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.
MeSH Terms
Amino Acid Sequence
Aspartate Aminotransferases/classification,genetics
Bacterial Proteins/genetics
Biological Evolution
Cell Nucleus
Cytosol/enzymology
Eukaryotic Cells/enzymology
Fungal Proteins/genetics
Genes
Isoenzymes/genetics
Mitochondria/enzymology
Models, Molecular
Molecular Sequence Data
Phylogeny
Plant Proteins/genetics
Prokaryotic Cells/enzymology
Protein Conformation
Sequence Alignment
Sequence Homology, Amino Acid
Species Specificity
Chemicals
Bacterial Proteins
Fungal Proteins
Isoenzymes
Plant Proteins
Aspartate Aminotransferases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Winefield C S
Department of Biochemistry, University of Otago, Dunedin, New Zealand.
Farnden K J
Reynolds P H
Marshall C J
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