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Evolutionary analysis of aspartate aminotransferases
- 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.
- Subjects :
- Models, Molecular
Nuclear gene
endocrine system diseases
Protein Conformation
Molecular Sequence Data
Biology
Isozyme
Fungal Proteins
Cytosol
Bacterial Proteins
Species Specificity
Phylogenetics
Genetics
Amino Acid Sequence
Aspartate Aminotransferases
Plastid
Molecular Biology
Peptide sequence
Gene
Phylogeny
Ecology, Evolution, Behavior and Systematics
Plant Proteins
Cell Nucleus
Sequence Homology, Amino Acid
nutritional and metabolic diseases
Biological Evolution
Molecular biology
Yeast
Mitochondria
Isoenzymes
Eukaryotic Cells
Genes
Prokaryotic Cells
Biochemistry
Sequence Alignment
hormones, hormone substitutes, and hormone antagonists
Subjects
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