BRENDA - Enzyme Database
show all sequences of 2.3.1.158

Phospholipid:diacylglycerol acyltransferase is a multifunctional enzyme involved in membrane lipid turnover and degradation while synthesizing triacylglycerol in the unicellular green microalga Chlamydomonas reinhardtii

Yoon, K.; Han, D.; Li, Y.; Sommerfeld, M.; Hu, Q.; Plant Cell 24, 3708-3724 (2012)

Data extracted from this reference:

Application
Application
Commentary
Organism
energy production
the strong lipase activity of PDAT with broad substrate specificity might be a potential biocatalyst for industrial lipid hydrolysis and conversion, particularly for biofuel production
Chlamydomonas reinhardtii
industry
the strong lipase activity of PDAT with broad substrate specificity might be a potential biocatalyst for industrial lipid hydrolysis and conversion, particularly for biofuel production
Chlamydomonas reinhardtii
Cloned(Commentary)
Commentary
Organism
gene encoding PDAT, DNA and amino acid sequence determination and analysis, phylogenetic tree, expression of full-length enzyme and of truncated PDAT lacking the transmembrane domain in Pichia pastoris
Chlamydomonas reinhardtii
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
-
Chlamydomonas reinhardtii
16020
-
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
95000
-
x * 104600, sequence calculation, x * 120000, recombinant full-length PDAT, SDS-PAGE, x * 95000, recombinant truncated PDAT lacking the transmembrane domain, SDS-PAGE
Chlamydomonas reinhardtii
104600
-
x * 104600, sequence calculation, x * 120000, recombinant full-length PDAT, SDS-PAGE, x * 95000, recombinant truncated PDAT lacking the transmembrane domain, SDS-PAGE
Chlamydomonas reinhardtii
120000
-
x * 104600, sequence calculation, x * 120000, recombinant full-length PDAT, SDS-PAGE, x * 95000, recombinant truncated PDAT lacking the transmembrane domain, SDS-PAGE
Chlamydomonas reinhardtii
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
phospholipid + 1,2-diacyl-sn-glycerol
Chlamydomonas reinhardtii
PDAT uses membrane lipids (e.g., phospholipids and glycolipids) as the substrates for the acyl transfer reaction or hydrolysis in vivo
lysophospholipid + triacylglycerol
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Chlamydomonas reinhardtii
-
-
-
Purification (Commentary)
Commentary
Organism
recombinant full-length enzyme and truncated PDAT lacking the transmembrane domain from Pichia pastoris by affinity chromatography
Chlamydomonas reinhardtii
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
PDAT shows broad substrate specificity, overview
720694
Chlamydomonas reinhardtii
?
-
-
-
-
phospholipid + 1,2-diacyl-sn-glycerol
PDAT uses membrane lipids (e.g., phospholipids and glycolipids) as the substrates for the acyl transfer reaction or hydrolysis in vivo
720694
Chlamydomonas reinhardtii
lysophospholipid + triacylglycerol
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 104600, sequence calculation, x * 120000, recombinant full-length PDAT, SDS-PAGE, x * 95000, recombinant truncated PDAT lacking the transmembrane domain, SDS-PAGE
Chlamydomonas reinhardtii
pI Value
Organism
Commentary
pI Value Maximum
pI Value
Chlamydomonas reinhardtii
sequence calculation
-
5.96
Application (protein specific)
Application
Commentary
Organism
energy production
the strong lipase activity of PDAT with broad substrate specificity might be a potential biocatalyst for industrial lipid hydrolysis and conversion, particularly for biofuel production
Chlamydomonas reinhardtii
industry
the strong lipase activity of PDAT with broad substrate specificity might be a potential biocatalyst for industrial lipid hydrolysis and conversion, particularly for biofuel production
Chlamydomonas reinhardtii
Cloned(Commentary) (protein specific)
Commentary
Organism
gene encoding PDAT, DNA and amino acid sequence determination and analysis, phylogenetic tree, expression of full-length enzyme and of truncated PDAT lacking the transmembrane domain in Pichia pastoris
Chlamydomonas reinhardtii
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
-
Chlamydomonas reinhardtii
16020
-
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
95000
-
x * 104600, sequence calculation, x * 120000, recombinant full-length PDAT, SDS-PAGE, x * 95000, recombinant truncated PDAT lacking the transmembrane domain, SDS-PAGE
Chlamydomonas reinhardtii
104600
-
x * 104600, sequence calculation, x * 120000, recombinant full-length PDAT, SDS-PAGE, x * 95000, recombinant truncated PDAT lacking the transmembrane domain, SDS-PAGE
Chlamydomonas reinhardtii
120000
-
x * 104600, sequence calculation, x * 120000, recombinant full-length PDAT, SDS-PAGE, x * 95000, recombinant truncated PDAT lacking the transmembrane domain, SDS-PAGE
Chlamydomonas reinhardtii
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
phospholipid + 1,2-diacyl-sn-glycerol
Chlamydomonas reinhardtii
PDAT uses membrane lipids (e.g., phospholipids and glycolipids) as the substrates for the acyl transfer reaction or hydrolysis in vivo
lysophospholipid + triacylglycerol
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant full-length enzyme and truncated PDAT lacking the transmembrane domain from Pichia pastoris by affinity chromatography
Chlamydomonas reinhardtii
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
PDAT shows broad substrate specificity, overview
720694
Chlamydomonas reinhardtii
?
-
-
-
-
phospholipid + 1,2-diacyl-sn-glycerol
PDAT uses membrane lipids (e.g., phospholipids and glycolipids) as the substrates for the acyl transfer reaction or hydrolysis in vivo
720694
Chlamydomonas reinhardtii
lysophospholipid + triacylglycerol
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 104600, sequence calculation, x * 120000, recombinant full-length PDAT, SDS-PAGE, x * 95000, recombinant truncated PDAT lacking the transmembrane domain, SDS-PAGE
Chlamydomonas reinhardtii
pI Value (protein specific)
Organism
Commentary
pI Value Maximum
pI Value
Chlamydomonas reinhardtii
sequence calculation
-
5.96
Expression
Organism
Commentary
Expression
Chlamydomonas reinhardtii
Cr-PDAT is transiently upregulated in response to N deprivation. The protein expression achieves the maximum level at 3 h after the onset of N depletion from the culture medium and then gradually decreases during the following 48 h
up
General Information
General Information
Commentary
Organism
evolution
PDAT belongs to the LCAT-like family
Chlamydomonas reinhardtii
malfunction
artificial microRNA silencing of PDAT alters the membrane lipid composition, reducing the maximum specific growth rate
Chlamydomonas reinhardtii
physiological function
phospholipid:diacylglycerol acyltransferase in the green microalga Chlamydomonas reinhardtii catalyzes triacylglycerol synthesis via two pathways: transacylation of diacylglycerol with acyl groups from phospholipids and galactolipids and diacylglycerol:diacylglycerol transacylation. PDAT-mediated membrane lipid turnover and triacylglycerol synthesis is essential for vigorous growth under favorable culture conditions and for membrane lipid degradation with concomitant production of triacylglycerol for survival under stress. PDAT also possesses acyl hydrolase activities using triacylglycerols, phospholipids, galactolipids, and cholesteryl esters as substrates
Chlamydomonas reinhardtii
General Information (protein specific)
General Information
Commentary
Organism
evolution
PDAT belongs to the LCAT-like family
Chlamydomonas reinhardtii
malfunction
artificial microRNA silencing of PDAT alters the membrane lipid composition, reducing the maximum specific growth rate
Chlamydomonas reinhardtii
physiological function
phospholipid:diacylglycerol acyltransferase in the green microalga Chlamydomonas reinhardtii catalyzes triacylglycerol synthesis via two pathways: transacylation of diacylglycerol with acyl groups from phospholipids and galactolipids and diacylglycerol:diacylglycerol transacylation. PDAT-mediated membrane lipid turnover and triacylglycerol synthesis is essential for vigorous growth under favorable culture conditions and for membrane lipid degradation with concomitant production of triacylglycerol for survival under stress. PDAT also possesses acyl hydrolase activities using triacylglycerols, phospholipids, galactolipids, and cholesteryl esters as substrates
Chlamydomonas reinhardtii
Expression (protein specific)
Organism
Commentary
Expression
Chlamydomonas reinhardtii
Cr-PDAT is transiently upregulated in response to N deprivation. The protein expression achieves the maximum level at 3 h after the onset of N depletion from the culture medium and then gradually decreases during the following 48 h
up
Other publictions for EC 2.3.1.158
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
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)
736102
Hung
Functional study of diacylglyc ...
Chlamydomonas reinhardtii
FEBS Lett.
587
2364-2370
2013
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1
3
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736422
Pan
Identification of a pair of ph ...
Linum usitatissimum
J. Biol. Chem.
288
24173-24188
2013
1
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1
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2
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2
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1
2
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736985
Fan
Dual role for phospholipid:dia ...
Arabidopsis thaliana
Plant Cell
25
3506-3518
2013
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1
1
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720694
Yoon
Phospholipid:diacylglycerol ac ...
Chlamydomonas reinhardtii
Plant Cell
24
3708-3724
2012
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2
1
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2
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3
1
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2
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1
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2
1
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1
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2
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1
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1
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2
1
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1
1
3
3
1
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-
721119
Zhang
Three diacylglycerol acyltrans ...
Yarrowia lipolytica, Yarrowia lipolytica ATCC 20362
Yeast
29
25-38
2012
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1
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1
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5
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1
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1
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720737
van Erp
Castor phospholipid:diacylglyc ...
Ricinus communis
Plant Physiol.
155
683-693
2011
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1
1
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1
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1
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3
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2
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1
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1
1
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1
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1
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2
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1
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697014
Dauk
-
The role of diacylglycerol acy ...
Arabidopsis thaliana
Botany
87
552-560
2009
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1
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1
1
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684576
Arabolaza
Multiple pathways for triacylg ...
Streptomyces coelicolor
Appl. Environ. Microbiol.
74
2573-2582
2008
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4
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687725
Czabany
Structural and biochemical pro ...
Saccharomyces cerevisiae
J. Biol. Chem.
283
17065-17074
2008
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1
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1
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688089
Hernandez
The utilization and desaturati ...
Olea europaea
J. Exp. Bot.
59
2425-2435
2008
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685341
Ghosal
Saccharomyces cerevisiae phosp ...
Saccharomyces cerevisiae
Biochim. Biophys. Acta
1771
1457-1463
2007
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1
1
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1
1
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5
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7
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676641
Mhaske
Isolation and characterization ...
Arabidopsis thaliana
Plant Physiol. Biochem.
43
413-417
2005
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660241
Stahl
Cloning and functional charact ...
Arabidopsis thaliana
Plant Physiol.
135
1324-1335
2004
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6
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2
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393081
Banas
The involvement of phospholipi ...
Arabidopsis thaliana, Crepis palaestina, Euphorbia lagascae, Ricinus communis
Biochem. Soc. Trans.
28
703-705
2000
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9
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18
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18
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393082
Dahlqvist
Phospholipid:diacylglycerol ac ...
Crepis palaestina, Helianthus annuus, Ricinus communis, Saccharomyces cerevisiae
Proc. Natl. Acad. Sci. USA
97
6487-6492
2000
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1
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4
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10
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3
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24
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1
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4
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3
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24
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