Isozymes
Isozymes (or isozymes) are enzymes that differ in amino acid sequence but catalyze the same chemical reaction. These enzymes usually display different kinetic parameters, 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.
History[edit | edit source]
The concept of isozymes was first proposed by R. Markert in 1956. He discovered that different enzymes could catalyze the same reaction, leading to the concept of isozymes.
Function[edit | edit source]
Isozymes often display different kinetic parameters. For example, they may have different Km and Vmax values for their substrates, or they may display different regulatory properties. The existence of isozymes allows for fine-tuning of metabolism to meet the specific needs of a given tissue or developmental stage.
Examples[edit | edit source]
Some examples of isozymes include lactate dehydrogenase, hexokinase, and cytochrome P450. These isozymes have different amino acid sequences but catalyze the same chemical reactions.
Clinical significance[edit | edit source]
Isozymes are clinically significant because they can be used as biomarkers for various diseases. For example, elevated levels of certain isozymes can indicate myocardial infarction, liver disease, or muscle damage.
See also[edit | edit source]
- Enzyme
- Amino acid
- Chemical reaction
- Metabolism
- R. Markert
- Km (biochemistry)
- Vmax (biology)
- Lactate dehydrogenase
- Hexokinase
- Cytochrome P450
- Biomarker
- Myocardial infarction
- Liver disease
- Muscle damage
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