Evolutionary Analysis of Aspartate Aminotransferases

Overview

Journal J Mol Evol

Specialty Biochemistry

Date 1995 Apr 1

PMID 7769621

Citations 11

Authors

C S Winefield

K J Farnden

P H Reynolds

C J Marshall

Affiliations

Soon will be listed here.

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.

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