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Information on EC 3.5.4.16 - GTP cyclohydrolase I and Organism(s) Thermus thermophilus and UniProt Accession Q5SH52

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EC Tree
IUBMB Comments
The reaction involves hydrolysis of two C-N bonds and isomerization of the pentose unit; the recyclization may be non-enzymic. This enzyme is involved in the de novo synthesis of tetrahydrobiopterin from GTP, with the other enzymes involved being EC 1.1.1.153 (sepiapterin reductase) and EC 4.2.3.12 (6-pyruvoyltetrahydropterin synthase) .
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This record set is specific for:
Thermus thermophilus
UNIPROT: Q5SH52
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Word Map
The taxonomic range for the selected organisms is: Thermus thermophilus
The enzyme appears in selected viruses and cellular organisms
Synonyms
gtp cyclohydrolase i, gtpch, gtp cyclohydrolase, gtp cyclohydrolase 1, gtp-ch, gtp-cyclohydrolase i, gch-1, gtpch1, gtpch i, guanosine triphosphate cyclohydrolase i, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dihydroneopterin triphosphate synthase
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GTP 8-formylhydrolase
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GTP cyclohydrolase
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guanosine triphosphate 8-deformylase
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guanosine triphosphate cyclohydrolase
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hydrolase, guanosine triphosphate cyclo-
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Punch protein
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
GTP + H2O = formate + 7,8-dihydroneopterin 3'-triphosphate
show the reaction diagram
substrate binding and reaction mechanism, transition state structure, modelling, overview
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amidine hydrolysis
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SYSTEMATIC NAME
IUBMB Comments
GTP 7,8-8,9-dihydrolase
The reaction involves hydrolysis of two C-N bonds and isomerization of the pentose unit; the recyclization may be non-enzymic. This enzyme is involved in the de novo synthesis of tetrahydrobiopterin from GTP, with the other enzymes involved being EC 1.1.1.153 (sepiapterin reductase) and EC 4.2.3.12 (6-pyruvoyltetrahydropterin synthase) [3].
CAS REGISTRY NUMBER
COMMENTARY hide
37289-19-3
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
GDP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine diphosphate
show the reaction diagram
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i.e. dihydroneopterin 3'-triphosphate
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?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
show the reaction diagram
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i.e. dihydroneopterin 3'-triphosphate
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
show the reaction diagram
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
the zinc ion is bound by residues Cys108, His111, and Cys179
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8-oxo-dGTP
competitive inhibition
8-oxo-GTP
competitive inhibition, binds tightly to the enzyme with higher affinity than GTP, structure and binding network, overview
ATP
competitive inhibition
dGTP
competitive inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0143
GDP
pH 8.5, 25°C, recombinant enzyme
0.0042
GTP
pH 8.5, 25°C, recombinant enzyme
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0017
GDP
pH 8.5, 25°C, recombinant enzyme
0.0035
GTP
pH 8.5, 25°C, recombinant enzyme
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00022
8-oxo-dGTP
pH 8.5, 25°C, recombinant enzyme
0.0000054
8-oxo-GTP
pH 8.5, 25°C, recombinant enzyme
0.071
ATP
pH 8.5, 25°C, recombinant enzyme
0.02
dGTP
pH 8.5, 25°C, recombinant enzyme
additional information
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified enzyme complexed with 8-oxo-GTP or 8-oxo-dGTP, and as free enzyme, hanging drop vapour diffusion method, 20°C, 0.002 ml of 13.7 mg/ml protein is mixed with 0.002 ml reservoir solution containing 0.1 M HEPES, pH 6.8, 2.0 M ammonium sulfate, 3.4% PEG 400, and 15% glycerol, X-ray diffraction structure determination and analysis at 2.0 and 1.8 A or at 2.2. A resolution, respectively
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain BL21(DE3) by ion exchange chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme expression in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tanaka, Y.; Nakagawa, N.; Kuramitsu, S.; Yokoyama, S.; Masui, R.
Novel reaction mechanism of GTP cyclohydrolase I. High-resolution X-ray crystallography of Thermus thermophilus HB8 enzyme complexed with a transition state analogue, the 8-oxoguanine derivative
J. Biochem.
138
263-275
2005
Thermus thermophilus (Q5SH52), Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579 (Q5SH52)
Manually annotated by BRENDA team