IMP cyclohydrolase

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IMP cyclohydrolase
Identifiers
EC no. 3.5.4.10
CAS no. 9013-81-4
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
Search
PMC articles
PubMed articles
NCBI proteins
IMP cyclohydrolase-like protein
PDB 2ntm EBI.jpg
crystal structure of puro from methanothermobacter thermoautotrophicus
Identifiers
SymbolIMP_cyclohyd
Pfam PF07826
InterPro IPR020600
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

In enzymology, an IMP cyclohydrolase (EC 3.5.4.10) is an enzyme that catalyzes the chemical reaction

Contents

IMP + H2O 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. [1]

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. [2]

As of late 2007, 14 structures have been solved for this class of enzymes, with PDB accession codes 1G8M, 1M9N, 1OZ0, 1P4R, 1PKX, 1PL0, 1THZ, 2B1G, 2B1I, 2IU0, 2IU3, 2NTK, 2NTL, and 2NTM.

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References

  1. Graupner M, Xu H, White RH (March 2002). "New class of IMP cyclohydrolases in Methanococcus jannaschii". J. Bacteriol. 184 (5): 1471–3. doi:10.1128/jb.184.5.1471-1473.2002. PMC   134845 . PMID   11844782.
  2. Saridakis V, Christendat D, Thygesen A, Arrowsmith CH, Edwards AM, Pai EF (July 2002). "Crystal structure of Methanobacterium thermoautotrophicum conserved protein MTH1020 reveals an NTN-hydrolase fold". Proteins. 48 (1): 141–3. doi: 10.1002/prot.10147 . PMID   12012346. S2CID   29556936.

Further reading

This article incorporates text from the public domain Pfam and InterPro: IPR020600