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Investigating the Kinetics of the Arabidopsis thaliana Acyltransferase At1g78690
Author(s) -
Jahns Max,
Garrett Teresa A
Publication year - 2019
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2019.33.1_supplement.796.5
Subject(s) - acyltransferase , chemistry , stereochemistry , arabidopsis thaliana , phosphatidylglycerol , arabidopsis , glycerophospholipids , biochemistry , acylation , enzyme , phospholipid , acyltransferases , biosynthesis , mutant , phosphatidylcholine , membrane , catalysis , gene
Headgroup acylated glycerophospholipids (GPLs) are a class of membrane phospholipids containing an acyl‐chain attached to the headgroup of the molecule that make up a relatively small portion of the cell envelope but are implicated in important functions such as the cell stress response and cell division. At1g78690 is an acyl‐transferase native to Arabidopsis thaliana that converts mono‐acylated GPLs to diacylated GPLs in vitro. Interestingly, overexpression of At1g78690 in E. coli leads to an accumulation of the headgroup acylated GPL acyl‐phosphatidylglycerol (acyl‐PG) in vivo . While At1g78690 is known to be capable of transferring an acyl chain from acyl‐CoA to two isoforms of bis (monoacyl glycerol) phosphate (BMP), 3,1’ BMP and 3,3’ BMP, to form acyl‐PG, it does not acylate 1,1’ BMP suggesting the enzyme possesses some stereoselectivity that needs to be further investigated. We reevaluate the extent to which At1g78690 is substrate selective, by further characterizing the ability of At1g78690 to acylate PG and 1,1 BMP. We also estimate the K m of At1g78690 on lyso‐PE, lyso‐PG, lyso PS, lyso‐PI, and 3,1’ and 3,3’ BMP. The kinetics of At1g78690 are measured via an acyl‐chain acceptor (either lyso‐PG, lyso‐PS, lyso‐PI, 3,1’ BMP or 3,3’ BMP) receiving a 13 C‐labeled acyl chain from acyl‐CoA. The kinetics of an enzyme can give insights into its substrate specificity, its catalytic and energetic properties, and its role in cellular phospholipid synthesis. Support or Funding Information This work was funded by National Science Foundation Research at Undergraduate Institution Award #1516805 to T. A. G. This abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .