GMP synthase [glutamine-hydrolyzing], GMP synthetase, Glutamine amidotransferase, GMPS, GMP synthase, guanosine 5'-monophosphate synthase, MLL/GMPS fusion protein.
GMP synthase [glutamine-hydrolyzing], GMP synthetase, Glutamine amidotransferase, GMPS, GMP synthase, guanosine 5'-monophosphate synthase, MLL/GMPS fusion protein.
Guanosine monophosphate synthetase (GMPS) is an enzyme that plays a crucial role in the de novo synthesis of guanosine monophosphate (GMP) from xanthosine monophosphate (XMP). This enzyme is part of the glutamine amidotransferase (GAT) family and is essential for various cellular processes, including DNA replication, transcription, and translation .
GMPS is a modular enzyme with distinct domains responsible for its catalytic activities. It catalyzes the hydrolysis of glutamine and transfers the generated ammonia to XMP, facilitating the synthesis of GMP. The enzyme’s structure includes an ammonia channel that connects the two catalytic sites, allowing efficient transfer of ammonia .
GMPS is vital for the synthesis of GMP, which is a precursor to guanosine triphosphate (GTP). GTP is essential for numerous cellular functions, including signal transduction, protein synthesis, and cell division. The enzyme’s activity is regulated by allosteric mechanisms, ensuring precise control of GMP synthesis .
The catalytic mechanism of GMPS involves two distinct activities: glutaminolysis and amination. The enzyme’s structure facilitates the coordination of these activities through conformational changes and the ammonia channel. This efficient mechanism ensures the continuous supply of GMP for cellular processes .
The expression and activity of GMPS are tightly regulated to maintain cellular homeostasis. Various factors, including feedback inhibition by GMP and GTP, modulate the enzyme’s activity. Additionally, post-translational modifications and interactions with other proteins contribute to the regulation of GMPS .