sphinganine-1-phosphate aldolase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: sphinganine 1-phosphate = phosphoethanolamine + palmitaldehyde. [EC:4.1.2.27]

Sphinganine-1-phosphate aldolase catalyzes the reversible aldol cleavage of sphinganine-1-phosphate (SPP) to palmitaldehyde and ethanolamine phosphate. This enzyme is a crucial component of the sphingolipid metabolic pathway, which is involved in a variety of cellular processes, including cell signaling, membrane organization, and apoptosis.

The aldol cleavage reaction is initiated by the formation of a Schiff base between the amino group of SPP and the active site lysine residue of the enzyme. This Schiff base intermediate is then stabilized by the interaction of the enzyme with the phosphate group of SPP. The aldol cleavage reaction proceeds through a series of proton transfer and electron rearrangement steps, ultimately resulting in the formation of palmitaldehyde and ethanolamine phosphate.

The activity of sphinganine-1-phosphate aldolase is regulated by a variety of factors, including the concentration of its substrates, the presence of inhibitors, and the cellular environment. The enzyme is also subject to post-translational modifications, such as phosphorylation, which can affect its activity.

The role of sphinganine-1-phosphate aldolase in cellular function is complex and multifaceted. The enzyme is involved in the biosynthesis of sphingolipids, which are essential components of cell membranes. It also plays a role in the degradation of sphingolipids, which is important for the removal of damaged or unwanted lipids.

In addition to its role in lipid metabolism, sphinganine-1-phosphate aldolase has been implicated in a number of other cellular processes, including cell growth, differentiation, and apoptosis. The enzyme is also a potential target for the development of new therapeutic agents for the treatment of diseases such as cancer and neurodegenerative disorders.'
"

Proteins (2)

Compounds (2)