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Information on EC 3.5.4.25 - GTP cyclohydrolase II
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3.5.4.25 GTP cyclohydrolase IIIUBMB Comments
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.
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Word Map
- 3.5.4.25
- riboflavin
-
anti-hcv
- lumazine
- guilliermondii
- famata
-
gtp-cyclohydrolase
-
2,5-diamino-6-ribosylamino-43h-pyrimidinone
-
flavinogenic
- 6,7-dimethyl-8-ribityllumazine
- pharmacology
- synthesis
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
gtp cyclohydrolase ii, riba2, 3,4-dihydroxy-2-butanone 4-phosphate synthase, gchii, gch ii, gtp cyclohydrolase 2, nbriba, gch-ii, gtp cyclohydrolase-ii, guanosine triphosphate cyclohydrolase ii, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
GCH II
GCH II/III
-
enzyme variant SCO 6655 shares features of GCH II and GCH III
GCHII
GTP 7,8-8,9-dihydrolase (diphosphate-forming)
-
-
-
-
GTP-8-formylhydrolase
guanosine triphosphate cyclohydrolase II
guanosine triphosphate cyclohydrolase II/3,4-dihydroxy-2-butanone-4-phosphate synthase
-
ribA
ribA2
RIBIV
-
-
-
-
ToxB
GTP-8-formylhydrolase
-
-
-
-
guanosine triphosphate cyclohydrolase II
-
-
-
-
ribA
-
-
-
-
ribA2
bifunctional enzyme with 3,4-dihydroxy-2-butanone 4-phosphate synthase and GTP cyclohydrolase II activities
ribA2
bifunctional enzyme with 3,4-dihydroxy-2-butanone 4-phosphate synthase and GTP cyclohydrolase II activities
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
GTP + 4 H2O = formate + 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + 2 phosphate
GTP + 4 H2O = formate + 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + 2 phosphate
-
-
-
-
GTP + 4 H2O = formate + 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + 2 phosphate
reaction mechanism
-
GTP + 4 H2O = formate + 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + 2 phosphate
2 C-N bonds are hydrolysed, releasing formate, with simultaneous removal of the terminal diphosphate, reaction mechanism
-
GTP + 4 H2O = formate + 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + 2 phosphate
ordered reaction mechanism, in which the hydrolytic release of diphosphate preceeds the hydrolytic attack of the imidazole ring, ring opening and formate release are dependent on zinc bound to the active site, overview
-
GTP + 4 H2O = formate + 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + 2 phosphate
RibA is a bifunctional enzyme possessing 3,4-dihydroxy-2-butanone 4-phosphate synthase activity, EC 4.1.99.12, located in the N-terminal half of the protein and GTP cyclohydrolase II activity of the C-terminal domain, overview
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of C-N bonds
hydrolysis of phosphoesters
-
-
-
-
hydrolysis of C-N bonds
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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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.
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CAS REGISTRY NUMBER
COMMENTARY
56214-35-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone triphosphate + 2 H2O
formate + 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate + diphosphate
2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone triphosphate + H2O
2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate + diphosphate
-
formamide-type intermediate analogue
-
-
?
dGTP + H2O
formate + 2,5-diamino-6-hydroxy-4-(5-phospho-deoxyribosylamino)pyrimidine + diphosphate
-
-
-
-
?
GTP + 3 H2O
formate + 2,5-diamino-6-beta-ribosylamino-4(3H)-pyrimidinone 5'-phosphate + diphosphate
GTP + 3 H2O
formate + 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + diphosphate
GTP + H2O
2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate + diphosphate + ?
enzyme catalyzes the first step in the biosynthesis of riboflavin
-
-
?
GTP + H2O
2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate + diphosphate + ?
GTP + H2O
formate + 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + diphosphate
GTP + H2O
formate + 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + diphosphate
GTP + H2O
formate + 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + diphosphate
GTP + H2O
formate + 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate + diphosphate
2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-triphosphate + H2O
?
-
-
-
-
?
2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-triphosphate + H2O
?
-
-
-
?
2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone triphosphate + 2 H2O
formate + 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate + diphosphate
-
compound does serve as a substrate but not as kinetically competent intermediate
-
-
?
2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone triphosphate + 2 H2O
formate + 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate + diphosphate
-
formamide-type intermediate analogue
-
-
?
GTP + 3 H2O
formate + 2,5-diamino-6-beta-ribosylamino-4(3H)-pyrimidinone 5'-phosphate + diphosphate
-
-
spontaneous isomerization into the alpha-isomer, also the product can easily spontaneously decompose under formation of 2,4,5-triamino-4-(3H)-pyrimidone
-
?
GTP + 3 H2O
formate + 2,5-diamino-6-beta-ribosylamino-4(3H)-pyrimidinone 5'-phosphate + diphosphate
-
first committed step in the biosynthesis of riboflavin, overview
-
-
?
GTP + 3 H2O
formate + 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + diphosphate
-
-
-
?
GTP + 3 H2O
formate + 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + diphosphate
-
-
-
?
GTP + H2O
2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate + diphosphate + ?
-
-
-
?
GTP + H2O
2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate + diphosphate + ?
-
-
the reaction product is exclusively formed by enzyme variant SCO 6655
-
?
GTP + H2O
formate + 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + diphosphate
-
GMP is a second reaction product of GTP cyclohydrolase II. The ratio of the main product, 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine and GMP is produced at an approximate ratio of 10:1
-
?
GTP + H2O
formate + 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + diphosphate
-
-
-
?
GTP + H2O
formate + 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + diphosphate
-
-
-
?
GTP + H2O
formate + 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + diphosphate
-
-
-
-
?
GTP + H2O
formate + 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + diphosphate
-
-
-
-
?
GTP + H2O
formate + 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + diphosphate
-
-
-
-
?
GTP + H2O
formate + 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + diphosphate
-
-
-
-
?
GTP + H2O
formate + 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + diphosphate
-
-
-
-
?
GTP + H2O
formate + 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + diphosphate
-
-
-
?
GTP + H2O
formate + 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + diphosphate
-
-
-
?
GTP + H2O
formate + 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + diphosphate
-
-
-
-
?
GTP + H2O
formate + 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + diphosphate
-
first committed step in the biosynthesis of riboflavin, overview
-
-
?
GTP + H2O
formate + 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate + diphosphate
-
-
GMP is also formed as a minor product
-
?
GTP + H2O
formate + 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate + diphosphate
-
first committed step in the biosynthesis of riboflavin, overview
-
-
?
GTP + H2O
formate + 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate + diphosphate
-
-
-
-
?
additional information
?
-
-
RibA is the rate limiting enzyme in an industrial riboflavin producing strain
-
-
?
additional information
?
-
-
RibA is a bifunctional enzyme possessing 3,4-dihydroxy-2-butanone 4-phosphate synthase activity, EC 4.1.99.12, located in the N-terminal half of the protein and GTP cyclohydrolase II activity of the C-terminal domain, overview
-
-
?
additional information
?
-
GTP cyclohydrolase II is a slow GTPase
-
-
?
additional information
?
-
enzyme may be involved in the biosynthesis of toxoflavin, which is produced from GTP in a series of steps that are likely initiated by GCH II
-
-
?
additional information
?
-
enzyme may be involved in the biosynthesis of toxoflavin, which is produced from GTP in a series of steps that are likely initiated by GCH II
-
-
?
additional information
?
-
enzyme may be involved in the biosynthesis of toxoflavin, which is produced from GTP in a series of steps that are likely initiated by GCH II
-
-
?
additional information
?
-
-
enzyme may be involved in the biosynthesis of toxoflavin, which is produced from GTP in a series of steps that are likely initiated by GCH II
-
-
?
additional information
?
-
substitution of Met with His leads to a protein that catalyzes the production of both 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate and 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate with equal efficiency
-
-
?
additional information
?
-
substitution of Met with His leads to a protein that catalyzes the production of both 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate and 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate with equal efficiency
-
-
?
additional information
?
-
substitution of Met with His leads to a protein that catalyzes the production of both 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate and 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate with equal efficiency
-
-
?
additional information
?
-
-
substitution of Met with His leads to a protein that catalyzes the production of both 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate and 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate with equal efficiency
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GTP + 3 H2O
formate + 2,5-diamino-6-beta-ribosylamino-4(3H)-pyrimidinone 5'-phosphate + diphosphate
-
first committed step in the biosynthesis of riboflavin, overview
-
-
?
GTP + 3 H2O
formate + 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + diphosphate
GTP + H2O
2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate + diphosphate + ?
enzyme catalyzes the first step in the biosynthesis of riboflavin
-
-
?
GTP + H2O
2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate + diphosphate + ?
-
-
-
?
GTP + H2O
formate + 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + diphosphate
GTP + H2O
formate + 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + diphosphate
GTP + H2O
formate + 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + diphosphate
GTP + H2O
formate + 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate + diphosphate
-
first committed step in the biosynthesis of riboflavin, overview
-
-
?
GTP + 3 H2O
formate + 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + diphosphate
-
-
-
?
GTP + 3 H2O
formate + 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + diphosphate
-
-
-
?
GTP + H2O
formate + 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + diphosphate
-
GMP is a second reaction product of GTP cyclohydrolase II. The ratio of the main product, 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine and GMP is produced at an approximate ratio of 10:1
-
?
GTP + H2O
formate + 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + diphosphate
-
-
-
?
GTP + H2O
formate + 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + diphosphate
-
-
-
?
GTP + H2O
formate + 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + diphosphate
-
-
-
-
?
GTP + H2O
formate + 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + diphosphate
-
-
-
-
?
GTP + H2O
formate + 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + diphosphate
-
-
-
-
?
GTP + H2O
formate + 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + diphosphate
-
-
-
-
?
GTP + H2O
formate + 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + diphosphate
-
-
-
-
?
GTP + H2O
formate + 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + diphosphate
-
first committed step in the biosynthesis of riboflavin, overview
-
-
?
additional information
?
-
-
RibA is the rate limiting enzyme in an industrial riboflavin producing strain
-
-
?
additional information
?
-
GTP cyclohydrolase II is a slow GTPase
-
-
?
additional information
?
-
enzyme may be involved in the biosynthesis of toxoflavin, which is produced from GTP in a series of steps that are likely initiated by GCH II
-
-
?
additional information
?
-
enzyme may be involved in the biosynthesis of toxoflavin, which is produced from GTP in a series of steps that are likely initiated by GCH II
-
-
?
additional information
?
-
enzyme may be involved in the biosynthesis of toxoflavin, which is produced from GTP in a series of steps that are likely initiated by GCH II
-
-
?
additional information
?
-
-
enzyme may be involved in the biosynthesis of toxoflavin, which is produced from GTP in a series of steps that are likely initiated by GCH II
-
-
?
additional information
?
-
substitution of Met with His leads to a protein that catalyzes the production of both 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate and 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate with equal efficiency
-
-
?
additional information
?
-
substitution of Met with His leads to a protein that catalyzes the production of both 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate and 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate with equal efficiency
-
-
?
additional information
?
-
substitution of Met with His leads to a protein that catalyzes the production of both 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate and 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate with equal efficiency
-
-
?
additional information
?
-
-
substitution of Met with His leads to a protein that catalyzes the production of both 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate and 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate with equal efficiency
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Zn2+
Zn2+
-
wild-type enzyme contains 0.71 mol Zn2+ per mol of subunit, while the content in the mutant enzymes is reduced to below 0.1 mol Zn2+ per mol of subunit, essential for activity, bound to the active site, required for ring opening and formate release with zinc acting as a Lewis acid, which activates the 2 water molecules involved in the sequential hydrolysis of 2 carbon-nitrogen bonds
Zn2+
content 1 molecule per monomer enzyme, enzyme requires a zinc ion which presumably activates a water molecule for excision of C-8 of GTP
Zn2+
content of 1 molecule per enzyme monomer, enzyme requires a zinc ion which presumably activates a water molecule for excision of C-8 of GTP
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phosphate
-
partial uncompetitive at low concentration, competitive at concentrations above 6 mM
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Tuberculosis
Structural basis for pH dependent monomer-dimer transition of 3,4-dihydroxy 2-butanone-4-phosphate synthase domain from Mycobacterium tuberculosis.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.031
2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-triphosphate
-
wild type enzyme, at pH 8.5 and 30°C
0.079
2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-triphosphate
-
mutant enzyme Y210C/A290T/Q293R/A296T/K322R/M361I, at pH 8.5 and 30°C
0.122
2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-triphosphate
-
mutant enzyme Y210C/A290T/Q293R/A296T/K322R/F339Y/M361I, at pH 8.5 and 30°C
0.008
GTP
M120Y variant, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
0.008
GTP
variant M120Y, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
0.0089
GTP
M120K variant, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
0.011
GTP
M120Q variant, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
0.015
GTP
M120I variant, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
0.019
GTP
M120F variant, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
0.019
GTP
variant M120F, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
0.024
GTP
wild type, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
0.033
GTP
M120S variant, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
0.044
GTP
-
mutant enzyme Y210C/A290T/Q293R/A296T/K322R/F339Y/M361I, at pH 8.5 and 30°C
0.048
GTP
variant Y123M, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
0.049
GTP
-
mutant enzyme Y210C/A290T/Q293R/A296T/K322R/M361I, at pH 8.5 and 30°C
0.05
GTP
M120H variant, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
0.056
GTP
wild type, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
0.059
GTP
M120A variant, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
0.063
GTP
wild type, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
0.067
GTP
M120C variant, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
0.067
GTP
M120N variant, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
0.085
GTP
variant D127A, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
0.092
GTP
variant R123M, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
0.1267
GTP
full-length bifunctional enzyme ribA2, at pH 8.0 and 37°C
0.15
GTP
M120T variant, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
0.1505
GTP
GCHII-domain of enzyme ribA2, at pH 8.0 and 37°C
0.19
GTP
M120G variant, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
0.23
GTP
variant G209D, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
additional information
additional information
-
kinetics, cooperative reaction with a Hill coefficient of 1.3
-
additional information
additional information
-
pre-steady state kinetics, single turnover experiments, stopped-flow experiments
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.05
2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-triphosphate
-
wild type enzyme, at pH 8.5 and 30°C
0.09
2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-triphosphate
-
mutant enzyme Y210C/A290T/Q293R/A296T/K322R/M361I, at pH 8.5 and 30°C
0.1
2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-triphosphate
-
mutant enzyme Y210C/A290T/Q293R/A296T/K322R/F339Y/M361I, at pH 8.5 and 30°C
0.0033
GTP
full-length bifunctional enzyme ribA2, at pH 8.0 and 37°C
0.065
GTP
-
mutant enzyme Y210C/A290T/Q293R/A296T/K322R/M361I, at pH 8.5 and 30°C
0.072
GTP
-
mutant enzyme Y210C/A290T/Q293R/A296T/K322R/F339Y/M361I, at pH 8.5 and 30°C
0.42
GTP
M120D variant, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
1.2
GTP
variant Y326F, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
1.8
GTP
M120W variant, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
3.18
GTP
M120E variant, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
3.18
GTP
SCO 2687, variant Y123F, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
4.86
GTP
variant Y326M, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
10.8
GTP
M120H variant, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
20.4
GTP
M120T variant, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
42
GTP
M120A variant, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
46.8
GTP
variant M120F, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
57
GTP
M120G variant, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
66
GTP
M120C variant, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
78
GTP
M120I variant, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
78
GTP
SCO 2687, variant D127A, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
84
GTP
M120S variant, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
84
GTP
variant M120Y, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
108
GTP
M120N variant, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
120
GTP
M120Q variant, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
150
GTP
wild type, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
168
GTP
SCO 2687, variant G209D, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
204
GTP
SCO 2687, wild type, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
228
GTP
SCO 2687, variant R123M, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
348
GTP
SCO 2687, variant Y123M, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
432
GTP
wild type, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.4
GTP
full-length bifunctional enzyme ribA2, at pH 8.0 and 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.015
-
purified recombinant wild-type enzyme, substrate 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone triphosphate cleaved to 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate
0.025
-
purified recombinant wild-type enzyme, substrate dGTP cleaved to dGMP
0.038
-
purified recombinant wild-type enzyme, substrate dGTP cleaved to 2,5-diamino-6-hydroxy-4-(5-phospho-deoxyribosylamino)pyrimidine