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Information on EC 2.7.6.3 - 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase
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EC Tree
2.7.6.3 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinaseIUBMB Comments
Binds 2 Mg2+ ions that are essential for activity . The enzyme participates in the biosynthetic pathways for folate (in bacteria, plants, fungi, and some archaeal species, including the haloarchaea) and methanopterin (in some archaeal species such as the Archaeoglobi and Methanobacteria). The enzyme exists in varying types of multifunctional proteins in different organisms. The enzyme from the bacterium Streptococcus pneumoniae also harbours the activity of EC 4.1.2.25, dihydroneopterin aldolase , the enzyme from the plant Arabidopsis thaliana harbours the activity of EC 2.5.1.15, dihydropteroate synthase , while the enzyme from yeast Saccharomyces cerevisiae is trifunctional with both of the two above mentioned activities .
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Word Map
- 2.7.6.3
-
pyrophosphorylation
- pyrophosphate
- pterins
-
folic
- dihydrofolate
-
bisubstrate
-
sulfa
- dihydroneopterin
- ampcpp
- tetrahydrofolate
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induced-fit
- drug development
- medicine
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase (hppk), 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, cythppk/dhps, fthppk-dhps, 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase, hppk/dhps, hydroxymethyldihydropterin pyrophosphokinase (hppk), 7,8-dihydroxymethylpterin-pyrophosphokinase, mithppk/dhps, hydroxymethyldihydropteridine pyrophosphokinase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase
2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase
2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase/dihydropteroate synthase
6-hydroxy-7,8-dihydropterin pyrophosphokinase
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6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase
6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase-dihydropteroate synthase
6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase/dihydropteroate synthase
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bifunctional enzyme
6-hydroxymethyl-7,8-dihydroxypterin pyrophosphokinase/7,8-dihydropteroate synthase
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bifunctional protein involved in tetrahydrofolate synthesis
7,8-dihydro-6-hydroxymethylpterin pyrophosphokinase
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7,8-dihydropteroate-synthesizing enzyme
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it is not possible to distinguish, whether the enzyme exists as an enzyme complex of 6-hydroxymethyl-7,8-dihydroxypterin pyrophosphokinase and 7,8-dihydropteroate synthase or whether both reactions are catalyzed by a single enzyme
7,8-dihydroxymethylpterin-pyrophosphokinase
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ATP:2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine 6'-pyrophosphotransferase
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FtHPPK-DHPS
H2-pteridine-CH2-OH pyrophosphokinase
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H2-pteridine-CH2OH pyrophosphokinase
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HPPK
HPPK-DHPS
HPPK/DHPS
HPPK/dihydropteroate synthase
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HPPK part of the bifunctional protein can function by itself but a larger part of the polypeptide is needed to ensure full functionality
hydroxymethyl-7,8-dihydropterin pyrophosphokinase/7,8-dihydropteroate synthase
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hydroxymethyldihydropteridine pyrophosphokinase
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hydroxymethyldihydropterin diphosphokinase/dihydropteroate synthase
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HPPK part of the bifunctional protein can function by itself but a larger part of the polypeptide is needed to ensure full functionality
hydroxymethyldihydropterin pyrophosphokinase-dihydropteroate synthase
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bifunctional enzyme
PPPK
pyrophosphokinase, 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine
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additional information
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6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase domain of the multifunctional folic acid synthesis enzyme
2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase
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2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase
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2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase
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2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase
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2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase/dihydropteroate synthase
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2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase/dihydropteroate synthase
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6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase
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6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase
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6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase-dihydropteroate synthase
HPPK-DHPS, bifunctional enzyme
6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase-dihydropteroate synthase
HPPK-DHPS, bifunctional enzyme
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HPPK
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HPPK
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + 6-hydroxymethyl-7,8-dihydropterin = AMP + 6-hydroxymethyl-7,8-dihydropterin diphosphate
ATP + 6-hydroxymethyl-7,8-dihydropterin = AMP + 6-hydroxymethyl-7,8-dihydropterin diphosphate
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ATP + 6-hydroxymethyl-7,8-dihydropterin = AMP + 6-hydroxymethyl-7,8-dihydropterin diphosphate
during its catalytic cycle, the enzyme must assume at least five liganded forms: the apoenzyme form (without either of the substrates), the binary substrate complex with MgATP, the ternary substrate complex (Michaelis complex) with MgATP and 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine, the ternary product complex with AMP and 6-hydroxymethyl-7,8-dihydropterin diphosphate (HPPP), and the binary product complex with HPPP
ATP + 6-hydroxymethyl-7,8-dihydropterin = AMP + 6-hydroxymethyl-7,8-dihydropterin diphosphate
in the enzyme mechanism, the assembly of the pterin-binding pocket depends on ATP-dependent conformational changes in the three active site loops
ATP + 6-hydroxymethyl-7,8-dihydropterin = AMP + 6-hydroxymethyl-7,8-dihydropterin diphosphate
ordered kinetic mechanism, with Mg2+-dependent ATP binding followed by rapid addition of 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine
ATP + 6-hydroxymethyl-7,8-dihydropterin = AMP + 6-hydroxymethyl-7,8-dihydropterin diphosphate
ordered kinetic mechanism, with Mg2+-dependent ATP binding followed by rapid addition of 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diphosphate transfer
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PATHWAY SOURCE
PATHWAYS
KEGG
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SYSTEMATIC NAME
IUBMB Comments
ATP:6-hydroxymethyl-7,8-dihydropterin 6'-diphosphotransferase
Binds 2 Mg2+ ions that are essential for activity [4]. The enzyme participates in the biosynthetic pathways for folate (in bacteria, plants, fungi, and some archaeal species, including the haloarchaea) and methanopterin (in some archaeal species such as the Archaeoglobi and Methanobacteria). The enzyme exists in varying types of multifunctional proteins in different organisms. The enzyme from the bacterium Streptococcus pneumoniae also harbours the activity of EC 4.1.2.25, dihydroneopterin aldolase [4], the enzyme from the plant Arabidopsis thaliana harbours the activity of EC 2.5.1.15, dihydropteroate synthase [7], while the enzyme from yeast Saccharomyces cerevisiae is trifunctional with both of the two above mentioned activities [6].
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CAS REGISTRY NUMBER
COMMENTARY
37278-23-2
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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
6-hydroxymethyl-7,8-dihydropterin + ATP
6-hydroxymethyl-7,8-dihydropterin diphosphate + AMP
6-hydroxymethyl-7,8-dihydropterin + MgATP2-
6-hydroxymethyl-7,8-dihydropterin diphosphate + MgAMP
biosynthesis of folate cofactors
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?
ATP + 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine
AMP + (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate
ATP + 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine
AMP + 2-amino-7,8-dihydro-4-hydroxy-6-(diphosphooxymethyl)pteridine
ATP + 6-hydroxymethyl-7,8-dihydropteridine
AMP + 6-hydroxymethyl-7,8-dihydropteridine diphosphate
ATP + 6-hydroxymethyl-7,8-dihydropteridine
AMP + 7,8-dihydro-6-(diphosphooxymethyl)pteridine
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-
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?
ATP + 6-hydroxymethyl-7,8-dihydropterin
AMP + H+ + (7,8-dihydropterin-6-yl)methyl diphosphate
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-
-
?
dATP + 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine
dAMP + 2-amino-7,8-dihydro-4-hydroxy-6-(diphosphooxymethyl)pteridine
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?
6-hydroxymethyl-7,8-dihydropterin + ATP
6-hydroxymethyl-7,8-dihydropterin diphosphate + AMP
tetrahydrofolate biosynthesis
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?
6-hydroxymethyl-7,8-dihydropterin + ATP
6-hydroxymethyl-7,8-dihydropterin diphosphate + AMP
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-
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?
6-hydroxymethyl-7,8-dihydropterin + ATP
6-hydroxymethyl-7,8-dihydropterin diphosphate + AMP
folate biosynthesis
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?
6-hydroxymethyl-7,8-dihydropterin + ATP
6-hydroxymethyl-7,8-dihydropterin diphosphate + AMP
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biosynthesis of folic acid
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?
ATP + 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine
AMP + (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate
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-
-
?
ATP + 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine
AMP + (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate
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-
-
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?
ATP + 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine
AMP + (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate
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-
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?
ATP + 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine
AMP + (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate
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?
ATP + 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine
AMP + (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate
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?
ATP + 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine
AMP + 2-amino-7,8-dihydro-4-hydroxy-6-(diphosphooxymethyl)pteridine
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?
ATP + 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine
AMP + 2-amino-7,8-dihydro-4-hydroxy-6-(diphosphooxymethyl)pteridine
key step in biosynthesis of folic acid
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?
ATP + 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine
AMP + 2-amino-7,8-dihydro-4-hydroxy-6-(diphosphooxymethyl)pteridine
ATP binding is followed by binding of 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine
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?
ATP + 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine
AMP + 2-amino-7,8-dihydro-4-hydroxy-6-(diphosphooxymethyl)pteridine
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?
ATP + 6-hydroxymethyl-7,8-dihydropteridine
AMP + 6-hydroxymethyl-7,8-dihydropteridine diphosphate
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?
ATP + 6-hydroxymethyl-7,8-dihydropteridine
AMP + 6-hydroxymethyl-7,8-dihydropteridine diphosphate
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?
ATP + 6-hydroxymethyl-7,8-dihydropteridine
AMP + 6-hydroxymethyl-7,8-dihydropteridine diphosphate
enzyme binds ATP first, followed by 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine
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?
ATP + 6-hydroxymethyl-7,8-dihydropteridine
AMP + 6-hydroxymethyl-7,8-dihydropteridine diphosphate
the product 6-hydroxymethyl-7,8-dihydropterin diphosphate is an intermediate in the pathway for folic acid biosynthesis
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?
ATP + 6-hydroxymethyl-7,8-dihydropteridine
AMP + 6-hydroxymethyl-7,8-dihydropteridine diphosphate
ordered bi-bi mechanism with ATP as the first substrate
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?
ATP + 6-hydroxymethyl-7,8-dihydropteridine
AMP + 6-hydroxymethyl-7,8-dihydropteridine diphosphate
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ir
ATP + 6-hydroxymethyl-7,8-dihydropteridine
AMP + 6-hydroxymethyl-7,8-dihydropteridine diphosphate
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ir
ATP + 6-hydroxymethyl-7,8-dihydropteridine
AMP + 6-hydroxymethyl-7,8-dihydropteridine diphosphate
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-
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?
ATP + 6-hydroxymethyl-7,8-dihydropteridine
AMP + 6-hydroxymethyl-7,8-dihydropteridine diphosphate
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ordered bi bi mechanism where ATP binds first and 6-hydroxymethyl-7,8-dihydropterin diphosphate is released last
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?
ATP + 6-hydroxymethyl-7,8-dihydropteridine
AMP + 6-hydroxymethyl-7,8-dihydropteridine diphosphate
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?
ATP + 6-hydroxymethyl-7,8-dihydropteridine
AMP + 6-hydroxymethyl-7,8-dihydropteridine diphosphate
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ir
ATP + 6-hydroxymethyl-7,8-dihydropterin
AMP + (7,8-dihydropterin-6-yl)methyl diphosphate
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?
ATP + 6-hydroxymethyl-7,8-dihydropterin
AMP + (7,8-dihydropterin-6-yl)methyl diphosphate
6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase/7,8-dihydropteroate synthase, i.e. mitHPPK/DHPS, is a bifunctional mitochondrial enzyme, which catalyzes the first two consecutive steps of tetrahydrofolate biosynthesis, folate biosynthesis in Arabidopsis thaliana, overview
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?
ATP + 6-hydroxymethyl-7,8-dihydropterin
AMP + (7,8-dihydropterin-6-yl)methyl diphosphate
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fourth step in folate biosynthesis, detailed overview
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?
ATP + 6-hydroxymethyl-7,8-dihydropterin
AMP + (7,8-dihydropterin-6-yl)methyl diphosphate
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the enzyme is absolutely specific for the substrate
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?
ATP + 6-hydroxymethyl-7,8-dihydropterin
AMP + (7,8-dihydropterin-6-yl)methyl diphosphate
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-
-
?
ATP + 6-hydroxymethyl-7,8-dihydropterin
AMP + (7,8-dihydropterin-6-yl)methyl diphosphate
step in the folate biosynthetic pathway, overview
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?
ATP + 6-hydroxymethyl-7,8-dihydropterin
AMP + (7,8-dihydropterin-6-yl)methyl diphosphate
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fourth step in folate biosynthesis, detailed overview
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?
ATP + 6-hydroxymethyl-7,8-dihydropterin
AMP + (7,8-dihydropterin-6-yl)methyl diphosphate
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the enzyme is absolutely specific for the substrate
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?
ATP + 6-hydroxymethyl-7,8-dihydropterin
AMP + (7,8-dihydropterin-6-yl)methyl diphosphate
Q7CKD7
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-
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?
additional information
?
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binding affinity for GTP and GMP, 75fold weaker than for ATP
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?
additional information
?
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binding affinity for GTP and GMP, 75fold weaker than for ATP
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?
additional information
?
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the enzyme does not hydrolyze alpha,beta-methyleneadenosine 5-triphosphate
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?
additional information
?
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the enzyme does not hydrolyze alpha,beta-methyleneadenosine 5-triphosphate
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?
additional information
?
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the bifunctional enzyme comprises the 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK) activity and dihydropteroate synthase (DHPS) activity, EC 2.5.1.15, the latter is very low due, at least in part, to the lack of a key residue that interacts with the substrate p-aminobenzoic acid
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-
?
additional information
?
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the enzyme does not hydrolyze alpha,beta-methyleneadenosine 5-triphosphate
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?
additional information
?
-
the bifunctional enzyme comprises the 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK) activity and dihydropteroate synthase (DHPS) activity, EC 2.5.1.15, the latter is very low due, at least in part, to the lack of a key residue that interacts with the substrate p-aminobenzoic acid
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-
?
additional information
?
-
the bifunctional HPPK-DHPS enzyme catalyzes sequential steps in the folate biosynthesis, i.e. the 6-hydroxymethylpterin pyrophosphokinase reaction and the dihydropteroate synthase, DHPS, reaction, EC 2.5.1.15
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-
?
additional information
?
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coupled assay method development using reduction of DHPS reaction product dihydropteroate to tetrahydropteroate by excess dihydrofolate reductase with the cofactor NADPH, the oxidation of NADPH is monitored, overview
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?
additional information
?
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Q7CKD7
HPPK is a key enzyme in the folate-biosynthetic pathway and is essential for microorganisms but absent from mammals
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-
?
additional information
?
-
-
HPPK is a key enzyme in the folate-biosynthetic pathway and is essential for microorganisms but absent from mammals
-
-
?
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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
6-hydroxymethyl-7,8-dihydropterin + ATP
6-hydroxymethyl-7,8-dihydropterin diphosphate + AMP
6-hydroxymethyl-7,8-dihydropterin + MgATP2-
6-hydroxymethyl-7,8-dihydropterin diphosphate + MgAMP
biosynthesis of folate cofactors
-
-
?
ATP + 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine
AMP + (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate
ATP + 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine
AMP + 2-amino-7,8-dihydro-4-hydroxy-6-(diphosphooxymethyl)pteridine
key step in biosynthesis of folic acid
-
-
?
ATP + 6-hydroxymethyl-7,8-dihydropteridine
AMP + 6-hydroxymethyl-7,8-dihydropteridine diphosphate
6-hydroxymethyl-7,8-dihydropterin + ATP
6-hydroxymethyl-7,8-dihydropterin diphosphate + AMP
tetrahydrofolate biosynthesis
-
-
?
6-hydroxymethyl-7,8-dihydropterin + ATP
6-hydroxymethyl-7,8-dihydropterin diphosphate + AMP
-
-
-
?
6-hydroxymethyl-7,8-dihydropterin + ATP
6-hydroxymethyl-7,8-dihydropterin diphosphate + AMP
folate biosynthesis
-
-
?
6-hydroxymethyl-7,8-dihydropterin + ATP
6-hydroxymethyl-7,8-dihydropterin diphosphate + AMP
-
biosynthesis of folic acid
-
-
?
ATP + 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine
AMP + (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate
-
-
-
?
ATP + 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine
AMP + (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate
-
-
-
-
?
ATP + 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine
AMP + (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate
-
-
-
?
ATP + 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine
AMP + (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate
-
-
-
?
ATP + 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine
AMP + (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate
-
-
-
-
?
ATP + 6-hydroxymethyl-7,8-dihydropteridine
AMP + 6-hydroxymethyl-7,8-dihydropteridine diphosphate
-
-
-
-
?
ATP + 6-hydroxymethyl-7,8-dihydropteridine
AMP + 6-hydroxymethyl-7,8-dihydropteridine diphosphate
the product 6-hydroxymethyl-7,8-dihydropterin diphosphate is an intermediate in the pathway for folic acid biosynthesis
-
?
ATP + 6-hydroxymethyl-7,8-dihydropterin
AMP + (7,8-dihydropterin-6-yl)methyl diphosphate
6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase/7,8-dihydropteroate synthase, i.e. mitHPPK/DHPS, is a bifunctional mitochondrial enzyme, which catalyzes the first two consecutive steps of tetrahydrofolate biosynthesis, folate biosynthesis in Arabidopsis thaliana, overview
-
-
?
ATP + 6-hydroxymethyl-7,8-dihydropterin
AMP + (7,8-dihydropterin-6-yl)methyl diphosphate
-
fourth step in folate biosynthesis, detailed overview
-
-
?
ATP + 6-hydroxymethyl-7,8-dihydropterin
AMP + (7,8-dihydropterin-6-yl)methyl diphosphate
step in the folate biosynthetic pathway, overview
-
-
?
ATP + 6-hydroxymethyl-7,8-dihydropterin
AMP + (7,8-dihydropterin-6-yl)methyl diphosphate
-
fourth step in folate biosynthesis, detailed overview
-
-
?
ATP + 6-hydroxymethyl-7,8-dihydropterin
AMP + (7,8-dihydropterin-6-yl)methyl diphosphate
Q7CKD7
-
-
-
?
additional information
?
-
the bifunctional enzyme comprises the 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK) activity and dihydropteroate synthase (DHPS) activity, EC 2.5.1.15, the latter is very low due, at least in part, to the lack of a key residue that interacts with the substrate p-aminobenzoic acid
-
-
?
additional information
?
-
the bifunctional enzyme comprises the 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK) activity and dihydropteroate synthase (DHPS) activity, EC 2.5.1.15, the latter is very low due, at least in part, to the lack of a key residue that interacts with the substrate p-aminobenzoic acid
-
-
?
additional information
?
-
the bifunctional HPPK-DHPS enzyme catalyzes sequential steps in the folate biosynthesis, i.e. the 6-hydroxymethylpterin pyrophosphokinase reaction and the dihydropteroate synthase, DHPS, reaction, EC 2.5.1.15
-
-
?
additional information
?
-
Q7CKD7
HPPK is a key enzyme in the folate-biosynthetic pathway and is essential for microorganisms but absent from mammals
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additional information
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HPPK is a key enzyme in the folate-biosynthetic pathway and is essential for microorganisms but absent from mammals
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
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required for binding of nucleotides and for the binding of 6-hydroxymethyl-7,8-dihydropteridine
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-Amino-4-hydroxy-6-carboxydihydropteridine
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competitive with 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine
2-amino-6-[(2-[4-[5-(6-amino-purin-9-yl)-3,4-dihydroxy-tetrahydrofuran-2-ylmethylsulfanyl]-piperidin-1-yl]-ethylamino)-methyl]-3H-pteridin-4-one
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2-amino-6-[(2-[4-[5-(6-amino-purin-9-yl)-3,4-dihydroxy-tetrahydrofuran-2-ylmethylsulfanyl]-piperidin-1-yl]-ethylamino)-methyl]-7,7-dimethyl-7,8-dihydro-3H-pteridin-4-one
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2-amino-7,7-dimethyl-4-oxo-3,4,7,8-tetrahydro-pteridine-6-carboxylic acid (2-(2-[5-(6-amino-purin-9-yl)-3,4-dihydroxy-tetrahydro-furan-2-ylmethanesulfonyl]-thylcarbamoyl)-ethyl)-amide
2-amino-7,7-dimethyl-4-oxo-3,4,7,8-tetrahydro-pteridine-6-carboxylic acid (2-(2-[5-(6-amino-purin-9-yl)-3,4-dihydroxy-tetrahydro-furan-2-ylmethanesulfonyl]-thylcarbamoyl)-ethyl)-amide, structure of the enzyme complex with HP-26. HP-26 has significant isozyme selectivity. HP-26 is an excellent lead for developing therapeutic agents for tularemia
2-amino-7,7-dimethyl-4-oxo-3,4,7,8-tetrahydro-pteridine-6-carboxylic acid (2-[4-[5-(6-amino-purin-9-yl)-3,4-dihydroxy-tetrahydro-furan-2-ylmethylsulfanyl]-piperidin-1-yl]-ethyl)-amide
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2-amino-7,7-dimethyl-4-oxo-3,4,7,8-tetrahydropteridine-6-carboxylic acid (2-[2-[5-(6-amino-purin-9-yl)-3,4-dihydroxy-tetrahydro-furan-2-ylmethanesulfonyl]-ethylcarbamoyl]-ethyl)-amide
about 45% residual activity at 0.01 mM, about 30% residual activity at 0.02 mM, about 15% residual activity at 0.05 mM, almost complete inhibition at 0.1 mM
2-amino-8-[2-(2-methylphenyl)-2-oxoethoxy]-1,4,5,9-tetrahydro-6H-purin-6-one
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2-amino-8-[2-(3-methylphenyl)-2-oxoethoxy]-1,4,5,9-tetrahydro-6H-purin-6-one
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2-amino-8-[2-(4-fluorophenyl)-2-oxoethoxy]-1,4,5,9-tetrahydro-6H-purin-6-one
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2-amino-8-[2-(4-hydroxyphenyl)-2-oxoethoxy]-1,4,5,9-tetrahydro-6H-purin-6-one
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2-amino-8-[2-(4-methoxyphenyl)-2-oxoethoxy]-1,4,5,9-tetrahydro-6H-purin-6-one
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2-amino-8-[2-(4-methylphenyl)-2-oxoethoxy]-1,4,5,9-tetrahydro-6H-purin-6-one
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2-amino-8-[[(2-fluorophenyl)methyl]sulfanyl]-1,9-dihydro-6H-purin-6-one
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compound shows high binding affinity. The guanine moiety interacts with the binding pocket residues through hydrogen bond interaction with residues T43, A44, V46, N56, R121 and is further stabilized by pi-stacking interaction between the aromatic rings of F54 and F123
2-amino-8-[[2-(4-methoxyphenyl)-2-oxoethyl]sulfanyl]-1,9-dihydro-6H-purin-6-one
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compound forms hydrogen bond and pi-pi interactions between the guanine moiety and the binding site residues. The imidazole-NH forms a hydrogen bond interaction with residue V46. The atoms in the pyrimidine ring interact with a cluster of residues including T43, A44, V46, F54, N56 and F123
4-[(2-amino-6-oxo-4,5,6,9-tetrahydro-1H-purin-8-yl)methyl]benzonitrile
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4-[[(2-amino-6-oxo-4,5,6,9-tetrahydro-1H-purin-8-yl)oxy]acetyl]benzonitrile
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5'-(1-[2-[(2-amino-7,7-dimethyl-4-oxo-3,4,7,8-tetrahydropteridine-6-carbonyl)amino]ethyl]-2-carboxypiperidine-4-sulfonyl)-5'-deoxyadenosine
bisubstrate inhibitor, Kd value is 0.000047 microM, compound is not sufficiently stable under the experimental conditions
5'-S-(1-[2-[(2-amino-7,7-dimethyl-4-oxo-3,4,7,8-tetrahydropteridine-6-carbonyl)amino]ethyl]-2-carboxypiperidin-4-yl)-5'-thioadenosine
bisubstrate inhibitor, the carboxylic group in the piperidine system mimics the gamma-phosphate of AMPCPP and the carboxylic group interacts with the side chains of H115, Y116, and R121
5'-S-[1-(2-([(2-amino-7,7-dimethyl-4-oxo-3,4,7,8-tetrahydropteridin-6-yl)carbonyl]amino)ethyl)piperidin-4-yl]-5'-thioadenosine
5'-S-[1-(2-([(2-amino-7,7-dimethyl-4-oxo-3,4,7,8-tetrahydropteridin-6-yl)carbonyl]amino)ethyl)piperidin-4-yl]-5'-thioadenosine, structure of the enzyme complex with HP-18. HP-18 has significant isozyme selectivity
5'-S-[1-(2-{[(2-amino-7,7-dimethyl-4-oxo-3,4,7,8-tetrahydropteridin-6-yl)carbonyl]amino}ethyl)piperidin-4-yl]-5'-thioadenosine
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6-hydroxymethyl-7,8-dihydropterin diphosphate
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competitive inhibitor of ATP, mixed type inhibitor of 6-hydroxymethyl-7,8-dihydropteridine
alpha,beta-methyleneadenosine triphosphate
competitive with respect to ATP
sulfadimethoxine
inhibition of dihydropteroate synthase activity
sulfamonomethoxine
inhibition of dihydropteroate synthase activity
2-(((2-amino-6-oxo-6,9-dihydro-1H-purin-8-yl)thio)methyl)-5-fluorobenzonitrile
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2-(((2-amino-6-oxo-6,9-dihydro-1H-purin-8-yl)thio)methyl)-5-fluorobenzonitrile
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2-(((2-amino-6-oxo-6,9-dihydro-1H-purin-8-yl)thio)methyl)-benzonitrile
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2-(((2-amino-6-oxo-6,9-dihydro-1H-purin-8-yl)thio)methyl)-benzonitrile
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2-((2-amino-6-oxo-6,9-dihydro-1H-purin-8-yl)thio)-N,N-diethylacetamide
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2-((2-amino-6-oxo-6,9-dihydro-1H-purin-8-yl)thio)-N,N-diethylacetamide
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