In biochemistry, isozymes (also known as isoenzymes or more generally as multiple forms of enzymes) are enzymes that differ in amino acid sequence but catalyze the same chemical reaction. Isozymes usually have different kinetic parameters (e.g. different KM values), or are regulated differently.

May 29, 2023 · Isozymes (also known as isoenzymes) are enzymes that differ in amino acid sequence but catalyze the same chemical reaction. These enzymes usually display different kinetic parameters (i.e. different KM values), or different regulatory properties.

Isozymes are present in the serum and tissues of mammals, amphibians, birds, insects, plants and unicellular organisms. Examples: Isozymes of numerous dehydro­genases, and several oxidases, transaminases, phosphatases, transphosphorylases, proteolytic en­zymes, aldolases. Characteristics of Isozymes: 1.

Isozymes are defined as multiple molecular forms of an enzyme demonstrating similar or identical catalytic properties.81 Three major categories of isozymes are tabulated by Harris.81 (a) Isozymes resulting from multiple gene loci coding distinctly different polypeptide chains; (b) isozymes arising as a result of multiple alleles at a single locu...

Mar 11, 2024 · Isozymes, also known as isoenzymes, are enzymes that differ in amino acid sequence but catalyze the same chemical reaction· They usually have different kinetic parameters or are regulated differently. Isozymes are often the result of gene duplication, but can also arise from polyploidization or nucleic acid hybridization.

Isozymes (also known as isoenzymes) are enzymes with varied amino acid sequences that catalyse the same chemical process. Various kinetic parameters (i.e. different KM values) or regulatory characteristics are frequently displayed by these enzymes.

Isozymes are defined as multiple forms of enzymes occurring in the same organism and having similar or identical catalytic activities. They are usually demonstrated by the technique of zone electrophoresis followed by in situ histochemical staining for the specific activity. Most isozymes can be classified into primary and secondary types.

Isoenzymes (or isozymes) are a group of enzymes that catalyze the same reaction but have different enzyme forms and catalytic efficiencies. Isozymes are usually distinguished by their electrophoretic mobilities. All living systems apparently require multiple molecular forms of certain enzymes in order to maximize biological capacity.

any of several forms of an enzyme that all catalyze the same reaction but may differ in reaction rate, inhibition by various substances, electrophoretic mobility, or immunologic properties. Several enzymes, particularly alkaline phosphatase, lactate dehydrogenase, and creatine kinase, have clinically important isoenzymes.

Isozymes (also known as isoenzymes) are homologous enzymes that catalyze the same reaction but differ in structure. The differences in the isozymes allow them to regulate the same reaction at different places in the specie. In particular they differ in amino acid sequences. They display different kinetic parameters as well as regulatory properties.