2.3.1.158: phospholipid:diacylglycerol acyltransferase
This is an abbreviated version!
For detailed information about phospholipid:diacylglycerol acyltransferase, go to the full flat file.
Word Map on EC 2.3.1.158
-
2.3.1.158
-
diacylglycerols
-
acyl-coa:diacylglycerol
-
biodiesel
-
acyl-coa-dependent
-
acyltransferase1
-
presenile
-
biotechnology
-
camelina
-
lpcat
-
accase
-
oleosins
-
energy production
-
industry
-
synthesis
-
molecular biology
- 2.3.1.158
- diacylglycerols
-
acyl-coa:diacylglycerol
-
biodiesel
-
acyl-coa-dependent
-
acyltransferase1
-
presenile
- biotechnology
- camelina
- lpcat
- accase
-
oleosins
- energy production
- industry
- synthesis
- molecular biology
Reaction
Synonyms
acyl-CoA-independent phospholipid:diacylglycerol acyltransferase, At3g44830, At5g13640, AtPDAT1, AtPDAT2, CHLREDRAFT_184281, CHLREDRAFT_188937, CsPDAT1-A, CsPDAT1-B, CsPDAT1-C, CsPDAT2-A, CsPDAT2-B, DGTT1, DGTT2, DGTT3, diacylglycerol acyltransferase type 2, LRO1, MiPDAT, PDAT, PDAT1, PDAT1A, PDAT2, phospholipid: diacylglycerol acyltransferase, phospholipid:diacylglycerol acyltransferase, ScPDAT, SiPDAT, SiPDAT2, YNR008w
ECTree
2.3.1.158 phospholipid:diacylglycerol acyltransferaseAdvanced search results
results (
results (Application
Application on EC 2.3.1.158 - phospholipid:diacylglycerol acyltransferase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
biotechnology
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
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
molecular biology
-
the conversion of a membrane bound lipid metabolizing enzyme into a soluble and active form might be applied to other enzymes with a membrane anchor region.
synthesis
-
the enzyme is useful for production of hydroxylated fatty acids and furtheron polyesters, biodiesel, and lubricants in transgenic plants expressing PDAT thereby avoiding the toxicity of castor bean seeds
biotechnology
-
the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production
biotechnology
-
the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production
biotechnology
the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production
biotechnology
the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production
biotechnology
the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production
biotechnology
the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production
biotechnology
Lobosphaera incisa Reisigl H4301
-
the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production
-
