N-Acetylputrescine

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Chemical compound



N-Acetylputrescine structure

N-Acetylputrescine is an acetylated derivative of the biogenic amine putrescine. It is a chemical compound that plays a role in the metabolism of polyamines, which are organic compounds having two or more primary amino groups.

Chemical Structure and Properties

N-Acetylputrescine is characterized by the presence of an acetyl group attached to the nitrogen atom of putrescine. The chemical formula for N-Acetylputrescine is C6H14N2O, and it has a molecular weight of 130.19 g/mol. The structure consists of a four-carbon chain with an acetyl group (CH3CO-) attached to one of the nitrogen atoms.

Biosynthesis and Metabolism

In biological systems, N-Acetylputrescine is formed through the acetylation of putrescine, a process catalyzed by the enzyme N-acetyltransferase. This modification is part of the polyamine catabolism pathway, which regulates the levels of polyamines in cells. Polyamines like putrescine, spermidine, and spermine are essential for cell growth and differentiation.

Biological Function

The acetylation of putrescine to form N-Acetylputrescine is a crucial step in the regulation of polyamine levels within the cell. This modification can affect the interaction of polyamines with DNA, RNA, and proteins, influencing various cellular processes such as gene expression, cell proliferation, and apoptosis.

Role in Disease

Alterations in polyamine metabolism, including the levels of N-Acetylputrescine, have been associated with several diseases, including cancer, neurodegenerative disorders, and inflammatory diseases. The dysregulation of polyamine acetylation can lead to abnormal cell growth and proliferation, contributing to the pathogenesis of these conditions.

Applications in Research

N-Acetylputrescine is used in research to study the role of polyamines in cellular processes and their implications in disease. It serves as a marker for polyamine metabolism and is used in assays to measure the activity of acetyltransferases and other enzymes involved in polyamine catabolism.

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Contributors: Prab R. Tumpati, MD