Anti-GART antibody [EPR11622]

Supplementary info

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

Activity summary

GART also known as phosphoribosylglycinamide formyltransferase is a multifunctional enzyme with a mass of approximately 100 kDa. It plays a significant mechanical role in purine biosynthesis. GART is primarily expressed in rapidly dividing cells and tissues with high metabolic activity. It is one of three enzymes encoded by the GART gene contributing to the trifunctional protein complex that includes glycinamide ribonucleotide synthetase (GARS) and aminoimidazole ribonucleotide synthetase (AIRS). These enzyme functions are critical for the mechanistic steps in purine metabolism increasing their importance in synthesizing nucleotides for DNA and RNA production.

Biological function summary

GART is involved in synthesizing purine nucleotides through its role in converting phosphoribosylamine to phosphoribosylglycinamide. It does this by catalyzing the transfer of a formyl group highlighting its operation as part of a trifunctional protein. The complex formation with enzymes GARS and AIRS enables efficient handling of intermediates therefore fostering a streamlined biosynthetic process. This contributes directly to the cellular nucleotide pool which is fundamental for cell proliferation signaling and energy transfer.

Pathways

GART fits into the purine biosynthetic pathway which is essential for nucleotide synthesis. This function links it closely with proteins such as IMP dehydrogenase which further processes inosine monophosphate to produce different purine nucleotides. It is also involved in folate metabolism as it requires folate derivatives for its formyl transferase activity. The close association with these pathways illustrates GART's integral role in both cellular growth and maintenance of genetic material.

Associated diseases and disorders

GART has implications in cancer and neurological disorders due to its role in nucleotide synthesis and cellular proliferation. Elevated expression levels of GART are observed in tumors indicating its potential involvement in oncogenesis. In addition abnormalities in purine metabolism or folate cycling can contribute to disorders like Down syndrome. Within this context proteins interacting with GART such as GARS and AIRS could potentially serve as associated targets for therapeutic intervention emphasizing the enzyme's relevance in disease pathology.