3.5.4.25: GTP cyclohydrolase II

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For detailed information about GTP cyclohydrolase II, go to the full flat file.

Reaction

Synonyms

3,4-dihydroxy-2-butanone 4-phosphate synthase, GCH II, GCH II/III, GCH-II, gch2, GCHII, GTP 7,8-8,9-dihydrolase (diphosphate-forming), GTP cyclohydrolase 2, GTP cyclohydrolase II, GTP cyclohydrolase-II, GTP-8-formylhydrolase, GTPCH II, GTPCH-II, guanosine triphosphate cyclohydrolase II, guanosine triphosphate cyclohydrolase II/3,4-dihydroxy-2-butanone-4-phosphate synthase, guanosine-5'-triphosphate cyclohydrolase-II, More, NbRibA, ribA, ribA2, RIBIV, ToxB

ECTree

     3 Hydrolases

         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds

             3.5.4 In cyclic amidines

                3.5.4.25 GTP cyclohydrolase II

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Results	in table
31774	AA Sequence
2	Application
1	CAS Registry Number
8	Cloned(Commentary)
3	Crystallization (Commentary)
15	General Information
12	Inhibitors
2	kcat/KM [mM/s]
1	Ki Value [mM]
39	KM Value [mM]
13	Metals/Ions
10	Molecular Weight [Da]
23	Natural Substrates/ Products (Substrates)
30	Organism
12	Pathway
7	PDB ID
8	pH Optimum
2	pH Range
1	pI Value
32	Protein Variants
8	Purification (Commentary)
5	Reaction
4	Reaction Type
30	Reference
3	Source Tissue
14	Specific Activity [micromol/min/mg]
2	Storage Stability
39	Substrates and Products (Substrate)
3	Subunits
39	Synonyms
1	Systematic Name
5	Temperature Optimum [°C]
1	Temperature Stability [°C]
35	Turnover Number [1/s]

Systematic Name

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Systematic Name on EC 3.5.4.25 - GTP cyclohydrolase II

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SYSTEMATIC NAME

IUBMB Comments

GTP 7,8-8,9-dihydrolase (formate-releasing, phosphate-releasing)

The enzyme, found in prokaryotes and some eukaryotes, hydrolytically cleaves the C-N bond at positions 8 and 9 of GTP guanine, followed by a subsequent hydrolytic attack at the base, which liberates formate, and cleavage of the alpha-beta phosphodiester bond of the triphosphate to form diphosphate. The enzyme continues with a slow cleavage of the diphosphate to form two phosphate ions. The enzyme requires zinc and magnesium ions for the cleavage reactions at the GTP guanine and triphosphate sites, respectively. It is one of the enzymes required for flavin biosynthesis in many bacterial species, lower eukaryotes, and plants. cf. EC 3.5.4.16, GTP cyclohydrolase I, EC 3.5.4.29, GTP cyclohydrolase IIa, and EC 3.5.4.39, GTP cyclohydrolase IV.