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Information on EC 3.5.4.16 - GTP cyclohydrolase I
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3.5.4.16 GTP cyclohydrolase IIUBMB 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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Word Map
- 3.5.4.16
- tetrahydrobiopterin
- bh4
- endothelial
- dystonia
- hydroxylase
-
dopa-responsive
- dopamine
- sepiapterin
- biopterin
- parkinsonism
- pterins
- pteridine
- catecholamine
- dihydrofolate
- serotonin
-
segawa
- interferon-gamma
-
neurotransmitter
- 2,4-diamino-6-hydroxypyrimidine
- folate
- levodopa
- l-dopa
- ptp
- dihydropteridine
-
dopaminergic
-
diurnal
-
nigrostriatal
-
endothelium-dependent
- striatum
- dahp
- phenylketonuria
- hyperphenylalaninemia
-
cytokine-stimulated
- nutrition
- dihydropteroate
-
ido
- n-acetylserotonin
-
6r-l-erythro-5,6,7,8-tetrahydrobiopterin
- 7,8-dihydrobiopterin
- 6-pyruvoyl-tetrahydropterin
- dihydrobiopterin
- molecular biology
- indoleamine
- tetrahydropterin
- biotechnology
- medicine
-
catecholaminergic
The enzyme appears in viruses and cellular organisms
Synonyms
dihydroneopterin triphosphate synthase, FelE, folE, GCH, GCH-1, GCH1, GCHI, GCYH-IA, GCYH-IB, GTP 8-formylhydrolase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dihydroneopterin triphosphate synthase
-
-
-
-
FelE
folE
GCH
GCH1
GCHI
GCYH-IA
GCYH-IB
GTP 8-formylhydrolase
-
-
-
-
GTP cyclohydrolase
-
-
-
-
GTP cyclohydrolase 1
GTP cyclohydrolase I
GTP cyclohydrolase IB
GTP-CH-I
GTP-CH1
GTP-cyclohydrolase 1
GTP-cyclohydrolase I
GTPCH
GTPCH I
GTPCH1
GTPCHI
guanosine 5'-triphosphate-cyclohydrolase I
guanosine triphosphate 8-deformylase
-
-
-
-
guanosine triphosphate cyclohydrolase
-
-
-
-
guanosine triphosphate cyclohydrolase 1
guanosine triphosphate cyclohydrolase I
hydrolase, guanosine triphosphate cyclo-
-
-
-
-
MptA
Punch protein
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
GTP + H2O = formate + 7,8-dihydroneopterin 3'-triphosphate
-
-
-
-
GTP + H2O = formate + 7,8-dihydroneopterin 3'-triphosphate
the reaction involves hydrolysis of two C-N bonds and isomerization of the pentose unit, the recyclization may be non-enzymatic
-
-
-
GTP + H2O = formate + 7,8-dihydroneopterin 3'-triphosphate
allosteric regulation mechanism, active site structure
-
GTP + H2O = formate + 7,8-dihydroneopterin 3'-triphosphate
enzyme contains to thiol groups per active site, reaction mechanism
-
GTP + H2O = formate + 7,8-dihydroneopterin 3'-triphosphate
reaction and regulation mechanism, enzyme forms a stimulatory complex with the GTP cyclohydrolase I feedback regulatory protein, i.e. GFRP
-
GTP + H2O = formate + 7,8-dihydroneopterin 3'-triphosphate
reaction mechanism involving reaction intermediates
-
GTP + H2O = formate + 7,8-dihydroneopterin 3'-triphosphate
reaction mechanism, active site structure, GTP binding strcuture
GTP + H2O = formate + 7,8-dihydroneopterin 3'-triphosphate
reaction mechanism, six consecutive unimolecular reaction steps, the first of which being reversible
-
GTP + H2O = formate + 7,8-dihydroneopterin 3'-triphosphate
The reaction involves hydrolysis of two C-N bonds and isomerization of the pentose unit, the recyclization may be non-enzymic, reaction mechanism
GTP + H2O = formate + 7,8-dihydroneopterin 3'-triphosphate
substrate binding and reaction mechanism, transition state structure, modelling, overview
GTP + H2O = formate + 7,8-dihydroneopterin 3'-triphosphate
substrate binding and reaction mechanism, transition state structure, modelling, overview
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amidine hydrolysis
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
MetaCyc
6-hydroxymethyl-dihydropterin diphosphate biosynthesis I, 6-hydroxymethyl-dihydropterin diphosphate biosynthesis IV (Plasmodium), drosopterin and aurodrosopterin biosynthesis, erythro-tetrahydrobiopterin biosynthesis I, preQ0 biosynthesis, tetrahydromonapterin biosynthesis, threo-tetrahydrobiopterin biosynthesis
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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].
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CAS REGISTRY NUMBER
COMMENTARY
37289-19-3
-
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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-ribofuranosylamino-4(3H)-pyrimidinone triphosphate + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
substrate is the reaction intermediate of the overall reaction
-
-
?
beta,gamma-methyleneguanosine 5'-triphosphate + H2O
dihydroneopterin 2',3'-cyclic phosphate + ?
beta-gamma-methyleneguanosine 5'-triphosphate + H2O
beta-gamma-methylene-7,8-dihydroneopterin 3'-triphosphate + formate
-
-
-
?
GDP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine diphosphate
GTP + H2O
2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone triphosphate + ?
-
mutant H179N is not able to perform the whole reaction step
-
-
r
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
GTP + H2O
formate + 7,8-dihydro-D-neopterin 2',3'-cyclic phosphate + diphosphate
-
-
-
-
?
guanosine 5'-[gamma-thio]triphosphate + H2O
dihydroneopterin 2',3'-cyclic phosphate + ?
-
-
-
-
?
beta,gamma-methyleneguanosine 5'-triphosphate + H2O
dihydroneopterin 2',3'-cyclic phosphate + ?
-
-
-
-
?
beta,gamma-methyleneguanosine 5'-triphosphate + H2O
dihydroneopterin 2',3'-cyclic phosphate + ?
-
-
-
-
?
GDP + H2O
dihydroneopterin 2',3'-cyclic phosphate + ?
-
-
-
-
?
GDP + H2O
dihydroneopterin 2',3'-cyclic phosphate + ?
-
-
-
-
?
GDP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine diphosphate
-
i.e. dihydroneopterin 3'-triphosphate
-
?
GDP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine diphosphate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
i.e. dihydroneopterin 3'-triphosphate
-
?
GTP + H2O
dihydroneopterin triphosphate + formate
-
first step in the biosynthesis of pteridine coenzymes, such as folic acid and tetrahydrobiopterin
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
Q8S3C2
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
Q8S3C2
the enzyme mediates the first and committing step pf the pterin branch of the folate-synthesis pathway
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
Q8S3C2
the enzyme mediates the first and committing step of the pterin branch of the folate-synthesis pathway
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
cyclization to dihydroneopterin triphosphate
i.e. dihydroneopterin triphosphate
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
first step in the biosynthesis pathway leading to dihydrofolate and tetrahydrobiopterin
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
rate-limiting enzyme in the biosynthesis of tetrahydrobiopterin, important in the regulation of monoamine neurotransmitters such a s dopamine, norepinephrine, and serotonin
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
substrate needs to be Mg2+-free
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
the enzyme is rate limiting in the tetrahydrobiopterin biosynthesis in adipose tissue, overview
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
the enzyme synthesizes the cofactor for the reaction of the phenylalanine hydroxylase
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
first committed step in the biosynthesis of tetrahydrofolate and tetrahydrobiopterin
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
complex series of reaction steps
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
first committed step in the biosynthesis of tetrahydrofolate and tetrahydrobiopterin
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
complex series of reaction steps
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
the enzyme produces the cofactor tetrahydrobiopterin essential for activities of tyrosine hydroxylase and DOPA decarboxylase
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
rate-limiting step in the biosynthesis of tetrahydrobiopterin, a key factor necessary for nitric oxide synthase, and for the hydrolxylases that are involved in the production of catecholamines and serotonin
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
estrogens play a regulatory role on the enzyme expression, the enzyme is involved in estrogen receptor interaction with cyclic AMP, role of receptor subtypes, overview
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
the enzyme controls the biosynthesis pathway of tetrahydrobiopterin, which is a necessary cofactor for inducible nitric oxide synthase
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
the enzyme is feedback regulated by the GTPCH feedback regulatory protein GFRP, overview
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
Serratia indica
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
Serratia indica
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
Serratia indica
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
Serratia indica
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
the enzyme mediates the first and committing step of the pterin branch of the folate-synthesis pathway
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
i.e. dihydroneopterin 3'-triphosphate
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
i.e. dihydroneopterin 3'-triphosphate
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
-
first step in pathway of pterins
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
-
first step in pathway of pterins
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
-
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
-
first step in pathway of pterins
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
-
first step in pathway of pterins
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
-
first step in pathway of pterins
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
-
first step in pathway of pterins
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
-
first step in pathway of pterins
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
-
first step in pathway of pterins
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
-
first step in biosynthesis of tetrahydrobiopterin, BH4
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
-
first step in pathway of pterins
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
-
first step in pathway of pterins
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
-
first step in pathway of pterins
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
-
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
-
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
-
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
-
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
-
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
-
first step in pathway of pterins
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
-
first step in pathway of pterins
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
Serratia indica
-
first step in pathway of pterins
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
Serratia indica
-
first step in pathway of pterins
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
Serratia indica
-
first step in pathway of pterins
-
?
GTP + H2O
formate + 7,8-dihydroneopterin 3'-triphosphate
-
-
-
?
GTP + H2O
formate + 7,8-dihydroneopterin 3'-triphosphate
-
-
-
?
GTP + H2O
formate + 7,8-dihydroneopterin 3'-triphosphate
-
-
-
?
GTP + H2O
formate + 7,8-dihydroneopterin 3'-triphosphate
-
-
-
?
GTP + H2O
formate + 7,8-dihydroneopterin 3'-triphosphate
-
-
-
?
GTP + H2O
formate + D-erythro-dihydroneopterin triphosphate
-
first commited step in the biosynthesis of tetrahydrofolate and tetrahydrobiopterin
-
-
?
GTP + H2O
formate + D-erythro-dihydroneopterin triphosphate
-
enzyme catalyzed opening of the imidazole ring of GTP, kinetically competent reaction intermediate is 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone
-
-
?
GTP + H2O
formate + D-erythro-dihydroneopterin triphosphate
-
-
-
-
?
GTP + H2O
formate + D-erythro-dihydroneopterin triphosphate
-
first step of the biosynthesis of (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin, i.e. BH4
-
-
?
additional information
?
-
-
GTPCH1 via tetrahydrobiopterin maintains normal blood pressure and endothelial function in vivo by preserving nitric oxide synthesis by endothelial NO synthase
-
-
?
additional information
?
-
-
GTP cyclohydrolase I stimulates tyrosine hydroxylase activity by increasing the maximal velocity of the enzyme and fails to block the feedback inhibition of tyrosine hydroxylase by dopamine
-
-
?
additional information
?
-
-
GCYH-I is not only the first enzyme of the tetrahydrofolate and tetrahydropterin pathways, but also the first enzyme of queuosine and archaeosine biosynthesis
-
-
?
additional information
?
-
-
GCYH-I is not only the first enzyme of the tetrahydrofolate and tetrahydropterin pathways, but also the first enzyme of queuosine and archaeosine biosynthesis
-
-
?
additional information
?
-
-
GTPCH I is the rate-limiting enzyme for de novo tetrahydrobiopterin synthesis
-
-
?
additional information
?
-
-
catalyzes the first step in the biosynthesis of methanopterin
-
-
?
additional information
?
-
-
no activity towards dGTP, ATP, GMP, ITP, fapy-GTP, or 7-methyl-GTP
-
-
?
additional information
?
-
-
catalyzes the first step in the biosynthesis of methanopterin
-
-
?
additional information
?
-
-
no activity towards dGTP, ATP, GMP, ITP, fapy-GTP, or 7-methyl-GTP
-
-
?
additional information
?
-
-
GTPCH1 via tetrahydrobiopterin maintains normal blood pressure and endothelial function in vivo by preserving nitric oxide synthesis by endothelial NO synthase
-
-
?
additional information
?
-
-
tetrahydrobiopterin production by GTPCH I occurs in close proximity to endothelial nitric oxide synthase
-
-
?
additional information
?
-
-
isozyme GTPCHIa activity is involved in formation of the black markings on the larva during fourth ecdysis, pigmentation pathway overview
-
-
?
additional information
?
-
-
enzyme deficiency causes hyperphenylalaninemia with severe neurological disorders, the 3,4-dihydroxyphenylalanine, i.e. DOPA, responsive form of dystonia, and endothelial dysfunction, all by (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin depletion, the GTP cyclohydrolase I feedback regulatory protein GFRP binds to the enzyme and mediates the regulation of the enzyme by L-phenylalanine and (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin
-
-
?
additional information
?
-
-
tetrahydrobiopterin, the cofactor required for hydroxylation of aromatic amino acids, regulates its own synthesis through feedback inhibition of the enzyme mediated by the regulatory subunit called GTP cyclohydrolase I feedback regulatory protein, i.e. GFRP
-
-
?
additional information
?
-
-
enzyme is complexed with the GTP cyclohydrolase I feedback regulatory protein, i.e. GFRP, in a ratio of 1:2, complex formation is induced by phenylalanine and (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin
-
-
?
additional information
?
-
-
enzyme is complexed with the GTP cyclohydrolase I feedback regulatory protein, i.e. GFRP, in a ratio of 1:2, complex formation is induced by phenylalanine and (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin, i.e. BH4
-
-
?
additional information
?
-
-
GCH-1 interacts with many signal transduction proteins such as receptors (NKG2-A/B-actvating NK receptor and latrophilin-2), kinase (Death-associated protein kinase 3), adaptors (Rho-GTPase-activating protein 7 and Rho-guanine nucleotide exchange factor 3) and transcriptional factors (ATF-6 alpha and interferon regulatory factor 1)
-
-
?
additional information
?
-
-
GCH1 interacts with GCH1 interacts with GTP cyclohydrolase I feedback regulatory protein, GFRP, and very long-chain specific acyl-CoA dehydrogenase in the liver, tubulin beta-2A chain in the liver and brain, DnaJ homolog subfamily A member 1 and fatty aldehyde dehydrogenase in the liver, heart and kidney and eukaryotic translation initiation factor 3 subunit I in all organs tested, overview. GCH1 associates with mitochondrial proteins and interacts with VLCAD, a mitochondrial protein
-
-
?
additional information
?
-
-
GCH1 interacts with GCH1 interacts with GTP cyclohydrolase I feedback regulatory protein, GFRP, and very long-chain specific acyl-CoA dehydrogenase in the liver, tubulin beta-2A chain in the liver and brain, DnaJ homolog subfamily A member 1 and fatty aldehyde dehydrogenase in the liver, heart and kidney and eukaryotic translation initiation factor 3 subunit I in all organs tested, overview. GCH1 associates with mitochondrial proteins and interacts with VLCAD, a mitochondrial protein
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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 + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
GTP + H2O
dihydroneopterin triphosphate + formate
-
first step in the biosynthesis of pteridine coenzymes, such as folic acid and tetrahydrobiopterin
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
Q8S3C2
the enzyme mediates the first and committing step pf the pterin branch of the folate-synthesis pathway
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
Q8S3C2
the enzyme mediates the first and committing step of the pterin branch of the folate-synthesis pathway
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
first step in the biosynthesis pathway leading to dihydrofolate and tetrahydrobiopterin
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
rate-limiting enzyme in the biosynthesis of tetrahydrobiopterin, important in the regulation of monoamine neurotransmitters such a s dopamine, norepinephrine, and serotonin
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
the enzyme is rate limiting in the tetrahydrobiopterin biosynthesis in adipose tissue, overview
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
the enzyme synthesizes the cofactor for the reaction of the phenylalanine hydroxylase
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
first committed step in the biosynthesis of tetrahydrofolate and tetrahydrobiopterin
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
first committed step in the biosynthesis of tetrahydrofolate and tetrahydrobiopterin
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
the enzyme produces the cofactor tetrahydrobiopterin essential for activities of tyrosine hydroxylase and DOPA decarboxylase
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
rate-limiting step in the biosynthesis of tetrahydrobiopterin, a key factor necessary for nitric oxide synthase, and for the hydrolxylases that are involved in the production of catecholamines and serotonin
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
estrogens play a regulatory role on the enzyme expression, the enzyme is involved in estrogen receptor interaction with cyclic AMP, role of receptor subtypes, overview
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
the enzyme controls the biosynthesis pathway of tetrahydrobiopterin, which is a necessary cofactor for inducible nitric oxide synthase
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
the enzyme is feedback regulated by the GTPCH feedback regulatory protein GFRP, overview
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
the enzyme mediates the first and committing step of the pterin branch of the folate-synthesis pathway
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
-
first step in pathway of pterins
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
-
first step in pathway of pterins
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
-
first step in pathway of pterins
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
-
first step in pathway of pterins
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
-
first step in pathway of pterins
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
-
first step in pathway of pterins
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
-
first step in pathway of pterins
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
-
first step in pathway of pterins
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
-
first step in biosynthesis of tetrahydrobiopterin, BH4
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
-
first step in pathway of pterins
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
-
first step in pathway of pterins
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
-
first step in pathway of pterins
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
-
first step in pathway of pterins
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
-
first step in pathway of pterins
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
Serratia indica
-
first step in pathway of pterins
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
Serratia indica
-
first step in pathway of pterins
-
?
GTP + H2O
formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine triphosphate
Serratia indica
-
first step in pathway of pterins
-
?
GTP + H2O
formate + 7,8-dihydroneopterin 3'-triphosphate
-
-
-
?
GTP + H2O
formate + 7,8-dihydroneopterin 3'-triphosphate
-
-
-
?
GTP + H2O
formate + 7,8-dihydroneopterin 3'-triphosphate
-
-
-
?
GTP + H2O
formate + 7,8-dihydroneopterin 3'-triphosphate
-
-
-
?
GTP + H2O
formate + 7,8-dihydroneopterin 3'-triphosphate
-
-
-
?
GTP + H2O
formate + D-erythro-dihydroneopterin triphosphate
-
first commited step in the biosynthesis of tetrahydrofolate and tetrahydrobiopterin
-
-
?
GTP + H2O
formate + D-erythro-dihydroneopterin triphosphate
-
first step of the biosynthesis of (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin, i.e. BH4
-
-
?
additional information
?
-
-
GTPCH1 via tetrahydrobiopterin maintains normal blood pressure and endothelial function in vivo by preserving nitric oxide synthesis by endothelial NO synthase
-
-
?
additional information
?
-
-
GTP cyclohydrolase I stimulates tyrosine hydroxylase activity by increasing the maximal velocity of the enzyme and fails to block the feedback inhibition of tyrosine hydroxylase by dopamine
-
-
?
additional information
?
-
-
GCYH-I is not only the first enzyme of the tetrahydrofolate and tetrahydropterin pathways, but also the first enzyme of queuosine and archaeosine biosynthesis
-
-
?
additional information
?
-
-
GCYH-I is not only the first enzyme of the tetrahydrofolate and tetrahydropterin pathways, but also the first enzyme of queuosine and archaeosine biosynthesis
-
-
?
additional information
?
-
-
GTPCH I is the rate-limiting enzyme for de novo tetrahydrobiopterin synthesis
-
-
?
additional information
?
-
-
catalyzes the first step in the biosynthesis of methanopterin
-
-
?
additional information
?
-
-
catalyzes the first step in the biosynthesis of methanopterin
-
-
?
additional information
?
-
-
GTPCH1 via tetrahydrobiopterin maintains normal blood pressure and endothelial function in vivo by preserving nitric oxide synthesis by endothelial NO synthase
-
-
?
additional information
?
-
-
tetrahydrobiopterin production by GTPCH I occurs in close proximity to endothelial nitric oxide synthase
-
-
?
additional information
?
-
-
isozyme GTPCHIa activity is involved in formation of the black markings on the larva during fourth ecdysis, pigmentation pathway overview
-
-
?
additional information
?
-
-
enzyme deficiency causes hyperphenylalaninemia with severe neurological disorders, the 3,4-dihydroxyphenylalanine, i.e. DOPA, responsive form of dystonia, and endothelial dysfunction, all by (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin depletion, the GTP cyclohydrolase I feedback regulatory protein GFRP binds to the enzyme and mediates the regulation of the enzyme by L-phenylalanine and (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin
-
-
?
additional information
?
-
-
tetrahydrobiopterin, the cofactor required for hydroxylation of aromatic amino acids, regulates its own synthesis through feedback inhibition of the enzyme mediated by the regulatory subunit called GTP cyclohydrolase I feedback regulatory protein, i.e. GFRP
-
-
?
additional information
?
-
-
GCH1 interacts with GCH1 interacts with GTP cyclohydrolase I feedback regulatory protein, GFRP, and very long-chain specific acyl-CoA dehydrogenase in the liver, tubulin beta-2A chain in the liver and brain, DnaJ homolog subfamily A member 1 and fatty aldehyde dehydrogenase in the liver, heart and kidney and eukaryotic translation initiation factor 3 subunit I in all organs tested, overview. GCH1 associates with mitochondrial proteins and interacts with VLCAD, a mitochondrial protein
-
-
?
additional information
?
-
-
GCH1 interacts with GCH1 interacts with GTP cyclohydrolase I feedback regulatory protein, GFRP, and very long-chain specific acyl-CoA dehydrogenase in the liver, tubulin beta-2A chain in the liver and brain, DnaJ homolog subfamily A member 1 and fatty aldehyde dehydrogenase in the liver, heart and kidney and eukaryotic translation initiation factor 3 subunit I in all organs tested, overview. GCH1 associates with mitochondrial proteins and interacts with VLCAD, a mitochondrial protein
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
Mg2+
Mn2+
Zn2+
additional information
Mn2+
-
at 2 mM Mn2+ is able to restore MptA activity to a higher level than Fe2+, Mn2+ enzyme is not inactivated by exposure to oxygen
Zn2+
-
isozyme GCYH-1A is a Zn2+-dependent enzyme, isozyme GCYH-IB is expressed only under Zn2+-limiting conditions
Zn2+
-
catalytically essential ion, complexed to 2 cysteine and 1 histidine residue
Zn2+
-
essential for activity, coordinated to a His-side chain of the active site
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
Zn2+
-
absolutely required, e.g. for activity and reconstitution of the denatured enzyme, 1 Zn2+ bound per subunit of the decameric enzyme
Zn2+
essential for activity, coordinated to a His-side chain of the active site, mechanistic role
Zn2+
the zinc ion is bound by residues Cys108, His111, and Cys179
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dihydrobiopterin
-
induction of feedback inhibition, binding site structure
GTP cyclohydrolase feedback regulatory protein
-
i.e. GFRP, GTP cyclohydrolase I, GTPCH-1, undergoes negative feedback regulation by its endproduct tetrahydrobiopterin via interaction with the GTP cyclohydrolase feedback regulatory protein, GFRP. GFRP binding increased the apparent Km of GTPCH-1, which also contributes to inhibition and increases the cooperativity of substrate binding in the wild-type but not the S81D mutant. GFRP both inhibits and stimulates GTPCH-1 activity in vitro depending on interactions with either tetrahydrobiopterin or phenylalanine. GTPCH-1 phosphorylation reduces its binding to GFRP
-
GTP cyclohydrolase I feedback regulatory protein GFRP
-
natural inhibitor, inhibition mechanism, in vitro inhibition together with 2,4-diamino-6-hydroxypyrimidine, the inhibition is fully reversible by L-phenylalanine, regulatory function in physiological feedback inhibition, overview
-
GTPCH feedback regulatory protein
-
GFRP, the allosteric regulatory protein GFRP triggers a noncompetitive attenuation of GTPCH activity, an allosteric effector is unnecessary for GFRP to influence GTPCH activity. GFRP-mediated allosteric regulation by small molecule effectors is indistinguishable for truncated mutant DELTA45-GTPCH and wild-type GTPCH
-
H2O2
-
more than 0.3 mM H2O2 result in a decrease in activity of GTPCHI, the function of the GTP cyclohydrolase I/GTP cyclohydrolase I feedback regulatory protein complex is not affected by H2O2
streptozotocin
-
the expression of GCH-I is decreased by streptozotocin treatment (60 mg/kg iv, 7 weeks)
(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin
-
i.e. BH4, feedback inhibition mediated by GTP cyclohydrolase I feedback regulatory protein, i.e. GFRP, in complex with the enzyme, binding site structure
(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin
-
i.e. BH4, feedback inhibition mediated by GTP cyclohydrolase I feedback regulatory protein, i.e. GFRP, inhibition is enhaced by dGTP
2,4-Diamino-6-hydroxypyrimidine
-
direct inhibitition at higher concentrations
2,4-Diamino-6-hydroxypyrimidine
-
DAHP, the inhibition mechanism involves the GTP cyclohydrolase I feedback regulatory protein GFRP, overview, the inhibition is fully reversible by L-phenylalanine
8-oxo-GTP
competitive inhibitor. The inhibitor interacts with a conserved active site Cys149, and this residue is S-nitrosylated. Ki/Km: 0.022
8-oxo-GTP
competitive inhibition, binds tightly to the enzyme with higher affinity than GTP, structure and binding network, overview
Co2+
-
inhibition by elimination of the required metal-free GTP when present at high concentration with respect to the GTP concentration, overview
L-erythro-5,6,7,8-tetrahydrobiopterin
-
indirect inhibition of 2,4-diamino-6-hydroxypyrimidine at lower concentrations with the help of feedback regulatory protein
L-erythro-5,6,7,8-tetrahydrobiopterin
-
L-phenylalanine reverses inhibition; with help of feedback regulatory protein
Mg2+
-
inhibition by elimination of the required metal-free GTP when present at high concentration with respect to the GTP concentration, formation of Mg-GTP, overview
Mn2+
-
inhibition by elimination of the required metal-free GTP when present at high concentration with respect to the GTP concentration, overview
tetrahydrobiopterin
-
GTP cyclohydrolase I, GTPCH-1, undergoes negative feedback regulation by its endproduct tetrahydrobiopterin via interaction with the GTP cyclohydrolase feedback regulatory protein, GFRP
tetrahydrobiopterin
-
induction of feedback inhibition of the enzyme via mediation of GFRP which forms a complex with the enzyme, binding site structure
tetrahydrobiopterin
-
the cofactor required for hydroxylation of aromatic amino acids regulates its own synthesis through feedback inhibition of the enzyme mediated by the regulatory subunit called GTP cyclohydrolase I feedback regulatory protein, i.e. GFRP
tetrahydrobiopterin
-
BH4, can limit its own synthesis by triggering decameric GTPCH to assemble in an inhibitory complex with two GTPCH feedback regulatory protein, GFRP, pentamers
Zn2+
-
inhibition by elimination of the required metal-free GTP when present at high concentration with respect to the GTP concentration, overview
additional information
-
synthesis and inhibitory potential of 7-deazaguanine derivatives on GTPCH I, inhibitory mechanism, overview
-
additional information
-
Mn2+ enzyme is not inactivated by exposure to oxygen
-
additional information
-
GTP-CH1 activity can be inhibited by tetrahydrobiopterin through its protein-protein interactions with GTP-CH1 regulatory protein
-
additional information
-
asymmetric dimethylarginine, ADMA, decreases GCH1 protein, but not mRNA concentrations, in pulmonary arterial endothelial cells because of the ubiquitination and proteasome-dependent degradation of GCH1. Overexpression of CHIP potentiates, whereas a CHIP U-box domain mutant attenuates, ADMA-induced GCH1 degradation and reductions in cellular BH4 concentrations. L-Arginine acts antagonistic and restores the activities
-
additional information
-
the N-terminal peptide of mammalian GTP cyclohydrolase I is an autoinhibitory control element and contributes to binding the allosteric regulatory protein GFRP. The autoinhibitory peptide provides a molecular mechanism for physiological up-regulation of GTPCH activity
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
17beta-estradiol
-
can regulate GTPCH gene expression via transcriptional mechanisms
interferon-gamma
-
GCH1 expression is strongly induced by a mixture of interleukin-1beta, tissue necrosis factor-alpha, and interferon-gamma released by microglia under brain-damaging conditions
-
interleukin-1beta
-
GCH1 expression is strongly induced by a mixture of interleukin-1beta, tissue necrosis factor-alpha, and interferon-gamma released by microglia under brain-damaging conditions
-
lipolysaccharide
commercially isolated from Escherichia coli serotype 026:B6, activates and upregulates the enzyme in adipose tissue, but in cultured 3T3-L1 adipocytes lipolysaccharide addition only increases the enzyme expression level in presence of TNFalpha and interferon gamma, overview
-
tissue necrosis factor-alpha
-
GCH1 expression is strongly induced by a mixture of interleukin-1beta, tissue necrosis factor-alpha, and interferon-gamma released by microglia under brain-damaging conditions
-
L-phenylalanine
-
feed-forward stimulation at subsaturating concentration of GTP mediated by GTP cyclohydrolase I feedback regulatory protein, i.e. GFRP
L-phenylalanine
-
feed-forward stimulation at subsaturating concentration of GTP mediated by GTP cyclohydrolase I feedback regulatory protein, i.e. GFRP, in complex with the enzyme, binding site structure
L-phenylalanine
-
stimulates the enzyme via mediation of GFRP which forms a complex with the enzyme
additional information
-
GTP cyclohydrolase I is activated by phosphorylation with protein kinase C or A
-
additional information
-
GTPCH expression is regulated by inflammatory stimuli, in association with reduced expression of GTP cyclohydrolase feedback regulatory protein
-
additional information
-
reduction in GTP-CH1 regulatory protein expression following proinflammatory stimulation is necessary for optimal GTP-CH1 activity
-
additional information
-
estrogen-triggered activation of GTP cyclohydrolase 1 gene expression, time course in transfected cells and mechanism, overview
-
additional information
-
lipopolysaccharide application by injection increases enzyme expression in kidney, but not in liver and lung
-
additional information
GTP-CH 1 mRNA and protein expression is unaltered by renal ischemia-reperfusion
-
additional information
-
GTP-CH 1 mRNA and protein expression is unaltered by renal ischemia-reperfusion
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.053
GTP
pH and temperature not specified in the publication
0.00987
GTP
-
isozyme GCYH-IB, in 100 mM HEPES (pH 8.0), 100 mM KCl, 0.5 mM MnCl2, 1 mM dithiothreitol, temperature not specified in the publication
additional information
additional information
steady-state kinetics
-
additional information
additional information
-
(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin and Phe ligand binding kinetics of the enzyme complex at pH 6.0 and pH 7.2
-
additional information
additional information
-
association and dissociation constants of wild-type and mutant enzymes in oligomerization
-
additional information
additional information
-
kinetics of the reaction steps, single turnover experiments, wild-type and H179N mutant enzymes, overview
-
additional information
additional information
-
stopped-flow kinetic analysis of the reaction, single turnover experiments, the rate-limiting step occurs rather late in the reaction sequence
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000265
GTP
pH and temperature not specified in the publication
0.0011
GTP
-
isozyme GCYH-IB, in 100 mM HEPES (pH 8.0), 100 mM KCl, 0.5 mM MnCl2, 1 mM dithiothreitol, temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
9.164
2'-deoxy-GTP
pH and temperature not specified in the publication
0.0457
7-deaza-GTP
pH and temperature not specified in the publication
0.000149
8-oxo-GTP
pH and temperature not specified in the publication
additional information
additional information
inhibition kinetics
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.000001
wild-type native enzyme and recombinant HAT10-tagged enzyme from expression in Escherichia coli BL21(DE3)
0.000029
recombinant enzyme from expression in Mycobacterium smegmatis/pSMT-260
0.0001
0.00027
recombinant HAT-tagged enzyme from expression in Escherichia coli JM109
0.00088
recombinant HAT-217-tagged enzyme from expression in Escherichia coli BL21(DE3)
0.088
wild-type enzyme, substrate 2-amino-5-formylamino-6-ribofuranosylamino-4(3H)-pyrimidinone triphosphate
6
purified recombinant HAT-tagged enzyme expressed in Escherichia coli
additional information
0.0001
below, mutant enzymes, substrate 2-amino-5-formylamino-6-ribofuranosylamino-4(3H)-pyrimidinone triphosphate
additional information
tissue dependent enzyme activity and effects of cytokines
additional information
-
tissue dependent enzyme activity and effects of cytokines
additional information
activity of differently expressed recombinant enzymes
additional information
-
activity of differently expressed recombinant enzymes
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.8
8.5
additional information
8.5
-
wild-type enzyme and mutants R56L, C110G, E111K, L134Q, K136E, H179Q, C181S, and R185G
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
50
the enzyme activity is improved by the rise in temperature up to 50°C
60
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Serratia indica
isozyme Pu-RA; GTP cyclohydrolase isoform Pu-RA
UniProt
brenda
isozyme Pu-RB; GTP cyclohydrolase isoform Pu-RB
UniProt
brenda
isozyme Pu-RC; GTP cyclohydrolase isoform Pu-RC
UniProt
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
the black markings on the larva during fourth ecdysis are involving the GTPCHI activity
brenda
-
transfected with a tet-off plasmid and a plasmid encoding human GCH1, the stable clone is named tet-GCH cell
brenda
additional information
cardiomyocyte GTP cyclohydrolase 1 protects the heart against diabetic cardiomyopathy
brenda
-
of pulmonary arteries, veins, airway epithelium, and nerves
brenda
-
larval, expression pattern of GTPCH isozymes Ia and Ib, overview
brenda
cardiac GTP cyclohydrolase 1 is degraded in remodeled hearts after myocardial infarction, concomitant with increases in the thickness of interventricular septum, interstitial fibrosis, and phosphorylated p38 mitogen-activated protein kinase and decreases in left ventricular anterior wall thickness, cardiac contractility, tetrahydrobiopterin, the dimers of nitric oxide synthase, sarcoplasmic reticulum Ca2+ release, and the expression of sarcoplasmic reticulum Ca2+ handling proteins
brenda
-
pulmonary arteries, veins, airway epithelium, and nerves, developmental regulation of GTP-CH1, equally expressed in pulmonary hypertensive and healthy piglets
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
GTPCH I is also co-localized with caveolin-1 to caveolar membrane microdomains of endothelial cells
-
brenda
-
GTPCH I staining is localized to perinuclear regions of the cell
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
malfunction
metabolism
additional information
physiological function
-
endothelium-specific GTP cyclohydrolase I overexpression accelerates refractory wound healing in streptozotocin-induced type 1 diabetic mice through enhanced constitutive NOS activity and suppressed oxidative stress
physiological function
-
GCH-1 is a key enzyme in de novo tetrahydrobiopterin biosynthesis. GCH-1 is critical for maintaining coupled NOS activity and aromatic amino acid hydroxylation, pain sensitivity and chronicity, and immune responses
physiological function
isozyme GCYH-IB functions to allow folate biosynthesis during Zn2+ starvation
physiological function
-
isozyme GCYH-IB functions to allow folate biosynthesis during Zn2+ starvation, isozyme GCYH-IB functionally replaces GCYH-IA in Bacillus subtilis under zinc-limiting conditions
physiological function
Dube3a, the fly UBE3A orthologue, positively regulates Punch/GCH1 in the fly brain. GCH1 is a UBE3A target involved in neurotransmitter regulation and has broad implications for how the function of this target may contribute to the pathogenesis of Angelman syndrome, duplication 15q autism as well as idiopathic autism linked to UBE3A regulated pathways
physiological function
-
GCH1 might have broader functions beyond tetrahydrobiopterin biosynthesis. It interacts with proteins in an organ dependent manner and eukaryotic translation initiation factor 3 subunit I, EIF3I, might be a general regulator of GCH1. GCH1 is regulated by protein-protein interaction
physiological function
-
GTP cyclohydrolase I interaction is required for degradation of the C-terminus of heat shock protein 70-interacting protein. GCH1 is a client protein for Hsp90. The U-box domain of CHIP is essential for ADMA-mediated GCH1 degradation in pulmonary arterial endothelial cells
physiological function
-
GTP cyclohydrolase I is the rate-limiting enzyme for tetrahydrobiopterin synthesis. Cardiac myocyte-specific overexpression of human GTP cyclohydrolase I protects against acute cardiac allograft rejection
physiological function
-
GTP cyclohydrolase I is the rate-limiting enzyme for tetrahydrobiopterin synthesis. Cardiac myocyte-specific overexpression of human GTP cyclohydrolase I protects against acute cardiac allograft rejection
physiological function
-
GTP cyclohydrolase I, GTPCH-1, is the rate-limiting enzyme involved in de novo biosynthesis of tetrahydrobiopterin, an essential cofactor for nitric oxide synthases and aromatic amino acid hydroxylases. GTPCH-1 undergoes negative feedback regulation by its endproduct tetrahydrobiopterin via interaction with the GTP cyclohydrolase feedback regulatory protein, GFRP. GTPCH-1 levels, GTPCH-1 phosphorylation status and GFRP levels play critical roles in regulating eNOS uncoupling in response to oscillatory shear stress, overview
physiological function
-
the autoinhibitory peptide provides a molecular mechanism for physiological up-regulation of GTPCH activity. GTPCH activity regulation by GTPCH feedback regulatory protein, GFRP
physiological function
-
GTP cyclohydrolase I is the rate-limiting enzyme for tetrahydrobiopterin synthesis. Cardiac myocyte-specific overexpression of human GTP cyclohydrolase I protects against acute cardiac allograft rejection
-
physiological function
-
GCH1 might have broader functions beyond tetrahydrobiopterin biosynthesis. It interacts with proteins in an organ dependent manner and eukaryotic translation initiation factor 3 subunit I, EIF3I, might be a general regulator of GCH1. GCH1 is regulated by protein-protein interaction
-
malfunction
-
decreases in GTPCH activity and expression in late stages of acute cardiac rejection due to a deficit in BH4
malfunction
-
decreases in GTPCH activity and expression in late stages of acute cardiac rejection due to a deficit in BH4. Mechanism of the decreased rejection appears related to decreased T cell proliferation and modulation of immune function by higher expression of genes involved in hematopoietic/stromal cell development and recruitment
malfunction
-
multimeric assemblies of wild-type GTPCH and truncation mutant DELTA45-GTPCH on their own display markedly different banding patterns
malfunction
three different heterozygous mutations in the Punch gene enhance the gmr-Dube3a rough eye phenotype causing a glazed appearance, loss of inter-ommatidial bristles and often displaying yellowish discoloration indicative of underlying neurodegeneration. In the heterozygous state these mutations in Punch show no eye phenotype when crossed to the gmr-GAL4 driver alone and the individual UAS-Dube3a stocks without gmr-GAL4 do not have rough eyes
malfunction
three different heterozygous mutations in the Punch gene enhance the gmr>Dube3a rough eye phenotype causing a glazed appearance, loss of inter-ommatidial bristles and often displaying yellowish discoloration indicative of underlying neurodegeneration. In the heterozygous state these mutations in Punch show no eye phenotype when crossed to the gmr-GAL4 driver alone and the individual UAS-Dube3a stocks without gmr-GAL4 do not have rough eyes
malfunction
GTP cyclohydrolase I gene polymorphisms are associated with endothelial dysfunction and oxidative stress in patients with type 2 diabetes mellitus
malfunction
-
decreases in GTPCH activity and expression in late stages of acute cardiac rejection due to a deficit in BH4
-
metabolism
-
GCH-1 is the rate-limiting enzyme for tetrahydrobiopterin synthesis
metabolism
-
GTP cyclohydrolase I is the rate-limiting enzyme in generation of tetrahydrobiopterin
metabolism
-
GTPCH I is the rate-limiting enzyme for de novo tetrahydrobiopterin synthesis
metabolism
-
GTP cyclohydrolase I is the rate-limiting enzyme for tetrahydrobiopterin synthesis
metabolism
-
GTP cyclohydrolase I is the rate-limiting enzyme for tetrahydrobiopterin synthesis
metabolism
-
GTP cyclohydrolase I, GTPCH-1, is the rate-limiting enzyme involved in de novo biosynthesis of tetrahydrobiopterin, an essential cofactor for nitric oxide synthases and aromatic amino acid hydroxylases
metabolism
-
the N-terminal peptide of mammalian GTP cyclohydrolase I is an autoinhibitory control element and contributes to binding the allosteric regulatory protein GFRP
metabolism
the Punch protein, an enzyme that produces tetrahydrobiopterin, is the rate-limiting co-factor in monoamine synthesis. Dube3a, the fly UBE3A orthologue, regulates Punch/GCH1 in the fly brain. Drosophila Ube3a regulates monoamine synthesis by increasing GTP cyclohydrolase I activity via a non-ubiquitin ligase mechanism, overview
metabolism
the Punch protein, an enzyme that produces tetrahydrobiopterin, is the rate-limiting cofactor in monoamine synthesis. Dube3a, the fly UBE3A orthologue, regulates Punch/GCH1 in the fly brain. Drosophila Ube3a regulates monoamine synthesis by increasing GTP cyclohydrolase I activity via a non-ubiquitin ligase mechanism, overview
metabolism
cardiac GTP cyclohydrolase 1 is degraded in remodeled hearts after myocardial infarction, concomitant with increases in the thickness of interventricular septum, interstitial fibrosis, and phosphorylated p38 mitogen-activated protein kinase and decreases in left ventricular anterior wall thickness, cardiac contractility, tetrahydrobiopterin, the dimers of nitric oxide synthase, sarcoplasmic reticulum Ca2+ release, and the expression of sarcoplasmic reticulum Ca2+ handling proteins. Transgenic overexpression of GTP cyclohydrolase 1 in cardiomyocytes reduces the thickness of interventricular septum and interstitial fibrosis and increases anterior wall thickness and cardiac contractility after infarction. Overexpression of GTP cyclohydrolase 1 decreases phosphorylated p38 mitogen-activated protein kinase and elevates tetrahydrobiopterin levels, the dimerization and phosphorylation of neuronal nitric oxide synthase, sarcoplasmic reticulum Ca2+ release, and sarcoplasmic reticulum Ca2+ handling proteins in post-infarction remodeled hearts
metabolism
-
GTP cyclohydrolase I is the rate-limiting enzyme for tetrahydrobiopterin synthesis
-
additional information
-
adult cardiac myocytes despite expression of GTPCH mRNA and protein have a defective basal and cytokine-stimulated synthesis of BH4 via the de novo synthesis pathway and impaired synthesis via the salvage pathway in contrast with that typically seen in neonatal cardiac myocytes
additional information
-
asymmetric dimethylarginine, ADMA, decreases GCH1 protein, but not mRNA concentrations, in pulmonary arterial endothelial cells because of the ubiquitination and proteasome-dependent degradation of GCH1. Hsp90-GCH1 interactions are reduced, whereas the association of GCH1 with Hsp70 and the C-terminus of Hsp70-interacting protein, i.e. CHIP, increases in the cells. In vivo Hsp90/GCH1 interactions are decreased, whereas GCH1-Hsp70 and GCH1-CHIP interactions and GCH1 ubiquitination are increased. L-Arginine acts antagonistic and restores the activities
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
108600
isozyme GCYH-1B, apparent molecular weight estimated from gel filtration
120000
-
wild-type enzyme in presence of 0.3 M KCl, mutants C110G, E111K, H112D, and C181S, gel filtration
135000
24500
10 * 24563, sequence calculation, 10 * 24500, MALDI-TOF mass spectrometry, 10 * 35000, recombinant HAT-tagged enzyme
24563
10 * 24563, sequence calculation, 10 * 24500, MALDI-TOF mass spectrometry, 10 * 35000, recombinant HAT-tagged enzyme
25000
28568
4 * 28568, isozyme GCYH-1B, apparent molecular weight estimated from gel filtration
30000
35000
39000
50000
additional information
-
MW of mutant E152K is very high in gel filtration approximately corresponding to a didecameric form
25000
-
10 * 25000, about, composed of a pentamers of 5 dimers, the active site is located at the interface between dimers, Lys136, Arg139, and Glu152 are especially important for the oligomerization
35000
10 * 24563, sequence calculation, 10 * 24500, MALDI-TOF mass spectrometry, 10 * 35000, recombinant HAT-tagged enzyme
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decamer
homodimer
homotetramer
tetramer
additional information
decamer
-
10 * 25000, about, composed of a pentamers of 5 dimers, the active site is located at the interface between dimers, Lys136, Arg139, and Glu152 are especially important for the oligomerization
decamer
10 * 24563, sequence calculation, 10 * 24500, MALDI-TOF mass spectrometry, 10 * 35000, recombinant HAT-tagged enzyme
decamer
-
10 * 24563, sequence calculation, 10 * 24500, MALDI-TOF mass spectrometry, 10 * 35000, recombinant HAT-tagged enzyme
-
decamer
-
2 pentamers which are positioned in a head-to-head manner to form the active decameric enzyme with an active site at the interface of each couple of dimer
homotetramer
4 * 28568, isozyme GCYH-1B, apparent molecular weight estimated from gel filtration
additional information
digestion of recombinant HAT-tagged enzyme with enterokinase results in proteins of 29.5 and 32.5 kDa
additional information
-
digestion of recombinant HAT-tagged enzyme with enterokinase results in proteins of 29.5 and 32.5 kDa
additional information
-
digestion of recombinant HAT-tagged enzyme with enterokinase results in proteins of 29.5 and 32.5 kDa
-
additional information
-
stimulatory and inhibitory enzyme-GFRP-complex sandwich structure, subunit composition of GFRP pentamer is betabetaalphabetabetaalphabetabeta, overview
additional information
-
multimeric assemblies of wild-type GTPCH and truncation mutant DELTA45-GTPCH on their own display markedly different banding patterns
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
additional information
-
ubiquitination and proteasome-dependent degradation of GCH1. The CHIP-ubiquitin pathway modifies GCH1 in a lamb model of pulmonary hypertension secondary to increased pulmonary blood flow
phosphoprotein
-
S81 phosphorylation enhances GTPCH-1 enzyme activity, GFRP modulates phosphorylation of GTPCH-1, and GTPCH-1 phosphorylation reduces its binding to GFRP, overview
phosphoprotein
-
GCH-1 has 8 potential phosphorylation sites (Ser51, Ser72, Thr85, Thr91, Thr103, Ser130, Ser167, and Thr231). Overexpressed rat GCH-1 is phosphorylated at Ser51, Ser167, and Thr231 in HEK-293 cells
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
selenomethionine-labeled isozyme GCYH-IB, sitting drop vapor diffusion method, using polyethylene glycol 6000 (10-16% (w/v)), LiCl (1-1.4 M), Tris (50 mM, pH 9.0), and Tris-HCl (50 mM, pH 7.0)
-
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
4.6 mg/ml purified recombinant DELTA42-hGTP-CH-I in 0.1 M potassium phosphate, pH 7.0, 0.02% NaN3, mixed with precipitation solution containing 6% PEG 6000, 150 mM KCl, 100 mM MOPS, pH 7.0, equilibration against precipitant solution, X-ray diffraction strcuture determination and analysis at 3.1 A resolution, modeling
sitting-drop vapor-diffusion method at 20°C. Crystallized from 1.3 M sodium citrate pH 7.3. The crystal structure is solved at a resolution of 2.4 A
crystals are grown at 20°C by vapor diffusion in sitting drops. High-resolution crystal structures of the enzyme: one in complex with the reaction intermediate analog and competitive inhibitor 8-oxo-GTP, and one with a TRIS molecule bound in the active site and mimicking another reaction intermediate
5 mg/ml enzyme subunit GTP cyclohydrolase I feedback regulatory protein, i.e. GFRP, free and complexed with the human catalytic subunit of the enzyme, batch procedure, at 4°C overnight, total reflection X-ray fluorescence spectrometry, structure determination and analysis at 2.6 A resolution, modeling
-
crystallization of purified recombinant enzyme and protein GFRP forming a BH2-induced inhibitory complex, involving dGTP, in 14% isopropanol, 0.2 M ammonium sulfate, 10% PEG 300, 10% ethylene glycol, 0.1 M MES-Na, pH 6.0, rapid freezing of crystals in liquid nitrogen, X-ray diffraction structure determination and analysis at 2.8 A resolution
-
purified recombinant enzyme complexed with recombinant wild-type and selenomethionine derivatized GFRP, the complex with the latter being used as CH3HGCl derivative, 5 mg/ml protein complex in 24% v/v 2-methyl-2,4-pentanediol, 75 mM Tris-HCl, pH 7.5, 50 mM KCl, 5 mM phenylalanine, X-ray diffraction structure determination and analysis at 2.7-2.8 A resolution, model building
-
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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S37E
-
the enzymatic activity is significantly higher than of wild type GTPCH isoform C
S135C
-
site-directed mutagenesis, 0.7% activity compared to the wild-type enzyme, decreased pH and temperature optimum
H179N
-
mutant H179N is not able to perform the whole reaction step, but can catalyzes the reversible formation of reaction intermediate 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone
K136E
-
site-directed mutagenesis, 0.25% activity compared to the wild-type enzyme, increased temperature optimum
C181S
R56L
-
site-directed mutagenesis, 14% activity compared to the wild-type enzyme, increased temperature optimum
C110G
-
site-directed mutagenesis, 0.22% activity compared to the wild-type enzyme, increased temperature optimum
E111K
-
site-directed mutagenesis, 3.1% activity compared to the wild-type enzyme, increased temperature optimum
H112D
-
site-directed mutagenesis, 0.23% activity compared to the wild-type enzyme, decreased pH optimum, increased temperature optimum
H113N
-
site-directed mutagenesis, 67% activity compared to the wild-type enzyme, decreased pH optimum, increased temperature optimum
L134Q
-
site-directed mutagenesis, 1.85% activity compared to the wild-type enzyme, increased temperature optimum
R139C
-
site-directed mutagenesis, 29.3% activity compared to the wild-type enzyme, decreased pH o