Summary
We report here the complete amino acid sequences of the cytosolic and mitochondrial aspartate aminotransferases from horse heart. The two sequences can be aligned so that 48.1% of the amino acid residues are identical. The sequences have been compared with those of the cytosolic isoenzymes from pig and chicken, the mitochondrial isoenzymes from pig, chicken, rat, and human, and the enzyme fromEscherichia coli. The results suggest that the mammalian cytosolic and mitochondrial isoenzymes have evolved at equal and constant rates whereas the isoenzymes from chicken may have evolved somewhat more slowly. Based on the rate of evolution of the mammalian isoenzymes, the geneduplication event that gave rise to cytosolic and mitochondrial aspartate aminotransferases is estimated to have occurred at least 109 years ago. The cytosolic and mitochondrial isoenzymes are equally related to the enzyme fromE. coli; the prokaryotic and eukaryotic enzymes diverged from one another at least 1.3×109 years ago.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Barra D, Bossa F, Doonan S, Fahmy HMA, Martini F, Hughes GJ (1976) Large scale purification and some properties of the mitochondrial aspartate aminotransferase from pig heart. Eur J Biochem 64:519–526
Barra D, Bossa F, Doonan S, Fahmy HMA, Hughes GJ, Martini F, Petruzzelli R, Wittman-Liebold B (1980) The cytosolic and mitochondrial aspartate aminotransferases from pig heart: a comparison of their primary structures predicted secondary structures and some physical properties. Eur J Biochem 108:405–414
Barra D, Schininà ME, Simmaco M, Bannister JV, Bannister WH, Rotilio G, Bossa F (1984) The primary structure of human liver manganese superoxide dismutase. J Biol Chem 259:12595–12601
Bossa F, Barra D, Martini F, Schininà ME, Doonan S, O'Donovan KMC (1981) Interspecies comparisons of aspartate aminotransferases based on terminal and active site sequences. Comp Biochem Physiol [B] 69:753–760
Dayhoff M (ed) (1978) Atlas of protein sequence and structure, vol 5, suppl 3. National Biomedical Research Foundation, Silver Spring, Maryland
Dobzhansky T, Ayala FJ, Stebbins GL, Valentine JW (1977) Evolution. WH Freeman, San Francisco
Doonan S, Doonan HJ, Hanford R, Vernon CA, Walker JM, Airoldi LP da S, Bossa F, Barra D, Carloni M, Fasella P, Riva F (1975) The primary structure of aspartate aminotransferase from pig heart muscle. Biochem J 149:497–506
Doonan S, Marra E, Passarella S, Saccone C, Quagliariello E (1984a) Transport of proteins into mitochondria. Int Rev Cytol 91:141–186
Doonan S, Barra D, Bossa F (1984b) Structural and genetic relationships between cytosolic and mitochondrial isoenzymes. Int J Biochem 16:1193–1199
Goodman M (1985) Rates of molecular evolution: the hominid slowdown. BioEssays 3:9–14
Graff-Hausner U, Wilson KJ, Christen P (1983) The covalent structure of mitochondrial aspartate aminotransferase from chicken: identification of segments of the polypeptide chain invariant specifically in the mitochondrial isoenzyme. J Biol Chem 258:8813–8826
Huynh QK, Sakakibara R, Watanabe T, Wada H (1980) Primary structure of mitochondrial glutamic oxaloacetic transaminase from rat liver: comparison with that of the pig heart isozyme. Biochem Biophys Res Commun 97:474–479
Joh T, Nomiyama H, Maeda S, Shimada K, Morino Y (1985) Cloning and sequence analysis of a cDNA encoding porcine mitochondrial aspartate aminotransferase precursor. Proc Natl Acad Sci USA 82:6065–6069
Kimura M (1983) The neutral theory of molecular evolution. Cambridge University Press, Cambridge, England
Kondo K, Wakabayashi S, Yagi T, Kagamiyama H (1984) The complete amino acid sequence of aspartate aminotransferase fromEscherichia coli: sequence comparisons with pig isoenzymes. Biochem Biophys Res Commun 122:62–67
Lee YM, Friedman DJ, Ayala FJ (1985) Complete amino acid sequence of copper-zinc superoxide dismutase fromDrosophila melanogaster. Arch Biochem Biophys 241:577–589
Lipman DJ, Pearson WR (1985) Rapid and sensitive protein similarity searches. Science 227:1435–1441
Martini F, Angelaccio S, Barra D, Doonan S, Bossa F (1983) Primary structure of aspartate aminotransferase from horse heart and comparison with that of other homotopic and heterotopic isoenzymes. Comp Biochem Physiol [B] 76:483–487
Martini F, Angelaccio S, Barra D, Doonan S, Bossa F (1984) Partial amino acid sequence and cysteine reactivities of cytosolic aspartate aminotransferase from horse heart. Biochim Biophys Acta 789:51–56
Martini F, Angelaccio S, Barra D, Pascarella S, Maras B, Doonan S, Bossa F (1985) The primary structure of mitochondrial aspartate aminotransferase from human heart. Biochim Biophys Acta 832:46–51
O'Donovan KMC, Doonan S, Marra E, Passarella S, Quagliariello E (1985) Removal of an N-terminal peptide from mitochondrial aspartate aminotransferase abolishes its interactions with mitochondria in vitro. Biochem J 228:609–614
Porter PB, Doonan S, Pearce FL (1981a) Interspecies comparisons of aspartate aminotransferases based on immunochemical methods. Comp Biochem Physiol [B] 69:761–767
Porter PB, Barra D, Bossa F, Cantalupo G, Doonan S, Martini F, Sheehan D, Wilkinson SM (1981b) Purification and basic properties of the aspartate aminotransferases from a variety of sources. Comp Biochem Physiol [B] 69:737–746
Shlyapnikov SV, Myasnikov AN, Severin ES, Myagkova MA, Torchinsky YuM, Braunstein AE (1979) Primary structure of cytoplasmic aspartate aminotransferase from chicken heart and its homology with pig heart isoenzymes. FEBS Lett 106:385–388
Simmaco M, Barra D, Bossa F (1985) Separation of phenylthiohydantoin-amino acids by high-performance liquid chromatography and some applications in dansyl Edman sequence analysis. J Chromatogr 349:99–103
Sonderegger P, Christen P (1978) Comparison of the evolution rates of cytosolic and mitochondrial aspartate aminotransferases. Nature 275:157–159
Sonderegger P, Gehring H, Christen P (1977) Interspecies comparison of cytosolic and mitochondrial aspartate aminotransferase: evidence for a more conservative evolution of the mitochondrial isoenzyme. J Biol Chem 252:609–612
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Doonan, S., Martini, F., Angelaccio, S. et al. The complete amino acid sequences of cytosolic and mitochondrial aspartate aminotransferases from horse heart, and inferences on evolution of the isoenzymes. J Mol Evol 23, 328–335 (1986). https://doi.org/10.1007/BF02100642
Received:
Revised:
Issue Date:
DOI: https://doi.org/10.1007/BF02100642