Relationship between enzyme heterozygosity and quaternary structure
- 1 February 1977
- journal article
- research article
- Published by Springer Nature in Biochemical Genetics
- Vol. 15 (1-2) , 123-135
- https://doi.org/10.1007/bf00484555
Abstract
The need for proteins to maintain particular quaternary structures constrains variability in amino acid sequence. Monomeric enzymes are then expected to be more variable than dimeric forms, which in turn are expected to be more variable than tetrameric forms. These predictions are confirmed by analysis of available data on enzyme variation. Theories relating enzyme heterozygosity to metabolic function are discussed in the light of these findings.Keywords
This publication has 67 references indexed in Scilit:
- Genic variation in marginal populations of Drosophila subobscuraHereditas, 2009
- Genetics of Zoarces populationsHereditas, 2009
- Genic variation in Scandinavian populations of Drosophila bifasciataHereditas, 2009
- Genetics and Morphometrics of Cerion at Pongo Carpet: A New Systematic Approach to the Enigmatic Land SnailSystematic Zoology, 1974
- Mutational pressure as the main cause of molecular evolution and polymorphismNature, 1974
- Evolutionary Divergence in the Genus Taricha (Salamandridae)Ichthyology & Herpetology, 1974
- Genic Variation in Hybridizing Populations of Gophers (Genus Thomomys)Systematic Zoology, 1972
- Protein Variation and Systematics in Kangaroo Rats (Genus Dipodomys)Systematic Zoology, 1971
- Metabolic Implications of Polymorphism as an Adaptive StrategyNature, 1971
- A profile of Drosophila species' enzymes assayed by electrophoresis. I. Number of alleles, heterozygosities, and linkage disequilibrium in glucose-metabolizing systems and some other enzymesBiochemical Genetics, 1970