This enzyme belongs to the family of ligases, specifically the cyclo-ligases, which form carbon-nitrogen bonds. The systematic name of this enzyme class is 5-formyltetrahydrofolate cyclo-ligase (ADP-forming). Other names in common use include 5,10-methenyltetrahydrofolate synthetase (MTHFS), formyltetrahydrofolic cyclodehydrase, and 5-formyltetrahydrofolate cyclodehydrase. This enzyme participates in one carbon pool by folate.
Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1SBQ, 1SOU, 1U3F, 1U3G, and 2JCB.
Substrate-level phosphorylation is a metabolism reaction that results in the production of ATP or GTP supported by the energy released from another high-energy bond that leads to phosphorylation of ADP or GDP to ATP or GTP (note that the reaction catalyzed by creatine kinase is not considered as "substrate-level phosphorylation"). This process uses some of the released chemical energy, the Gibbs free energy, to transfer a phosphoryl (PO3) group to ADP or GDP. Occurs in glycolysis and in the citric acid cycle.
Phosphoribosylformylglycinamidine cyclo-ligase is the fifth enzyme in the de novo synthesis of purine nucleotides. It catalyzes the reaction to form 5-aminoimidazole ribotide (AIR) from formylglycinamidine-ribonucleotide FGAM. This reaction closes the ring and produces a 5-membered imidazole ring of the purine nucleus (AIR):
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In enzymology, a UDP-N-acetylmuramoyl-L-alanine—D-glutamate ligase is an enzyme that catalyzes the chemical reaction
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References
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
Greenberg DM, Wynston LK, Nagabhushanan A (1965). "Further studies on N5-formyltetrahydrofolic acid cyclodehydrase". Biochemistry. 4 (9): 1872–1878. doi:10.1021/bi00885a026.
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