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Evolutionary analysis of aspartate aminotransferases

Authors :
Christopher S. Winefield
Paul H. S. Reynolds
Craig J. Marshall
Kevin J. F. Farnden
Source :
Journal of Molecular Evolution. 40:455-463
Publication Year :
1995
Publisher :
Springer Science and Business Media LLC, 1995.

Abstract

Aspartate aminotransferase isoenzymes are located in both the cytosol and organelles of eukaryotes, but all are encoded in the nuclear genome. In the work described here, a phylogenetic analysis was made of aspartate aminotransferases from plants, animals, yeast, and a number of bacteria. This analysis suggested that five distinct branches are present in the aspartate aminotransferase tree. Mitochondrial forms of the enzyme form one distinct group, bacterial aspartate aminotransferase formed another, and the plant and vertebrate cytosolic isoenzymes each formed a distinct group. Plant cytosolic isozymes formed a further group of which the plastid sequences were a member. The yeast mitochondrial and cytosolic aspartate aminotransferases formed groups separate from other members of the family.

Details

ISSN :
14321432 and 00222844
Volume :
40
Database :
OpenAIRE
Journal :
Journal of Molecular Evolution
Accession number :
edsair.doi.dedup.....c879c1ed453fc06b9f2a3a526f4163db
Full Text :
https://doi.org/10.1007/bf00164031