Recombinant Human AASDHPPT protein

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

AASDHPPT also known as L-aminoadipate-semialdehyde dehydrogenase phosphopantetheinyl transferase is a specialized enzyme that catalyzes the transfer of 4'-phosphopantetheine from coenzyme A to holo-acyl carrier protein (ACP) domains. With a molecular mass of approximately 32 kDa AASDHPPT plays an important role in the post-translational modification of ACP domains in lysine biosynthesis. This enzyme expresses in many tissues with strong presence in liver and kidney tissues. Its enzymatic activity is vital for maintaining proper cellular function.

Biological function summary

AASDHPPT functions by participating in the synthesis of lysine through its role as a phosphopantetheinyl transferase enzyme. It is an essential part of the post-translational modification complex that ensures correct functionality of ACP domains involved in metabolic pathways. Through modification of ACP domains AASDHPPT supports the synthesis of important biomolecules essential for metabolic processes. The enzyme's activity has direct impact on the production and availability of lysine an amino acid necessary for protein synthesis and various metabolic functions.

Pathways

AASDHPPT integrates into several critical metabolic pathways prominently the lysine biosynthesis pathway. Additionally its function links closely with fatty acid biosynthesis pathways due to the common role of ACP domains in numerous metabolic transformations. In the context of these pathways AASDHPPT associates with proteins like serine palmitoyltransferase emphasizing its broad role in metabolic regulation and enzyme activation during biosynthetic reactions.

AASDHPPT links to certain metabolic disorders such as familial hyperlysinemia which arises from disruptions in the lysine biosynthesis pathway. Alterations in AASDHPPT activity can affect lysine levels and metabolic balance contributing to this condition. Additionally improper function of this enzyme has indirect connections to metabolic disorders involving the liver as variations in pathway activity can impact liver function. The enzyme interacts with proteins such as alpha-aminoadipic semialdehyde dehydrogenase further illustrating its involvement in a network of metabolic processes and potential disease links.