3uow: Difference between revisions
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/ | [https://www.uniprot.org/uniprot/GUAA_PLAF7 GUAA_PLAF7] Catalyzes the conversion of xanthine monophosphate (XMP) to GMP in the presence of glutamine and ATP through an adenyl-XMP intermediate, which is the final step of de novo synthesis of GMP (PubMed:17868038, PubMed:21413787, PubMed:26592566, PubMed:32358899). The conversion of XMP to GMP involves the coordinated action of the glutamine amidotransferase (GATase) domain that catalyzes the hydrolysis of the amide side chain of glutamine producing ammonia and the ATP pyrophosphatase (ATPPase) domain that catalyzes the synthesis of adenyl-XMP intermediate from ATP (PubMed:17868038, PubMed:21413787, PubMed:26592566, PubMed:32358899). The ammonia produced by the GATase domain is tunnelled to the ATP-PPase domain where it attacks the adenyl-XMP intermediate generating GMP (PubMed:17868038, PubMed:21413787, PubMed:26592566, PubMed:32358899).<ref>PMID:17868038</ref> <ref>PMID:21413787</ref> <ref>PMID:26592566</ref> <ref>PMID:32358899</ref> | ||
== References == | |||
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</StructureSection> | </StructureSection> | ||
Latest revision as of 13:19, 1 July 2026
Crystal Structure of PF10_0123, a GMP Synthetase from Plasmodium Falciparum
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