Isozyme

Isozymes (also known as isoenzymes) are K_M values), or different regulatory properties. The existence of isozymes permits the fine-tuning of metabolism to meet the particular needs of a given tissue or developmental stage (for example lactate dehydrogenase (LDH)). In catalyse the same reaction, the two words are usually used interchangeably.

Introduction

Isozymes were first described by R. L. Hunter and Clement Markert (1957) who defined them as different variants of the same enzyme having identical functions and present in the same individual. This definition encompasses (1) enzyme variants that are the product of different genes and thus represent different loci (described as isozymes) and (2) enzymes that are the product of different alleles of the same gene (described as allozymes).

Isozymes are usually the result of gene duplication, but can also arise from polyploidisation or gene expression, then the two variants may both be favoured by natural selection and become specialised to different functions. For example, they may be expressed at different stages of development or in different tissues.

Allozymes may result from point mutations or from insertion-deletion (mutation, there are three things that may happen to a new allozyme:

1. It is most likely that the new allele will be non-functional — in which case it will probably result in low fitness and be removed from the population by natural selection.
2. Alternatively, if the genetic drift.
3. In rare cases the mutation may result in an enzyme that is more efficient, or one that can catalyse a slightly different chemical reaction, in which case the mutation may cause an increase in fitness, and be favoured by natural selection.

An example of an isozyme

An example of an isozyme is glycogen synthesis by liver cells. Both of these processes must only occur when glucose is abundant, or problems occur.

Distinguishing isozymes

Isozymes (and allozymes) are variants of the same enzyme. Unless they are identical in terms of their biochemical properties, for example their enzyme kinetics, they may be distinguished by a biochemical assay. However, such differences are usually subtle (particularly between allozymes which are often neutral variants). This subtlety is to be expected, because two enzymes that differ significantly in their function are unlikely to have been identified as isozymes.

Whilst isozymes may be almost identical in function, they may differ in other ways. In particular, cellulose acetate gels are now (as of 2005) the norm.

All the proteins from the tissue are present in the gel, so that individual enzymes must be identified using an assay that links their function to a staining reaction. For example, detection can be based on the localised NADP, which generated in zones of enzyme activity. This assay method requires that the enzymes are still functional after separation (native gel electrophoresis), and provides the greatest challenge to using isozymes as a laboratory technique.

Isozymes and allozymes as molecular markers

Population genetics is essentially a study of the causes and effects of genetic variation within and between populations, and in the past isozymes have been amongst the most widely used single nucleotide polymorphisms and microsatellites), they are still amongst the quickest and cheapest marker systems to develop, and remain (as of 2005) an excellent choice for projects that only need to identify low levels of genetic variation, e.g. quantifying mating systems.

Other major examples

• The metabolism and steroidogenesis.

References

• Hunter, R. L. and C.L. Merkert. (1957) Histochemical demonstration of enzymes separated by zone electrophoresis in starch gels. Science 125: 1294-1295
• Wendel, JF, and NF Weeden. 1990. "Visualisation and interpretation of plant isozymes." Pp. 5-45 in D. E. Soltis and P. S. Soltis, eds. Isozymes in plant biology. Chapman and Hall, London.
• Weeden, NF, and JF Wendel. 1990. "Genetics of plant isozymes". Pp. 46-72 in D. E. Soltis and P. S. Soltis, eds. Isozymes in plant biology. Chapman and Hall, London
• Crawford, DJ. 1989. "Enzyme electrophoresis and plant systematics". Pp. 146-164 in D. E. Soltis and P. S. Soltis, eds. Isozymes in plant biology. Dioscorides, Portland, Oregon.
• Hamrick, JL, and MJW Godt. 1990. "Allozyme diversity in plant species". Pp. 43-63 in A. H. D. Brown, M. T. Clegg, A. L. Kahler and B. S. Weir, eds. Plant Population Genetics, Breeding, and Genetic Resources. Sinauer, Sunderland