In enzymology, an IMP cyclohydrolase (EC 3.5.4.10) is an enzyme that catalyzes the chemical reaction
IMP + H2O ⇌ {\displaystyle \rightleftharpoons } 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide Thus, the two substrates of this enzyme are IMP and H2O, whereas its product is 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is IMP 1,2-hydrolase (decyclizing). Other names in common use include inosinicase, and inosinate cyclohydrolase. This enzyme catalyses the cyclisation of 5-formylamidoimidazole-4-carboxamide ribonucleotide to IMP, a reaction which is important in de novo purine biosynthesis in archaeal species.
Structural studies In most cases this single-domain protein is arranged to form an overall fold that consists of a four-layered alpha-beta-beta-alpha core structure. The two antiparallel beta-sheets pack against each other and are covered by alpha-helices on one face of the molecule. The protein is structurally similar to members of the N-terminal nucleophile (NTN) hydrolase superfamily. A deep pocket was in fact found on the surface of IMP cyclohydrolase in a position equivalent to that of active sites of NTN-hydrolases, but an N-terminal nucleophile could not be found. Therefore, it is thought that this enzyme is structurally but not functionally similar to members of the NTN-hydrolase family. As of late 2007, 14 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1G8M, PDB: 1M9N, PDB: 1OZ0, PDB: 1P4R, PDB: 1PKX, PDB: 1PL0, PDB: 1THZ, PDB: 2B1G, PDB: 2B1I, PDB: 2IU0, PDB: 2IU3, PDB: 2NTK, PDB: 2NTL, and PDB: 2NTM.
References
Further reading FLAKS JG, ERWIN MJ, BUCHANAN JM (1957). "Biosynthesis of the purines. XVIII 5-Amino-1-ribosyl-4-imidazolecarboxamide 5'-phosphate transformylase and inosinicase". J. Biol. Chem. 229 (2): 603–12. doi:10.1016/S0021-9258(19)63668-9. PMID 13502325.


