ADSSL1

The subcellular localization of ADSSL1 protein is primarily within mitochondria, facilitated by mitochondrial targeting sequences and import machinery.

Post-translational modifications, such as phosphorylation or acetylation, and regulatory factors like metabolic signals or protein-protein interactions, may modulate the activity or stability of ADSSL1 protein.

ADSSL1 protein can interact with other enzymes involved in purine metabolism, forming complexes that regulate nucleotide synthesis and energy metabolism.

Genetic variations or mutations in the ADSSL1 gene can impact the expression or function of ADSSL1 protein, potentially leading to disorders associated with purine metabolism abnormalities.

ADSSL1 protein plays a critical role in purine nucleotide metabolism, contributing to the deamination and recycling of adenylosuccinate to maintain nucleotide homeostasis.

ADSSL1 protein contains conserved structural domains, including a catalytic domain and nucleotide-binding motifs, that contribute to its enzymatic activity and substrate specificity.

The enzymatic activity of ADSSL1 protein, catalyzing the conversion of adenylosuccinate to AMP, can be measured using enzymatic assays that quantify substrate utilization and product formation.

Experimental approaches such as knockout or overexpression studies have been utilized to investigate the functional significance of ADSSL1 protein, revealing its role in cellular metabolism and energy balance.

ADSSL1 protein exhibits tissue-specific expression, with higher levels observed in skeletal muscle, heart, and brain. Factors involved in its regulation include transcriptional control and signaling pathways.

Dysregulation or dysfunction of ADSSL1 protein can disrupt cellular purine metabolism, leading to imbalances in nucleotide levels and potential contributions to diseases such as neurodegenerative disorders or metabolic syndromes.