Brassica napus cDNAs encoding fatty acyl-CoA synthetase

Brassica napus cDNAs encoding fatty acyl-CoA synthetase From a cDNA library of developing siliques of rapeseed (Brassica napus L.) we have isolated five full-length clones encoding polypeptides of the AMP-binding protein family. Two cDNAs encode fatty acyl-CoA synthetase activity (EC 6.2.1.3). The deduced polypeptides share about 52% identical amino acids. After expression in Escherichia coli the predicted enzymatic activity was confirmed by in vitro assays and product analysis. The enzymatic activity for one of the clones was characterized in detail by determination of the K m for oleic acid (10.4 µm) and the pH optimum (between 7 and 8). For the three additional clones no enzymatic activities could be demonstrated after expression in E. coli, although two of them exhibit similarity to either eukaryotic or prokaryotic acyl-CoA synthetases. The sequences are compared to a number of related expressed sequence tags from Brassica and Arabidopsis. Potential subcellular locations and functions of the deduced polypeptides within plant cells are discussed. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Plant Molecular Biology Springer Journals

Brassica napus cDNAs encoding fatty acyl-CoA synthetase

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Publisher
Kluwer Academic Publishers
Copyright
Copyright © 1997 by Kluwer Academic Publishers
Subject
Life Sciences; Biochemistry, general; Plant Sciences; Plant Pathology
ISSN
0167-4412
eISSN
1573-5028
D.O.I.
10.1023/A:1005780529307
Publisher site
See Article on Publisher Site

Abstract

From a cDNA library of developing siliques of rapeseed (Brassica napus L.) we have isolated five full-length clones encoding polypeptides of the AMP-binding protein family. Two cDNAs encode fatty acyl-CoA synthetase activity (EC 6.2.1.3). The deduced polypeptides share about 52% identical amino acids. After expression in Escherichia coli the predicted enzymatic activity was confirmed by in vitro assays and product analysis. The enzymatic activity for one of the clones was characterized in detail by determination of the K m for oleic acid (10.4 µm) and the pH optimum (between 7 and 8). For the three additional clones no enzymatic activities could be demonstrated after expression in E. coli, although two of them exhibit similarity to either eukaryotic or prokaryotic acyl-CoA synthetases. The sequences are compared to a number of related expressed sequence tags from Brassica and Arabidopsis. Potential subcellular locations and functions of the deduced polypeptides within plant cells are discussed.

Journal

Plant Molecular BiologySpringer Journals

Published: Sep 29, 2004

References

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