosylglycerol + fatty acid
-
-
-
-
?
monogalactosylmonoacylglycerol + H2O
monogalactosylglycerol + fatty acid
-
111% of the activity with monogalactosyldiacylglycerol
-
-
?
monogalactosylmonoacylglycerol + H2O
monogalactosylglycerol + fatty acid
-
132% of the activity with monogalactosyldiacylglycerol
-
-
?
monogalactosylmonoacylglycerol + H2O
monogalactosylglycerol + fatty acid
-
394% of the activity with monogalactosyldiacylglycerol
-
-
?
monogalactosylmonoacylglycerol + H2O
monogalactosylglycerol + fatty acid
-
68% of the activity with monogalactosyldiacylglycerol
-
-
?
phosphatidic acid + H2O
?
-
7% of the activity with monogalactosyldiacylglycerol
-
-
?
phosphatidic acid + H2O
?
-
8% of the activity with monogalactosyldiacylglycerol
-
-
?
phosphatidic acid + H2O
?
-
16% of the activity with monogalactosyldiacylglycerol
-
-
?
phosphatidylcholine + H2O
?
from henn egg yolk
-
-
?
phosphatidylcholine + H2O
?
-
27% of the activity with monogalactosyldiacylglycerol
-
-
?
phosphatidylcholine + H2O
?
-
31% of the activity with monogalactosyldiacylglycerol
-
-
?
phosphatidylcholine + H2O
?
-
equal activity compared to monogalactosyldiacylglycerol
-
-
?
phosphatidylcholine + H2O
?
-
14% of the activity with monogalactosyldiacylglycerol
-
-
?
phosphatidylcholine + H2O
?
-
fatty acid with chain lengths of C16:0, C16:1, C18:1, C18:2, C18:3, the polyunsaturated substrates are preferentially hydrolyzed
-
-
?
phosphatidylethanolamine + H2O
?
-
traces of the activity with monogalactosyldiacylglacerol
-
-
?
phosphatidylethanolamine + H2O
?
-
11% of the activity with monogalactosyldiacylglycerol
-
-
?
phosphatidylethanolamine + H2O
?
-
33% of the activity with monogalactosyldiacylglycerol
-
-
?
phosphatidylethanolamine + H2O
?
-
1% of the activity with monogalactosyldiacylglycerol
-
-
?
phosphatidylglycerol + H2O
?
-
47% of the activity with monogalactosyldiacylglycerol
-
-
?
phosphatidylglycerol + H2O
?
-
77% of the activity with monogalactosyldiacylglycerol
-
-
?
phosphatidylglycerol + H2O
?
-
151% of the activity with monogalactosyldiacylglycerol
-
-
?
phosphatidylglycerol + H2O
?
-
fatty acid with chain lengths of C16:0, C16:1, C18:1, C18:2, C18:3, the polyunsaturated substrates are preferentially hydrolyzed
-
-
?
phosphatidylglycerol + H2O
?
-
fatty acid with chain lengths of C16:0, C16:1, C18:1, C18:2, C18:3
-
-
?
sulfoquinovosyldiaclglycerol + H2O
?
-
14% of the activity with monogalactosyldiacylglycerol
-
-
?
sulfoquinovosyldiaclglycerol + H2O
?
-
43% of the activity with monogalactosyldiacylglycerol
-
-
?
sulfoquinovosyldiaclglycerol + H2O
?
-
52% of the activity with monogalactosyldiacylglycerol
-
-
?
triacylglycerol + H2O
?
-
traces of the activity with monogalactosyldiacylglycerol
-
-
?
triacylglycerol + H2O
?
-
below 0.1% of the activity with monogalactosyldiacylglycerol
-
-
?
triacylglycerol + H2O
?
-
below 0.1% of the activity with monogalactosyldiacylglycerol
-
-
?
additional information
?
-
-
the enzyme hydrolyzes the membrane lipids to release various saturated and unsaturated fatty acids, including arachidonic acid as substrate for prostaglandin synthesis
-
-
?
additional information
?
-
-
pancreatic lipase-related protein 2 only hydrolyzes one ester bond at the sn-1 position of galactolipids
-
-
?
additional information
?
-
the purified (phospho)lipase of Fusariumsolani (FSL) is active on both triglycerides and phospholipids. But the enzyme is also capable of hydrolyzing galactolipids. FSL hydrolyzes synthetic medium chain-length substrates monogalactosyldiacylglycerol and digalactosyldiacylglycerol at high rates, as well as natural long chain monogalactosyldiacylglycerol extracted from leek leaves. It is the microbial enzyme with the highest activity on galactolipids identified so far with a level of activity comparable to that of pancreatic lipase-related protein 2. Enzyme FSL has a broad substrate specificity towards different classes of lipids, triglycerides, phospholipids and galactolipids
-
-
?
additional information
?
-
the purified (phospho)lipase of Fusariumsolani (FSL) is active on both triglycerides and phospholipids. But the enzyme is also capable of hydrolyzing galactolipids. FSL hydrolyzes synthetic medium chain-length substrates monogalactosyldiacylglycerol and digalactosyldiacylglycerol at high rates, as well as natural long chain monogalactosyldiacylglycerol extracted from leek leaves. It is the microbial enzyme with the highest activity on galactolipids identified so far with a level of activity comparable to that of pancreatic lipase-related protein 2. Enzyme FSL has a broad substrate specificity towards different classes of lipids, triglycerides, phospholipids and galactolipids
-
-
?
additional information
?
-
the purified (phospho)lipase of Fusariumsolani (FSL) is active on both triglycerides and phospholipids. But the enzyme is also capable of hydrolyzing galactolipids. FSL hydrolyzes synthetic medium chain-length substrates monogalactosyldiacylglycerol and digalactosyldiacylglycerol at high rates, as well as natural long chain monogalactosyldiacylglycerol extracted from leek leaves. It is the microbial enzyme with the highest activity on galactolipids identified so far with a level of activity comparable to that of pancreatic lipase-related protein 2. Enzyme FSL has a broad substrate specificity towards different classes of lipids, triglycerides, phospholipids and galactolipids
-
-
?
additional information
?
-
the purified (phospho)lipase of Fusariumsolani (FSL) is active on both triglycerides and phospholipids. But the enzyme is also capable of hydrolyzing galactolipids. FSL hydrolyzes synthetic medium chain-length substrates monogalactosyldiacylglycerol and digalactosyldiacylglycerol at high rates, as well as natural long chain monogalactosyldiacylglycerol extracted from leek leaves. It is the microbial enzyme with the highest activity on galactolipids identified so far with a level of activity comparable to that of pancreatic lipase-related protein 2. Enzyme FSL has a broad substrate specificity towards different classes of lipids, triglycerides, phospholipids and galactolipids
-
-
?
additional information
?
-
the purified (phospho)lipase of Fusariumsolani (FSL) is active on both triglycerides and phospholipids. But the enzyme is also capable of hydrolyzing galactolipids. FSL hydrolyzes synthetic medium chain-length substrates monogalactosyldiacylglycerol and digalactosyldiacylglycerol at high rates, as well as natural long chain monogalactosyldiacylglycerol extracted from leek leaves. It is the microbial enzyme with the highest activity on galactolipids identified so far with a level of activity comparable to that of pancreatic lipase-related protein 2. Enzyme FSL has a broad substrate specificity towards different classes of lipids, triglycerides, phospholipids and galactolipids
-
-
?
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
-
-
?
additional information
?
-
galactolipase (ckGL) hydrolyzes the acyl ester bond of galactolipids such as digalactosyldiacylglycerol (DGDG)
-
-
?
additional information
?
-
-
galactolipase (ckGL) hydrolyzes the acyl ester bond of galactolipids such as digalactosyldiacylglycerol (DGDG)
-
-
?
additional information
?
-
galactolipase (ckGL) hydrolyzes the acyl ester bond of galactolipids such as digalactosyldiacylglycerol, substrate specificity in descending order: digalactosyldiacylglycerol (100%), monogalactosyldiacylglycerol and phosphatidylglycerol (about 40%), sulfoquinovosyldiacylglycerol (about 20%). The enzyme exhibits mostly no activity toward glycerides and other phospholipids. e.g. 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoserine and 1,2-dimyristoyl-sn-glycero-3-phosphate, or tristearin, diplamitin, and olive oil. ckGL preferably hydrolyzes the sn-1 acyl ester bond in the substrates
-
-
?
additional information
?
-
-
galactolipase (ckGL) hydrolyzes the acyl ester bond of galactolipids such as digalactosyldiacylglycerol, substrate specificity in descending order: digalactosyldiacylglycerol (100%), monogalactosyldiacylglycerol and phosphatidylglycerol (about 40%), sulfoquinovosyldiacylglycerol (about 20%). The enzyme exhibits mostly no activity toward glycerides and other phospholipids. e.g. 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoserine and 1,2-dimyristoyl-sn-glycero-3-phosphate, or tristearin, diplamitin, and olive oil. ckGL preferably hydrolyzes the sn-1 acyl ester bond in the substrates
-
-
?
additional information
?
-
galactolipase (ckGL) hydrolyzes the acyl ester bond of galactolipids such as digalactosyldiacylglycerol (DGDG)
-
-
?
additional information
?
-
galactolipase (ckGL) hydrolyzes the acyl ester bond of galactolipids such as digalactosyldiacylglycerol, substrate specificity in descending order: digalactosyldiacylglycerol (100%), monogalactosyldiacylglycerol and phosphatidylglycerol (about 40%), sulfoquinovosyldiacylglycerol (about 20%). The enzyme exhibits mostly no activity toward glycerides and other phospholipids. e.g. 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoserine and 1,2-dimyristoyl-sn-glycero-3-phosphate, or tristearin, diplamitin, and olive oil. ckGL preferably hydrolyzes the sn-1 acyl ester bond in the substrates
-
-
?
additional information
?
-
-
the enzyme utilizes galactolipids, phospholipids, sulpholipids and phosphatidylglycerol as substrates, releasing fatty acids esterified to the hydroxyl groups at carbon 1 and 2 of glycerol
-
-
?
additional information
?
-
-
the enzyme utilizes galactolipids, phospholipids, sulpholipids and phosphatidylglycerol as substrates, releasing fatty acids esterified to the hydroxyl groups at carbon 1 and 2 of glycerol
-
-
?
additional information
?
-
Talaromyces thermophilus lipase (TTL, EC 3.1.1.3) also hydrolyzes monogalactosyl diacylglycerol (MGDG) and digalactosyl diacylglycerol (DGDG) substrates presented in various forms to the enzyme. The enzyme has galactolipase activity on galactolipid micelles, monomolecular films, and UV-absorbing surface-coated substrate, overview. TTL possesses broad substrate specificity and is active on triglycerides with various acyl chain lengths, phospholipids, and galactolipids
-
-
?
additional information
?
-
-
Talaromyces thermophilus lipase (TTL, EC 3.1.1.3) also hydrolyzes monogalactosyl diacylglycerol (MGDG) and digalactosyl diacylglycerol (DGDG) substrates presented in various forms to the enzyme. The enzyme has galactolipase activity on galactolipid micelles, monomolecular films, and UV-absorbing surface-coated substrate, overview. TTL possesses broad substrate specificity and is active on triglycerides with various acyl chain lengths, phospholipids, and galactolipids
-
-
?
additional information
?
-
-
galactolipid-bile salt mixed micelles are the best substrate form for the microbial enzyme
-
-
?
additional information
?
-
displays preferentially galactolipid acyl hydrolase activity, phospholipids are very slowly hydrolysed and triacylglycerols are not deacylated
-
?
additional information
?
-
-
displays preferentially galactolipid acyl hydrolase activity, phospholipids are very slowly hydrolysed and triacylglycerols are not deacylated
-
?
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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
1,2-diacyl-3-beta-D-galactosyl-sn-glycerol + H2O
?
-
-
-
?
1,2-diacyl-3-O-alpha-D-galactosyl-(1->6)-beta-D-galactosyl-sn-glycerol + H2O
?
-
-
-
?
1,2-diacyl-3-O-alpha-D-galactosyl-(1->6)-beta-D-galactosyl-sn-glycerol + H2O
?
-
-
-
?
monogalactosyldiacylglycerol + H2O
?
-
extent of polar lipids breakdown in chill-sensitive and chill-tolerant inbreeds during chilling and post-chilling rewarming is correlated with galactolipase activity in chloroplast
-
-
?
additional information
?
-
-
the enzyme hydrolyzes the membrane lipids to release various saturated and unsaturated fatty acids, including arachidonic acid as substrate for prostaglandin synthesis
-
-
?
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
-
-
?
additional information
?
-
galactolipase (ckGL) hydrolyzes the acyl ester bond of galactolipids such as digalactosyldiacylglycerol (DGDG)
-
-
?
additional information
?
-
-
galactolipase (ckGL) hydrolyzes the acyl ester bond of galactolipids such as digalactosyldiacylglycerol (DGDG)
-
-
?
additional information
?
-
galactolipase (ckGL) hydrolyzes the acyl ester bond of galactolipids such as digalactosyldiacylglycerol (DGDG)
-
-
?
additional information
?
-
-
the enzyme utilizes galactolipids, phospholipids, sulpholipids and phosphatidylglycerol as substrates, releasing fatty acids esterified to the hydroxyl groups at carbon 1 and 2 of glycerol
-
-
?
additional information
?
-
-
the enzyme utilizes galactolipids, phospholipids, sulpholipids and phosphatidylglycerol as substrates, releasing fatty acids esterified to the hydroxyl groups at carbon 1 and 2 of glycerol
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
CaCl2
Mn2+
Sodium dithionite
-
highest activity between 4-7 mM, above decrease of activation
additional information
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,4,6-trifluoro-1,3,5-triazine
-
16% inhibition at 7 mM, 93% inhibition at 74 mM, 98% inhibition at 741 mM
Digitonin
-
complete inhibition, concentration below critical micellar concentration
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
N-Acetylimidazole
-
30% inhibition at 30fold mol per mol of enzyme, 48% inhibition at 465fold mol per mol of enzyme, complete inhibition at 180000fold mol per mol of enzyme
Trypsin
-
1000 units, pH 7.6, phosphate buffer at 24°C, completely inactivated
-
Zwittergent 3-19
-
complete inhibition, concentration below critical micellar concentration
CaCl2
-
no inhibition at 0.1 mM, 13% inhibition at 1 mM, 47% inhibition at 10 mM
SDS
-
complete inhibition, concentration below critical micellar concentration
Triton X-100
-
complete inhibition, concentration below critical micellar concentration
additional information
-
not affected by 0.3 mM p-chloromercuribenzoate, and 30 mM N-ethylmaleimide
-
additional information
-
not affected by dimethyl(2-hydroxy-5-nitrobenzyl)-sulfonium bromide, N-bromosuccinimide, p-chloromercuribenzoate
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Triton X-100
strongly activating, best at 0.3% w/v. Absence of this detergent causes the inactivation of ckGL even in the enzyme assay, as it does during the purification
EDTA
-
212% activity compared to assay without additives at 0.1 mM, 198% at 1 mM, 161% at 10 mM
additional information
-
DGL expression is rapidly induced by wounding and activated by phospholipase D
-
additional information
-
gene expression is induced by drought stress, wounding, and methyl jasmonate treatments
-
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
-
additional information
-
increased galactolipase activity is an important factor contributing to chilling susceptibility
-
additional information
-
increased galactolipase activity is an important factor contributing to chilling susceptibility
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.54
1,2-diacyl-3-O-alpha-D-galactosyl-(1->6)-beta-D-galactosyl-sn-glycerol
pH 6.5, 37°C, native enzyme
1.05
1,2-diacyl-3-O-alpha-D-galactosyl-(1->6)-beta-D-galactosyl-sn-glycerol
pH 6.5, 37°C, recombinant enzyme
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
498
1,2-diacyl-3-O-alpha-D-galactosyl-(1->6)-beta-D-galactosyl-sn-glycerol
pH 6.5, 37°C, recombinant enzyme
1390
1,2-diacyl-3-O-alpha-D-galactosyl-(1->6)-beta-D-galactosyl-sn-glycerol
pH 6.5, 37°C, native enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
474.3
1,2-diacyl-3-O-alpha-D-galactosyl-(1->6)-beta-D-galactosyl-sn-glycerol
pH 6.5, 37°C, recombinant enzyme
2574.1
1,2-diacyl-3-O-alpha-D-galactosyl-(1->6)-beta-D-galactosyl-sn-glycerol
pH 6.5, 37°C, native enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.07
0.13
0.67
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
3351
-
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
3785
substrate 1,2-octanoyl-3-O-alpha-D-galactosyl-(1->6)-beta-D-galactosyl-sn-glycerol, pH 8.0, 37°C
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
40500
substrate 1,2-di-O-alpha-eleostearoyl-3-O-beta-D-galactopyranosyl-sn-glycerol, pH 8.0, 37°C, purified native enzyme
4167
-
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
4250
substrate phosphatidylcholine, pH 8.0, 37°C, purified native enzyme
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
4375
-
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
4658
substrate 1,2-octanoyl-3-O-alpha-D-galactosyl-sn-glycerol, pH 8.0, 37°C
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
5420
-
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
9800
substrate 3-O-(6-O-alpha-D-galactopyranosyl-beta-D-galactopyranosyl)-1,2-di-O-octanoyl-sn-glycerol, pH 8.0, 37°C, purified native enzyme
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10.5
5.5
-
monogalactosyldiacylglycerol as substrate, at 35°C, shift to pH 6.0 in the presence of Triton X-100
5.5 - 6
6
-
monogalactosyldiacylglycerol as substrate, at 35°C, shift from pH 5.5 in the presence of Triton X-100
7.2
-
with both monogalactosyldiacylglycerol and digalactosyldiacylglycerol as substrates, Tris-maleate buffer in the presence of 1.5 mM
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 8
-
pH 5: about 10% of the maximal activity, pH 8: about 50% of the maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
35
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 20
10 - 50
-
the enzymatic activity increases gradually from 10 to 30°C, drastically increases at 37°C and then continuously decreases over 37°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Pisum arvense
L. convar. botyris cv. Elgon and cv. Wiedenska Biala, no activity in convar. capitata cv. Ditmarska Najwczesniejsza
-
-
brenda
chilling-sensitive lines Cm7 and Co151, and chilling-tolerant lines S215 and EP1
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
galactolipase activity is generally higher in the chloroplast fraction of chilling-sensitive species than in chilling-tolerant and chilling-insensitive genotypes
brenda
-
galactolipase activity is generally higher in the chloroplast fraction of chilling-sensitive species than in chilling-tolerant and chilling-insensitive genotypes
brenda
-
often shows slightly higher activity after freezing
brenda
-
in aged chloroplasts of chilling-sensitive lines, enzyme activity was higher than in aged chloroplasts of chilling-tolerant lines
brenda
-
galactolipase activity is generally higher in the chloroplast fraction of chilling-sensitive species than in chilling-tolerant and chilling-insensitive genotypes
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
additional information
evolution
differences between galactolipases and lipases with regard to function, substrate recognition mechanism, and biochemical roles, overview. Phylogenetic analysis based on amino acid sequences also show that ckGL is clearly separated from groups containing phospholipase A1, PLA1
evolution
-
differences between galactolipases and lipases with regard to function, substrate recognition mechanism, and biochemical roles, overview. Phylogenetic analysis based on amino acid sequences also show that ckGL is clearly separated from groups containing phospholipase A1, PLA1
-
physiological function
-
pancreatic lipase-related protein 2 is the main enzyme involved in the digestion of these common vegetable lipids in the gastrointestinal tract
physiological function
-
pancreatic lipase-related protein 2 is the main enzyme involved in the digestion of these common vegetable lipids in the gastrointestinal tract
physiological function
galactolipase (ckGL) hydrolyzes the acyl ester bond of galactolipids such as digalactosyldiacylglycerol (DGDG)
physiological function
-
galactolipase (ckGL) hydrolyzes the acyl ester bond of galactolipids such as digalactosyldiacylglycerol (DGDG)
-
additional information
structure-activity relationships of FSL, three-simensional modeling of the enzyme, in silico docking of medium chains substrates MGDG and DGDG and phospholipid in the active site of enzyme FSL, homology modeling of FSL, detailed overview
additional information
three-dimensional structure molecular modelling and dynamic light scattering measurements, sequence comparisons, overview
additional information
-
three-dimensional structure molecular modelling and dynamic light scattering measurements, sequence comparisons, overview
additional information
-
structure-activity relationships of FSL, three-simensional modeling of the enzyme, in silico docking of medium chains substrates MGDG and DGDG and phospholipid in the active site of enzyme FSL, homology modeling of FSL, detailed overview
-
additional information
-
structure-activity relationships of FSL, three-simensional modeling of the enzyme, in silico docking of medium chains substrates MGDG and DGDG and phospholipid in the active site of enzyme FSL, homology modeling of FSL, detailed overview
-
additional information
Thermomyces dupontii Stolk
-
three-dimensional structure molecular modelling and dynamic light scattering measurements, sequence comparisons, overview
-
additional information
-
structure-activity relationships of FSL, three-simensional modeling of the enzyme, in silico docking of medium chains substrates MGDG and DGDG and phospholipid in the active site of enzyme FSL, homology modeling of FSL, detailed overview
-
additional information
-
structure-activity relationships of FSL, three-simensional modeling of the enzyme, in silico docking of medium chains substrates MGDG and DGDG and phospholipid in the active site of enzyme FSL, homology modeling of FSL, detailed overview
-
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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_BOVIN
469
0
52193
Swiss-Prot
Secretory Pathway (Reliability: 2)
LIPR2_CAVPO
434
0
47678
Swiss-Prot
other Location (Reliability: 1)
LIPR2_HUMAN
469
0
51961
Swiss-Prot
Secretory Pathway (Reliability: 2)
PLIP1_ARATH
649
0
71735
Swiss-Prot
Chloroplast (Reliability: 2)
PLIP2_ARATH
713
1
78346
Swiss-Prot
other Location (Reliability: 5)
PLIP3_ARATH
649
1
73044
Swiss-Prot
other Location (Reliability: 5)
LIPR2_MOUSE
482
1
54017
Swiss-Prot
Secretory Pathway (Reliability: 1)
LIPR2_MYOCO
470
0
52060
Swiss-Prot
Secretory Pathway (Reliability: 1)
LIPR2_PIG
471
0
53199
Swiss-Prot
Secretory Pathway (Reliability: 2)
LIPR2_RAT
468
0
52535
Swiss-Prot
Secretory Pathway (Reliability: 2)
PLA12_ARATH
471
0
52800
Swiss-Prot
Chloroplast (Reliability: 3)
A0A7C8Z702_OPUST
123
0
13985
TrEMBL
other Location (Reliability: 2)
A0A7C9B055_OPUST
153
2
17439
TrEMBL
other Location (Reliability: 3)
A0A2P6REB9_ROSCH
288
0
32449
TrEMBL
other Location (Reliability: 3)
A0A2G9H1S2_9LAMI
182
0
20416
TrEMBL
other Location (Reliability: 2)
A0A2P6R8L8_ROSCH
627
0
70581
TrEMBL
other Location (Reliability: 3)
A0A7C8Z774_OPUST
192
0
22015
TrEMBL
other Location (Reliability: 4)
A0A396JY70_MEDTR
699
1
78151
TrEMBL
Chloroplast (Reliability: 5)
A0A2P6PID0_ROSCH
728
1
80556
TrEMBL
other Location (Reliability: 4)
G7L433_MEDTR
695
0
78483
TrEMBL
Chloroplast (Reliability: 4)
A0A2Z5TTR4_PARKE
535
0
59126
TrEMBL
Mitochondrion (Reliability: 4)
A0A7C9EK65_OPUST
243
0
26052
TrEMBL
Chloroplast (Reliability: 4)
A0A2P6Q0I2_ROSCH
76
0
8254
TrEMBL
other Location (Reliability: 3)
A0A7C9EPK6_OPUST
117
0
13631
TrEMBL
other Location (Reliability: 5)
A0A2P6SIB8_ROSCH
666
0
74852
TrEMBL
Chloroplast (Reliability: 3)
A0A396H6Y0_MEDTR
685
0
76056
TrEMBL
Chloroplast (Reliability: 2)
A0A7C8Z9Y2_OPUST
148
0
16507
TrEMBL
other Location (Reliability: 3)
C7YUZ1_FUSV7
Fusarium vanettenii (strain ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL 45880 / 77-13-4)
348
0
37433
TrEMBL
-
LIPR1_CANLF
467
0
51482
Swiss-Prot
other Location (Reliability: 3)
Q95KP4_HORSE
452
0
50063
TrEMBL
Secretory Pathway (Reliability: 4)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
110000
146000 - 242000
native enzyme, gel filtration and native PAGE
40000
50000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
proteolytic modification
Thr61 is the predominant N-terminal amino acid of mature ckGL, Ala60 might be removed by an aminopeptidase after the transport of ckGL into the chloroplast
proteolytic modification
-
Thr61 is the predominant N-terminal amino acid of mature ckGL, Ala60 might be removed by an aminopeptidase after the transport of ckGL into the chloroplast
-
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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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
N336Q
the mutant enzyme is not glycosylated and shows identical kinetic properties to the wild type enzyme
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 7
purified native enzyme, 4°C, 30 min, completely stable at
749696
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
4 - 40
purified native enzyme, pH 6.5, 30 min, completely stable at
50
-
incubation for 10 min at pH 7.5, 95% loss of activity, retains more thant 60% of its activity at pH 5.5
60
65
-
inactivated, pH 4 after 20 min, 80% of the activity retained by the same heating at pH 7.5
60
-
70-75% of the activity left after 10 min, monogalacatosyldiacylglycerol as substrate, 16% of the activity left after 10 min with digalactosyldiacylglycerol as substrate
60
-
completely inactivated after 10 min at pH 8.0, 70% of its activity retained at pH 5.5
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acetone
Ethanol
ether
additional information
-
no effect with ethyl ether, methanol, and chloroform
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, (NH4)2SO4-precipitation at pH-optimum, after 4 weeks 53.6% of the original activity left
-
reduced activity after 3-4 h storage on ice, though improved stability in the presence of bovine serum albumin
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, DEAE-Toyopearl 650 M colum chromatography, and HW-55F gel filtration
-
native enzyme 163fold from Chlorella kessleri strain 11h to homogeneity, it is not possible to purify active enzyme in the absence of Triton X-100 or by using other detergents because the enzyme becomes inactive during the procedure. Recombinant His-tagged enzyme 15.5fold from Escherichia coli strain JM109 by 2 steps of nickel affinity chromatography
Superdex 75 gel filtration and Macro-Prep DEAE column chromatography
Superdex 75 gel filtration and Macro-Prep DEAE column chromatography
Superdex 75 gel filtration and Macro-Prep DEAE column chromatography
Superdex 75 gel filtration and Macro-Prep DEAE column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Pichia pastoris
expressed in SF9 insect cells (wild type enzyme) and in Pichia pastoris (mutant enzyme N336Q)
gene chGL or glp1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain JM109
recombinant expression of enzyme FSl in Escherichia coli strain XL1-Blue
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
feeding Epiphyas postvittana on a fatty acid-free artificial diet induces a large increase in galactolipase activity
-
switching Tineola bisselliella larvae to wool leads has no effect on the level of galactolipase activity
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
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
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
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
O'Sullivan, J.N.; Warwick, N.W.M.; Dalling, M.J.
A galactolipase activity associated with the thylakoids of wheat leaves (Triticum aestivum L.)
J. Plant Physiol.
131
393-404
1987
Triticum aestivum
-
brenda
Gemel, J.; Kaniuga, Z.
Comparison of galactolipase activity and free fatty acid levels in chloroplasts of chill-sensitive and chill-resistant plants
Eur. J. Biochem.
166
229-233
1987
Beta vulgaris, Brassica napus, Brassica oleracea, Vicia faba, Capsicum annuum, Cucumis sativus, Dahlia pinnata, Lupinus angustifolius, Solanum lycopersicum, Solanum habrochaites, Solanum peruvianum, Medicago sativa subsp. x varia, Nicotiana tabacum, no activity in Brassica rapa, no activity in Cucumis melo, no activity in Cucurbita maxima, no activity in Cucurbita pepo, no activity in Glycine max, no activity in Hordeum vulgare, no activity in Passiflora edulis, no activity in Passiflora quadrangularis, Phaseolus coccineus, Phaseolus vulgaris, Pisum arvense, Pisum sativum, Spinacia oleracea, Zea mays, no activity in Passiflora edulis Sims, Pisum arvense L., no activity in Passiflora quadrangularis L.
brenda
Kaniuga, Z.; Gemel, J.
Galactolipase activity and free fatty acid levels in chloroplasts
FEBS Lett.
171
55-58
1984
Brassica oleracea, Vicia faba, Solanum lycopersicum, no activity in Lactuca sativa, Phaseolus vulgaris, Pisum arvense, Pisum sativum, Spinacia oleracea, Zea mays
-
brenda
Matsuda, H; Hirayama, O.
Purification of a galactolipase from rice bran affinity chromatography on palmitoyled gauze
Agric. Biol. Chem.
43
463-469
1979
Oryza sativa
-
brenda
Matsuda, H.; Tanaka, G.; Morita, K.; Hirayama, O.
Purification of a lipolytic acyl-hydrolase from Phaseolus vulgaris leaves by affinity chromatography on palmitolyated gauze and its properties
Agric. Biol. Chem.
43
563-570
1979
Phaseolus vulgaris
-
brenda
Matsuda, H.; Hirayama, O.
Enzymatic properties of a galactolipase from rice bran
Agric. Biol. Chem.
43
697-703
1979
Oryza sativa
-
brenda
Matsuda, H.; Hirayama, O.
Purification and properties of a lipolytic acyl-hydrolase from potato leaves
Biochim. Biophys. Acta
573
155-165
1979
Solanum tuberosum
brenda
Hirayama, O.; Matsuda, H.; Takeda, H.; Maenaka, K.; Takatsuka, H.
Purification and properties of a lipid acyl-hydrolase from potato tubers
Biochim. Biophys. Acta
384
127-137
1975
Solanum tuberosum
brenda
Sastry, P.S.; Kates, M.
Monogalactosyl and digalactosyl diglyceride acyl hydrolase
Methods Enzymol.
14
204-208
1969
Phaseolus coccineus
-
brenda
Bajwa, S.S.; Sastry, P.S.
Degradation of monogalactosyl diglyceride and digalactosyl diglyceride by sheep pancreatic enzymes
Biochem. J.
144
177-187
1974
Cavia porcellus, Ovis aries, Rattus norvegicus
brenda
Helmsing, P.J.
Purification and properties of galactolipase
Biochim. Biophys. Acta
178
519-533
1969
Phaseolus coccineus
brenda
Helmsing, P.J.
Hydrolysis of galactolipids by enzymes in spinach leaves
Biochim. Biophys. Acta
144
470-472
1967
Spinacia oleracea
brenda
Sahsah, Y.; Thi, A.T.P.; Roy-Macauley, H.; D'Arcy-Lameta, A.; Repellin, A.; Zuily-Fodil, Y.
Purification and characterization of a soluble lipolytic acylhydrolase from cowpea (Vigna unguiculata L.) leaves
Biochim. Biophys. Acta
1215
66-73
1994
Vigna unguiculata
brenda
Kaniuga, Z.; Saczynska, V.; Miskiewicz, E.; Garstka, M.
Degradation of leaf polar lipids during chilling and post-chilling rewarming of Zea mays genotypes reflects differences in their response to chilling stress. The role of galactolipase
Acta Physiol. Plant.
21
45-56
1999
Zea mays
-
brenda
Kaniuga, Z.; Saczynska, V.; Miskiewicz, E.
Galactolipase activity but not the level of high-melting-point phosphatidylglycerol is related to chilling tolerance in differentially sensitive Zea mays inbred lines
Plant Cell Rep.
17
897-901
1998
Zea mays
brenda
Matos, A.R.; D'Arcy-Lameta, A.; Franca, M.; Zuily-Fodil, Y.; Pham-Thi, A.T.
A patatin-like protein with galactolipase activity is induced by drought stress in Vigna unguiculata leaves
Biochem. Soc. Trans.
28
779-781
2000
Vigna unguiculata (Q9AQT8), Vigna unguiculata
brenda
Terasaki, M.; Itabashi, Y.
Glycerolipid acyl hydrolase activity in the brown alga Cladosiphon okamuranus Tokida
Biosci. Biotechnol. Biochem.
67
1986-1989
2003
Cladosiphon okamuranus
brenda
Matos, A.R.; d'Arcy-Lameta, A.; Franca, M.; Petres, S.; Edelman, L.; Kader, J.C.; Zuily-Fodil, Y.; Pham-Thi, A.T.
A novel patatin-like gene stimulated by drought stress encodes a galactolipid acyl hydrolase
FEBS Lett.
491
188-192
2001
Vigna unguiculata (Q9AQT8), Vigna unguiculata
brenda
Kim, M.J.; Oh, J.M.; Cheon, S.H.; Cheong, T.K.; Lee, S.H.; Choi, E.O.; Lee, H.G.; Park, C.S.; Park, K.H.
Thermal inactivation kinetics and application of phospho- and galactolipid-degrading enzymes for evaluation of quality changes in frozen vegetables
J. Agric. Food Chem.
49
2241-2248
2001
Daucus carota, Spinacia oleracea
brenda
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
brenda
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
brenda
Lafont, D.; Carriere, F.; Ferrato, F.; Boullanger, P.
Syntheses of an a-D-Gal-(1->6)-b-D-Gal diglyceride,as lipase substrate
Carbohydr. Res.
341
695-704
2006
Cavia porcellus
brenda
Lion, U.; Wiesemeier, T.; Weinberger, F.; Beltran, J.; Flores, V.; Faugeron, S.; Correa, J.; Pohnert, G.
Phospholipases and Galactolipases Trigger Oxylipin-Mediated Wound-Activated Defence in the Red Alga Gracilaria chilensis against Epiphytes
Chembiochem
7
457-462
2006
Agarophyton chilense
brenda
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)
brenda
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
brenda
Hyun, Y.; Choi, S.; Hwang, H.J.; Yu, J.; Nam, S.J.; Ko, J.; Park, J.Y.; Seo, Y.S.; Kim, E.Y.; Ryu, S.B.; Kim, W.T.; Lee, Y.H.; Kang, H.; Lee, I.
Cooperation and functional diversification of two closely related galactolipase genes for jasmonate biosynthesis
Dev. Cell
14
183-192
2008
Arabidopsis thaliana
brenda
Illijas, M.I.; Terasaki, M.; Nakamura, R.; Iijima, N.; Hara, A.; Fusetani, N.; Itabashi, Y.
Purification and characterization of glycerolipid acyl-hydrolase from the red alga Gracilaria vermiculophylla
Fish. Sci.
74
670-676
2008
Agarophyton vermiculophyllum
brenda
Matos, A.R.; Gigon, A.; Laffray, D.; Petres, S.; Zuily-Fodil, Y.; Pham-Thi, A.T.
Effects of progressive drought stress on the expression of patatin-like lipid acyl hydrolase genes in Arabidopsis leaves
Physiol. Plant.
134
110-120
2008
Arabidopsis thaliana
brenda
Kaniuga, Z.
Chilling response of plants: importance of galactolipase, free fatty acids and free radicals
Plant Biol.
10
171-184
2008
Solanum lycopersicum, Solanum tuberosum, Zea mays, no activity in Solanum x ajanhuiri
brenda
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
brenda
Christeller, J.T.; Amara, S.; Carriere, F.
Galactolipase, phospholipase and triacylglycerol lipase activities in the midgut of six species of lepidopteran larvae feeding on different lipid diets
J. Insect Physiol.
57
1232-1239
2011
Ephestia kuehniella, Epiphyas postvittana, Galleria mellonella, Helicoverpa armigera, Plodia interpunctella, Tineola bisselliella
brenda
Amara, S.; Delorme, V.; Record, M.; Carriere, F.
Inhibition of phospholipase A1, lipase and galactolipase activities of pancreatic lipase-related protein 2 by methyl arachidonyl fluorophosphonate (MAFP)
Biochim. Biophys. Acta
1821
1379-1385
2012
Homo sapiens (P54317), Homo sapiens
brenda
Amara, S.; Lafont, D.; Parsiegla, G.; Point, V.; Chabannes, A.; Rousset, A.; Carrire, F.
The galactolipase activity of some microbial lipases and pancreatic enzymes
Eur. J. Lipid Sci. Technol.
115
442-451
2013
Cavia porcellus, Thermomyces lanuginosus
-
brenda
Hashiro, S.; Fujiuchi, K.; Sugimori, D.; Yasueda, H.
A novel galactolipase from a green microalga Chlorella kessleri purification, characterization, molecular cloning, and heterologous expression
Appl. Microbiol. Biotechnol.
102
1711-1723
2018
Parachlorella kessleri (A0A2Z5TTR4), Parachlorella kessleri, Parachlorella kessleri 11h (A0A2Z5TTR4)
brenda
Jallouli, R.; Othman, H.; Amara, S.; Parsiegla, G.; Carriere, F.; Srairi-Abid, N.; Gargouri, Y.; Bezzine, S.
The galactolipase activity of Fusarium solani (phospho)lipase
Biochim. Biophys. Acta
1851
282-289
2015
Fusarium vanettenii (C7YUZ1), Fusarium vanettenii MPVI (C7YUZ1), Fusarium vanettenii 77-13-4 (C7YUZ1), Fusarium vanettenii ATCC MYA-4622 (C7YUZ1), Fusarium vanettenii FGSC 9596 (C7YUZ1)
-
brenda
Belhaj, I.; Amara, S.; Parsiegla, G.; Sutto-Ortiz, P.; Sahaka, M.; Belghith, H.; Rousset, A.; Lafont, D.; Carriere, F.
Galactolipase activity of Talaromyces thermophilus lipase on galactolipid micelles, monomolecular films and UV-absorbing surface-coated substrate
Biochim. Biophys. Acta
1863
1006-1015
2018
Thermomyces dupontii (F6LQK7), Thermomyces dupontii, Thermomyces dupontii Stolk (F6LQK7)
brenda
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Release 2023.1 (January 2023)
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