GTP cyclohydrolase II

GTP cyclohydrolase II
Identifiers
EC no.3.5.4.25
CAS no.56214-35-8
Databases
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
Rheareactions
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

GTP cyclohydrolase II (EC 3.5.4.25) is an enzyme characterised from Escherichia coli that catalyzes the hydrolysis of guanosine triphosphate to give 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine (1), formic acid, and orthophosphoric acid (Pi):

2D representation of the chemical structure of guanosine triphosphate.
guanosine triphosphate
 
4 H2O
Rightward reaction arrow with minor substrate(s) from top left and minor product(s) to top right
 
 
 
2D representation of the chemical structure of 2,5-Diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine.
(1)
+ 2 Pi
 

This enzyme is a hydrolase, one acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is GTP 7,8-8,9-dihydrolase (diphosphate-forming). Other names in use include guanosine triphosphate cyclohydrolase II, and GTP-8-formylhydrolase. The reaction is part of riboflavin biosynthesis.

Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes PDB: 2BZ0​ and PDB: 2BZ1​.

References

  1. ↑ Foor F, Brown GM (1975). "Purification and properties of guanosine triphosphate cyclohydrolase II from Escherichia coli". J. Biol. Chem. 250 (9): 3545–51. doi:10.1016/S0021-9258(19)41549-4. PMID 235552.
  2. ↑ Enzyme 3.5.4.25 at KEGG Pathway Database.
  3. ↑ Liu, Shuang; Hu, Wenya; Wang, Zhiwen; Chen, Tao (2020). "Production of riboflavin and related cofactors by biotechnological processes". Microbial Cell Factories. 19 (1) 31. doi:10.1186/s12934-020-01302-7. PMC 7017516. PMID 32054466.