Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.5.4.16 extracted from

  • Rebelo, J.; Auerbach, G.; Bader, G.; Bracher, A.; Nar, H.; Hosl, C.; Schramek, N.; Kaiser, J.; Bacher, A.; Huber, R.; Fischer, M.
    Biosynthesis of pteridines. Reaction mechanism of GTP cyclohydrolase I (2003), J. Mol. Biol., 326, 503-516.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
crystallization of purified recombinant enzyme mutants H112S, H113S, and C181S, free, mutant H112S in 0.1 M MES, pH 6.0, 0.2 M sodium acetate, 3 mM sodium azide, or complexed with substrate GTP, mutants H112S and C181S in 0.1 M MOPS, pH 7.0, 10% w/v PEG 6000, 0.1 M ammonium sulfate, or mutant H113S in 0.1 M Tris-HCl, pH 8.5, 0.2 M (NH4)H2PO4, 50% v/v 2-methyl-2,4-pentanediol, addition of GTP for the complex formation, hanging drop vapour diffusion method at room temperature, X-ray diffraction structure determination and analysis at about 2.1-3.2 A resolution, modeling Escherichia coli

Protein Variants

Protein Variants Comment Organism
C110S highly reduced activity in both reaction steps using GTP or 2-amino-5-formylamino-6-ribofuranosylamino-4(3H)-pyrimidinone triphosphate as substrate, reduced zinc content compared to the wild-type enzyme Escherichia coli
C181S determination of crystal structure, highly reduced activity in both reaction steps using GTP or 2-amino-5-formylamino-6-ribofuranosylamino-4(3H)-pyrimidinone triphosphate as substrate, reduced zinc content compared to the wild-type enzyme Escherichia coli
H112S determination of crystal structure, highly reduced activity in both reaction steps using GTP or 2-amino-5-formylamino-6-ribofuranosylamino-4(3H)-pyrimidinone triphosphate as substrate, reduced zinc content compared to the wild-type enzyme Escherichia coli
H113S determination of crystal structure, highly reduced activity in both reaction steps using GTP or 2-amino-5-formylamino-6-ribofuranosylamino-4(3H)-pyrimidinone triphosphate as substrate, reduced zinc content compared to the wild-type enzyme Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ required, wild-type enzyme contains 0.9 mol of Zn2+ per mol of enzyme subunit, while the zinc content of the mutant enzymes is reduced to below 0.2 Zn2+ per mol of enzyme subunit Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
GTP + H2O Escherichia coli
-
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A6T5
-
-

Reaction

Reaction Comment Organism Reaction ID
GTP + H2O = formate + 7,8-dihydroneopterin 3'-triphosphate reaction mechanism, active site structure, GTP binding strcuture Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.0001
-
below, mutant enzymes, substrate 2-amino-5-formylamino-6-ribofuranosylamino-4(3H)-pyrimidinone triphosphate Escherichia coli
0.0001
-
below, mutant enzymes, substrate GTP Escherichia coli
0.088
-
wild-type enzyme, substrate 2-amino-5-formylamino-6-ribofuranosylamino-4(3H)-pyrimidinone triphosphate Escherichia coli
0.091
-
wild-type enzyme, substrate GTP Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-amino-5-formylamino-6-ribofuranosylamino-4(3H)-pyrimidinone triphosphate + H2O substrate is the reaction intermediate of the overall reaction Escherichia coli formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
?
GTP + H2O
-
Escherichia coli formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
?
GTP + H2O cyclization to dihydroneopterin triphosphate Escherichia coli formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate i.e. dihydroneopterin triphosphate ?