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Information on EC 2.3.1.20 - diacylglycerol O-acyltransferase and Organism(s) Saccharomyces cerevisiae and UniProt Accession Q08650
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2.3.1.20 diacylglycerol O-acyltransferaseIUBMB Comments
Palmitoyl-CoA and other long-chain acyl-CoAs can act as donors.
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Word Map
- 2.3.1.20
- triacylglycerols
- triglyceride
- adipose
- milk
- acyl-coas
- lipoprotein
- obesity
- cholesterol
- droplet
- cattle
- adipocytes
- lipase
- steatosis
-
lipogenesis
-
lipogenic
-
high-fat
-
holstein
-
oleic
-
dairy
-
proliferator-activated
- phosphatidate
- glycerolipids
-
lipolysis
-
oleaginous
- glycerol-3-phosphate
- chylomicron
-
biodiesel
-
srebf1
-
oilseed
-
lipotoxicity
- stearoyl-coa
- acaca
- camelina
- industry
-
insig1
- biofuel production
-
oleosins
-
cholinephosphotransferase
- elovl6
- drug development
-
triacylglyceride
-
holstein-friesian
- sn-1,2-diacylglycerols
- analysis
- glycerolphosphate
- oleoyl-coa
- protein-1c
-
lipin
- lpaat
-
ricinoleic
- medicine
- baylyi
- chylomicronemia
- biotechnology
-
steryl
-
kennedy
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
dgat1, dgat2, dgat, diacylglycerol acyltransferase, diacylglycerol acyltransferase 1, diacylglycerol o-acyltransferase, dgat-1, monoacylglycerol acyltransferase, acyl-coa:diacylglycerol acyltransferase, diacylglycerol acyltransferase 2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,2-diacylglycerol acyltransferase
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acyl-CoA:1,2-dioleoyl-sn-glycerol acyltransferase
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acyltransferase, diacylglycerol
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DGAT
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DGAT1
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DGAT1A
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DGAT2
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DGAT2A
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diacylglycerol acyltransferase
diglyceride acyltransferase
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diglyceride O-acyltransferase
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palmitoyl-CoA-sn-1,2-diacylglycerol acyltransferase
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diacylglycerol acyltransferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:1,2-diacyl-sn-glycerol O-acyltransferase
Palmitoyl-CoA and other long-chain acyl-CoAs can act as donors.
CAS REGISTRY NUMBER
COMMENTARY
9029-98-5
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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
acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
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endogenous 1,2-diacylglycerol
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-
?
acyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-oleoyl-3-acylglycerol
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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
acyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-oleoyl-3-acylglycerol
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-
-
-
?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
both the N and C termini are oriented toward the cytosol and have different catalytic roles. A highly conserved motif, 129YFP131, and a hydrophilic segment exclusive to yeast DGAT2 reside in a long endoplasmic reticulum luminal loop following the first transmembrane domain and play an essential role in enzyme catalysis. The strongly conserved residue His195 within the motif HPHG, which may play a role in the active site of DGAT2, is likely embedded in the membrane
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
overexpression of the enzyme gene in Saccharomyces cerevisiae leads to accumulation of full-length prtein in wild-type and accumulation of full-length protein and a N-terminally truncated protein in a snf2 disruption mutant, lacking a DNA-dependent ATPase that forms the SWI/SNF chromatin remodeling complex. Proteolytic cleavage at the N-terminal region is involved in enzyme activation in the snf2 disruptant, a major cleavage site lies between residues Lys29 and Ser30
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic cleavage at the N-terminal region is involved in enzyme activation in the snf2 disruptant, which lacks a DNA-dependent ATPase that forms the SWI/SNF chromatin remodeling complex. Major cleavage site lies between residues Lys29 and Ser30
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H193E/G196S
mutation to corresponding motif found in plant, abolishes enzymic activity
additional information
additional information
construction of N- and C-terminal truncation mutants N1(DELTA1-62), N2 (DELTA1-33), C1 (DELTA374-418), C2 (DELTA391-418), C3 (DELTA413-418), C4 (DELTA413-418, 413::A6). Mutant N1 lacking the entire hydrophilic N terminus presents minimal activity while maintaining a substantial expression level. Removal of the first 33 amino acid residues in the N-terminus, mutant N2, results in minor decrease in enzyme activity. Deletion of the last six amino acid residues from the C-terminus, mutant C3, causes a decrease in the enzyme activity of more than 80%. Deletion of the whole C-terminus, mutant C1, completely abolishes the enzyme activity and has a substantial impact on the protein accumulation. Mutant C2 lacking about half of the C-terminus, exhibits a complete loss of activity. In mutant C4, the last six amino acid residues are replaced with six alanine residues. This mutant retains similar activity and expression levels to C3. Deletion of the first putative TMD between residues 70 and 91 also results in the total loss of activity
additional information
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construction of N- and C-terminal truncation mutants N1(DELTA1-62), N2 (DELTA1-33), C1 (DELTA374-418), C2 (DELTA391-418), C3 (DELTA413-418), C4 (DELTA413-418, 413::A6). Mutant N1 lacking the entire hydrophilic N terminus presents minimal activity while maintaining a substantial expression level. Removal of the first 33 amino acid residues in the N-terminus, mutant N2, results in minor decrease in enzyme activity. Deletion of the last six amino acid residues from the C-terminus, mutant C3, causes a decrease in the enzyme activity of more than 80%. Deletion of the whole C-terminus, mutant C1, completely abolishes the enzyme activity and has a substantial impact on the protein accumulation. Mutant C2 lacking about half of the C-terminus, exhibits a complete loss of activity. In mutant C4, the last six amino acid residues are replaced with six alanine residues. This mutant retains similar activity and expression levels to C3. Deletion of the first putative TMD between residues 70 and 91 also results in the total loss of activity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
the enzyme without the N-terminal 29 amino acids is expressed in Saccharomyces cerevisiae mutant DELTAdga1
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Christiansen, K.
Utilization of endogenous diacylglycerol for the synthesis of triacylglycerol, phosphatidylcholine and phosphatidylethanolamine by lipid particles from bakers yeast (Saccharomyces cerevisiae)
Biochim. Biophys. Acta
574
448-460
1979
Saccharomyces cerevisiae
Kamisaka, Y.; Kimura, K.; Uemura, H.; Shibakami, M.
Activation of diacylglycerol acyltransferase expressed in Saccharomyces cerevisiae: overexpression of Dga1p lacking the N-terminal region in the Deltasnf2 disruptant produces a significant increase in its enzyme activity
Appl. Microbiol. Biotechnol.
88
105-115
2010
Saccharomyces cerevisiae (Q08650), Saccharomyces cerevisiae
Liu, Q.; Siloto, R.M.; Snyder, C.L.; Weselake, R.J.
Functional and topological analysis of yeast acyl-CoA:diacylglycerol acyltransferase 2, an endoplasmic reticulum enzyme essential for triacylglycerol biosynthesis
J. Biol. Chem.
286
13115-13126
2011
Saccharomyces cerevisiae (Q08650), Saccharomyces cerevisiae
EXTERNAL LINKS (specific for EC-Number 2.3.1.20)
Transporter Classification Database (TCDB): 2.A.50.4.1, 2.A.50.4.10
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Release 2023.1 (January 2023)
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