Atg8 activating enzyme activity

Definition

Target type: molecularfunction

Catalysis of the activation of the small ubiquitin-related modifier APG8, through the formation of an ATP-dependent high-energy thiolester bond. [GOC:mah]

Atg8 activating enzyme activity is a crucial step in the autophagy pathway, a cellular process responsible for degrading and recycling damaged organelles and proteins. This activity is catalyzed by an enzyme called Atg7, which plays a vital role in attaching the Atg8 protein to the autophagosomal membrane. The process starts with Atg7 activating Atg8 by first converting it into a high-energy thioester intermediate. This reaction involves the transfer of AMP from ATP to the carboxyl terminus of Atg8, generating Atg8-AMP. Next, Atg7 transfers the activated Atg8-AMP to the carboxyl terminus of phosphatidylethanolamine (PE), a lipid molecule present in the autophagosomal membrane. This process results in the formation of a covalent bond between Atg8 and PE, which anchors Atg8 to the autophagosomal membrane. This attachment of Atg8 to the membrane is essential for the formation of the autophagosome, the double-membrane vesicle that engulfs the cellular cargo destined for degradation. The Atg8 activating enzyme activity, therefore, plays a critical role in the initiation and progression of autophagy, enabling the efficient removal of damaged cellular components and maintaining cellular homeostasis.'
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Proteins (1)

Compounds (1)