Amastatin

Amastatin is a naturally occurring inhibitor of aminopeptidases, enzymes that catalyze the cleavage of amino acids from the amino terminus of protein or peptide substrates. It is a potent inhibitor of aminopeptidase A, which is responsible for the conversion of angiotensin II to angiotensin III. Amastatin is also an inhibitor of aminopeptidase B, leucine aminopeptidase, and microsomal aminopeptidase.

Amastatin was first isolated from the culture broths of two strains of Actinomycetes, Streptomyces and Nocardia, by researchers at the Tokyo University of Agriculture and Technology in 1976. It is a member of the oligopeptide class of compounds, which are composed of two or more amino acids linked by peptide bonds.

Chemical Structure and Properties[edit | edit source]

Amastatin is a dipeptide composed of the amino acids alanine and hydroxylysine, linked by a peptide bond. The hydroxylysine residue is further modified by the addition of a hydroxamic acid group, which is responsible for the compound's inhibitory activity.

The molecular formula of amastatin is C₈H₁₆N₂O₄, and its molecular weight is 204.22 g/mol. It is a white, crystalline solid that is soluble in water and polar organic solvents.

Biological Activity and Applications[edit | edit source]

Amastatin is a potent inhibitor of several aminopeptidases, with the highest activity against aminopeptidase A. This enzyme is responsible for the conversion of angiotensin II to angiotensin III, a process that is important in the regulation of blood pressure and fluid balance in the body. By inhibiting this enzyme, amastatin can potentially be used to treat hypertension and other cardiovascular diseases.

In addition to its potential therapeutic applications, amastatin is also used as a research tool in the study of aminopeptidases and their role in protein processing and degradation.

See Also[edit | edit source]

Amastatin Resources
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