synthase1like

synthase1like is a protein-coding gene identified in several eukaryotic genomes, most notably in yeast and mammalian cells. It encodes a member of the synthase family, characterized by a Rossmann‑fold domain implicated in ATP binding. The protein is thought to participate in lipid or carbohydrate biosynthesis pathways, although its precise enzymatic activity remains unconfirmed.

Biochemical studies in Saccharomyces cerevisiae have shown that deletions of synthase1like result in growth defects when cells are grown on nonfermentable carbon sources, suggesting a role in mitochondrial metabolism. In mammalian cells, transcript levels of synthase1like are highest in the liver and brown adipose tissue, indicating possible involvement in fatty acid oxidation or energy homeostasis. Knockdown experiments in cultured hepatocytes lead to accumulation of acyl‑carnitines, further supporting a metabolic regulatory function.

The gene shares conserved motifs with bacterial and plant synthases involved in cofactor synthesis, hinting at an evolutionary conserved mechanism. Structural modeling predicts a catalytic triad comprised of Ser, Asp, and His residues, a common arrangement in acyl‑transferase enzymes. Mutagenesis of these residues reduces enzymatic activity in vitro, confirming their functional importance.

Clinical relevance has been suggested by genome‑wide association studies linking polymorphisms in synthase1like to altered lipid profiles in humans. However, no direct disease association has been established to date. Further biochemical characterization and in‑vivo studies are required to delineate its exact role in cellular metabolism.