GTP cyclohydrolase II | |||||||||
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Identifiers | |||||||||
EC no. | 3.5.4.25 | ||||||||
CAS no. | 56214-35-8 | ||||||||
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 | ||||||||
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In enzymology, a GTP cyclohydrolase II (EC 3.5.4.25) is an enzyme that catalyzes the chemical reaction
- GTP + 3 H2O formate + 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + diphosphate
Thus, the two substrates of this enzyme are GTP and H2O, whereas its 3 products are formate, 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine, and diphosphate.
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 GTP 7,8-8,9-dihydrolase (diphosphate-forming). Other names in common use include guanosine triphosphate cyclohydrolase II, and GTP-8-formylhydrolase. This enzyme participates in riboflavin metabolism.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2BZ0 and 2BZ1.
References
- 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.
Hydrolases: carbon-nitrogen non-peptide (EC 3.5) | |
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3.5.1: Linear amides / Amidohydrolases | |
3.5.2: Cyclic amides/ Amidohydrolases | |
3.5.3: Linear amidines/ Ureohydrolases | |
3.5.4: Cyclic amidines/ Aminohydrolases | |
3.5.5: Nitriles/ Aminohydrolases | |
3.5.99: Other |
Enzymes | |
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Activity | |
Regulation | |
Classification | |
Kinetics | |
Types |
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