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PMID: 7769621 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

Evolutionary analysis of aspartate aminotransferases.

Journal of molecular evolution ·Vol. 40 ·No. 4 ·1995-04-00 ·Pages 455-63

Winefield CS, Farnden KJ, Reynolds PH, Marshall CJ

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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Article Info
Journal
Journal of molecular evolution
Abbr.
J Mol Evol
ISSN
0022-2844
Published
1995-04-00
Pages
455-63
Language
English
Region
Germany
NLM ID
0360051
Subset
IM
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