Ancient divergence of long and short isoforms of adenylate kinase molecular evolution of the nucleoside monophosphate kinase family
- 6 May 1996
- journal article
- Published by Wiley in FEBS Letters
- Vol. 385 (3) , 214-220
- https://doi.org/10.1016/0014-5793(96)00367-5
Abstract
Adenylate kinases (AK) from vertebrates are separated into three isoforms, AK1, AK2 and AK3, based on structure, subcellular localization and substrate specificity. AK1 is the short type with the amino acid sequence being 27 residues shorter than sequences of the long types, AK2 and AK3. A phylogenetic tree prepared for the AK isozymes and other members of the nucleoside monophosphate (NMP) kinase family shows that the divergence of long and short types occurred first and then differentiation in subcellular localization or substrate specificity took place. The first step involved a drastic change in the three-dimensional structure of the LID domain. The second step was caused mainly by smaller changes in amino acid sequences.Keywords
This publication has 54 references indexed in Scilit:
- The Structure of Uridylate Kinase with Its Substrates, Showing the Transition State GeometryJournal of Molecular Biology, 1994
- Site‐directed mutagenesis of AMP‐binding residues in adenylate kinase Alteration of substrate specificityFEBS Letters, 1993
- The adenylate kinase family in yeast: identification of URA6 as a multicopy suppressor of deficiency in major AMP kinaseGene, 1992
- The rapid generation of mutation data matrices from protein sequencesBioinformatics, 1992
- Refined structure of the complex between guanylate kinase and its substrate GMP at 2·0 Å resolutionJournal of Molecular Biology, 1992
- Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9 Å resolutionJournal of Molecular Biology, 1992
- The refined structure of the complex between adenylate kinase from beef heart mitochondrial matrix and its substrate AMP at 1.85 Å resolutionJournal of Molecular Biology, 1991
- Induced-fit movements in adenylate kinasesJournal of Molecular Biology, 1990
- Structure of the complex of adenylate kinase from Escherichia coli with the inhibitor P1,P5-di(adenosine-5′-)pentaphosphateJournal of Molecular Biology, 1988
- Confidence Limits on Phylogenies: An Approach Using the BootstrapEvolution, 1985