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The involvement of phospholipid:diacylglycerol acyltransferases in triacylglycerol production

Banas, A ; Dahlqvist, A ; Ståhl, U ; Lenman, Marit LU and Stymne, S (2000) In Biochemical Society Transactions 28(6). p.703-705
Abstract
We have characterized three CoA-independent types of enzyme, phospholipases, phospholipid:diacylglycerol acyltransferases (PDATs) and cholinephosphotransferases, responsible for the removal of unusual fatty acids from phosphatidylcholine (PC) in microsomal preparations from developing oil seeds. The metabolism of sn-2-[(14)C]acyl-PC was monitored in microsomal preparations from various oilseeds having either medium-chain, acetylenic, epoxy or hydroxy fatty acids as their major fatty acids in the oil. The results indicate that PDAT plays a major role in removing ricinoleic acid and vernolic acid from phospholipids in Ricinus communis and Crepis palaestina seeds, respectively. However, vernolic, crepenynic and capric acids are primarily... (More)
We have characterized three CoA-independent types of enzyme, phospholipases, phospholipid:diacylglycerol acyltransferases (PDATs) and cholinephosphotransferases, responsible for the removal of unusual fatty acids from phosphatidylcholine (PC) in microsomal preparations from developing oil seeds. The metabolism of sn-2-[(14)C]acyl-PC was monitored in microsomal preparations from various oilseeds having either medium-chain, acetylenic, epoxy or hydroxy fatty acids as their major fatty acids in the oil. The results indicate that PDAT plays a major role in removing ricinoleic acid and vernolic acid from phospholipids in Ricinus communis and Crepis palaestina seeds, respectively. However, vernolic, crepenynic and capric acids are primarily removed from phospholipids by phospholipases in Euphorbia lagascae, Crepis rubra and elm seeds, respectively. Further, we show that significant PDAT activity is also present in vegetative tissues of Arabidopsis thaliana. (Less)
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author
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publishing date
type
Contribution to journal
publication status
published
subject
keywords
lipid, oleosine, protein, starch
in
Biochemical Society Transactions
volume
28
issue
6
pages
703 - 705
publisher
Biochemical Society
external identifiers
  • scopus:0034470082
ISSN
0300-5127
language
English
LU publication?
no
additional info
The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Department of Cell and Organism Biology (Closed 2011.) (011002100)
id
546da1ac-af06-4a99-8af1-dec8f4617e0f (old id 1209851)
date added to LUP
2016-04-01 12:01:30
date last changed
2022-03-28 19:06:52
@article{546da1ac-af06-4a99-8af1-dec8f4617e0f,
  abstract     = {{We have characterized three CoA-independent types of enzyme, phospholipases, phospholipid:diacylglycerol acyltransferases (PDATs) and cholinephosphotransferases, responsible for the removal of unusual fatty acids from phosphatidylcholine (PC) in microsomal preparations from developing oil seeds. The metabolism of sn-2-[(14)C]acyl-PC was monitored in microsomal preparations from various oilseeds having either medium-chain, acetylenic, epoxy or hydroxy fatty acids as their major fatty acids in the oil. The results indicate that PDAT plays a major role in removing ricinoleic acid and vernolic acid from phospholipids in Ricinus communis and Crepis palaestina seeds, respectively. However, vernolic, crepenynic and capric acids are primarily removed from phospholipids by phospholipases in Euphorbia lagascae, Crepis rubra and elm seeds, respectively. Further, we show that significant PDAT activity is also present in vegetative tissues of Arabidopsis thaliana.}},
  author       = {{Banas, A and Dahlqvist, A and Ståhl, U and Lenman, Marit and Stymne, S}},
  issn         = {{0300-5127}},
  keywords     = {{lipid; oleosine; protein; starch}},
  language     = {{eng}},
  number       = {{6}},
  pages        = {{703--705}},
  publisher    = {{Biochemical Society}},
  series       = {{Biochemical Society Transactions}},
  title        = {{The involvement of phospholipid:diacylglycerol acyltransferases in triacylglycerol production}},
  volume       = {{28}},
  year         = {{2000}},
}