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Information on EC 4.1.2.25 - dihydroneopterin aldolase
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4.1.2.25 dihydroneopterin aldolaseIUBMB Comments
The enzyme participates in folate (in bacteria, plants and fungi) and methanopterin (in archaea) biosynthesis. The enzymes from the bacterium Escherichia coli and the plant Arabidopsis thaliana also catalyse the epimerisation of the 2' hydroxy-group (EC 5.1.99.8, 7,8-dihydroneopterin epimerase) [2,3]. The enzyme from the bacterium Mycobacterium tuberculosis is trifunctional and also catalyses EC 5.1.99.8 and EC 1.13.11.81, 7,8-dihydroneopterin oxygenase . The enzyme from the yeast Saccharomyces cerevisiae also catalyses the two subsequent steps in the folate biosynthesis pathway - EC 2.7.6.3, 2-amino-4-hydroxy-6-(hydroxymethyl)dihydropteridine diphosphokinase, and EC 2.5.1.15, dihydropteroate synthase .
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Word Map
- 4.1.2.25
- folate
-
dhnas
- 6-hydroxymethyl-7,8-dihydropterin
-
folic
-
pyrophosphokinase
- dihydropteroate
- pteridine
-
cyclohydrolase
- tetrahydrofolate
- pneumocystis
-
hydroxymethyldihydropterin
-
epimerization
- tetrahydrobiopterin
- carinii
- aldolases
-
octamer
- antifolate
- medicine
- pharmacology
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
dihydroneopterin aldolase, dhna-hppk, dihydroneopterin aldolase/epimerase, rv3607c, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aldolase, dihydroneopterin
-
-
-
-
DHNA
DHNA-HPPK
-
DHNA is part of the bifunctional dihydroneopterin aldolase/6 hydroxymethyl-7,8-dihydropterin pyrophosphokinase, also called SulD
dihydroneopterin aldolase
dihydroneopterin aldolase/epimerase
FASA
-
-
-
-
FolB
FolB1
MptD
Rv3607c
DHNA
-
-
-
-
DHNA
-
DHNA catalyzes both the cleavage of 7,8-dihydroneopterin to form 6-hydroxymethyl-7,8-dihydropterin and glycolaldehyde and the epimerization of 7,8-dihydroneopterin to form 7,8-dihydro-l-monapterin
DHNA
-
DHNA catalyzes both the cleavage of 7,8-dihydroneopterin to form 6-hydroxymethyl-7,8-dihydropterin and glycolaldehyde and the epimerization of 7,8-dihydroneopterin to form 7,8-dihydro-l-monapterin
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
7,8-dihydroneopterin = 6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde
mechanism
-
7,8-dihydroneopterin = 6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde
mechanism
-
7,8-dihydroneopterin = 6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde
polarization of the 2'-hydroxy group of the substrate can serve as the initial reaction step for the aldolase
-
7,8-dihydroneopterin = 6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde
polarization of the 2'-hydroxy group of the substrate can serve as the initial reaction step for the aldolase
-
-
7,8-dihydroneopterin = 6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
-
-
of an aldehyde, C-C bond cleavage
-
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PATHWAY SOURCE
PATHWAYS
KEGG
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SYSTEMATIC NAME
IUBMB Comments
7,8-dihydroneopterin glycolaldehyde-lyase [6-(hydroxymethyl)-7,8-dihydropterin-forming]
The enzyme participates in folate (in bacteria, plants and fungi) and methanopterin (in archaea) biosynthesis. The enzymes from the bacterium Escherichia coli and the plant Arabidopsis thaliana also catalyse the epimerisation of the 2' hydroxy-group (EC 5.1.99.8, 7,8-dihydroneopterin epimerase) [2,3]. The enzyme from the bacterium Mycobacterium tuberculosis is trifunctional and also catalyses EC 5.1.99.8 and EC 1.13.11.81, 7,8-dihydroneopterin oxygenase [6]. The enzyme from the yeast Saccharomyces cerevisiae also catalyses the two subsequent steps in the folate biosynthesis pathway - EC 2.7.6.3, 2-amino-4-hydroxy-6-(hydroxymethyl)dihydropteridine diphosphokinase, and EC 2.5.1.15, dihydropteroate synthase [4].
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CAS REGISTRY NUMBER
COMMENTARY
37290-59-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + glycolaldehyde
6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
7,8-dihydroneopterin + 7,8-dihydromonapterin
2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + glycolaldehyde
-
-
-
?
2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + glycolaldehyde
-
-
-
?
2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + glycolaldehyde
-
not reversible
-
?
2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + glycolaldehyde
Escherichia coli B / ATCC 11303
-
-
-
?
2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + glycolaldehyde
-
-
-
?
2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + glycolaldehyde
-
-
-
?
2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + glycolaldehyde
-
-
-
?
2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + glycolaldehyde
-
-
-
?
2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + glycolaldehyde
-
-
-
?
2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + glycolaldehyde
-
-
-
?
2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + glycolaldehyde
-
-
-
?
2-Amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
?
-
enzyme is involved in the biosynthetic pathway of tetrahydrofolate
-
-
?
2-Amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
?
-
enzyme is involved in the biosynthetic pathway of tetrahydrofolate
-
-
?
2-Amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
?
-
first enzyme in the folate synthesis pathway
-
-
?
2-Amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
?
-
the enzyme is involved in the de novo synthesis of folic acid from guanosine triphosphate
-
-
?
2-Amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
?
-
first enzyme in the folate synthesis pathway
-
-
?
2-amino-4-hydroxy-6-(L-threo-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
?
-
-
-
-
?
2-amino-4-hydroxy-6-(L-threo-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
?
Escherichia coli B / ATCC 11303
-
-
-
-
?
2-amino-4-hydroxy-6-(L-threo-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
?
-
-
-
-
?
2-amino-4-hydroxy-6-(L-threo-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
?
-
-
-
-
?
6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
7,8-dihydroneopterin + 7,8-dihydromonapterin
-
-
-
r
6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
7,8-dihydroneopterin + 7,8-dihydromonapterin
-
-
-
-
r
6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
7,8-dihydroneopterin + 7,8-dihydromonapterin
-
-
-
-
r
6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
7,8-dihydroneopterin + 7,8-dihydromonapterin
-
-
-
r
6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
7,8-dihydroneopterin + 7,8-dihydromonapterin
-
reaction is reversible, and C-C bond formation has both 7,8-dihydroneopterin and 7,8-dihydromonapterin as products plus 7,8-dihydroxanthopterin
-
r
6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
7,8-dihydroneopterin + 7,8-dihydromonapterin
-
-
-
r
7,8-dihydromonapterin
6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
-
-
-
?
7,8-dihydromonapterin
6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
-
-
-
r
7,8-dihydromonapterin
6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
-
-
-
-
?
7,8-dihydroneopterin
6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde
-
-
-
?
7,8-dihydroneopterin
6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde
-
-
-
r
7,8-dihydroneopterin
6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde
-
-
-
-
r
7,8-dihydroneopterin
6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde
-
-
-
-
r
7,8-dihydroneopterin
6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde
-
-
-
r
7,8-dihydroneopterin
6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde
-
-
-
r
7,8-dihydroneopterin
6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
-
-
?
7,8-dihydroneopterin
6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
-
-
-
?
7,8-dihydroneopterin
6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
-
-
-
?
7,8-dihydroneopterin
6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
-
-
-
-
?
7,8-dihydroneopterin
6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
-
-
-
-
r
7,8-dihydroneopterin
6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
-
protonation of the reaction intermediate occurs preferentially in the pro-S-position
-
?
7,8-dihydroneopterin
6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
-
-
-
-
?
7,8-dihydroneopterin
6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
-
-
-
r
7,8-dihydroneopterin
6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
-
-
-
-
?
7,8-dihydroneopterin
6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
-
-
-
?
7,8-dihydroneopterin
6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
-
-
-
-
ir
7,8-dihydroneopterin
6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
-
-
-
-
?
7,8-dihydroneopterin
6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
-
-
-
-
r
7,8-dihydroneopterin
6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
-
-
-
?
7,8-dihydroneopterin
6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
-
-
-
-
?
additional information
?
-
-
enzyme also mediates the epimerisation of 7,8-dihydroneopterin to 7,8-dihydromonapterin
-
?
additional information
?
-
enzyme also mediates the epimerisation of 7,8-dihydroneopterin to 7,8-dihydromonapterin
-
?
additional information
?
-
enzyme also mediates the epimerisation of 7,8-dihydroneopterin to 7,8-dihydromonapterin
-
?
additional information
?
-
-
enzyme catalyzes both the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin, reaction of EC 4.1.2.25, and the epimerization of 7,8-dihydroneopterin to 7,8-dihydromonapterin, it carries out the aldol cleavage reaction on the epimerization product, 7,8-dihydromonapterin, as well as on 7,8-dihydroneopterin
-
-
?
additional information
?
-
enzyme catalyzes both the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin, reaction of EC 4.1.2.25, and the epimerization of 7,8-dihydroneopterin to 7,8-dihydromonapterin, it carries out the aldol cleavage reaction on the epimerization product, 7,8-dihydromonapterin, as well as on 7,8-dihydroneopterin
-
-
?
additional information
?
-
enzyme catalyzes both the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin, reaction of EC 4.1.2.25, and the epimerization of 7,8-dihydroneopterin to 7,8-dihydromonapterin, it carries out the aldol cleavage reaction on the epimerization product, 7,8-dihydromonapterin, as well as on 7,8-dihydroneopterin
-
-
?
additional information
?
-
-
also catalyzes the epimerization of carbon 2' of dihydroneopterin and dihydromonapterin
-
-
?
additional information
?
-
-
no activity with: 2-amino-4-hydroxy-6-(D-threo-1,2,3-trihydroxypropyl)-7,8-dihydropteridine and 2-amino-4-hydroxy-6-(L-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
-
-
?
additional information
?
-
Escherichia coli B / ATCC 11303
-
no activity with: 2-amino-4-hydroxy-6-(D-threo-1,2,3-trihydroxypropyl)-7,8-dihydropteridine and 2-amino-4-hydroxy-6-(L-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
-
-
?
additional information
?
-
-
also catalyzes the epimerization of carbon 2' of dihydroneopterin and dihydromonapterin
-
-
?
additional information
?
-
-
also catalyzes the epimerization of carbon 2' of dihydroneopterin and dihydromonapterin
-
-
?
additional information
?
-
enzyme can utilize both dihydroneopterin and 7,8-dihydromonapterin as substrates to generate 6-hydroxymethyl-7,8-dihydropterin. The reaction generates three different pterin products, one of which is not produced by other wild-type dihydroneopterin aldolases. The enzyme-substrate complex partitions 51% in the first turnover to form the aldolase products, 24% to the epimerase product and 25% to the oxygenase products. The aldolase reaction is strongly pH dependent. Chemistry is rate limiting for the aldolase reaction, and two protons and a likely solvent contribution are involved in formation and breakage of a common intermediate
-
-
?
additional information
?
-
-
enzyme can utilize both dihydroneopterin and 7,8-dihydromonapterin as substrates to generate 6-hydroxymethyl-7,8-dihydropterin. The reaction generates three different pterin products, one of which is not produced by other wild-type dihydroneopterin aldolases. The enzyme-substrate complex partitions 51% in the first turnover to form the aldolase products, 24% to the epimerase product and 25% to the oxygenase products. The aldolase reaction is strongly pH dependent. Chemistry is rate limiting for the aldolase reaction, and two protons and a likely solvent contribution are involved in formation and breakage of a common intermediate
-
-
?
additional information
?
-
-
enzyme also mediates the epimerisation of 7,8-dihydroneopterin to 7,8-dihydromonapterin
-
?
additional information
?
-
-
enzyme catalyzes both the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin, reaction of EC 4.1.2.25, and the epimerization of 7,8-dihydroneopterin to 7,8-dihydromonapterin, it carries out the aldol cleavage reaction on the epimerization product, 7,8-dihydromonapterin, as well as on 7,8-dihydroneopterin
-
-
?
additional information
?
-
enzyme catalyzes both the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin and the epimerization of 7,8-dihydroneopterin to 7,8-dihydromonapterin, reaction of EC 5.1.99.8
-
-
?
additional information
?
-
-
enzyme catalyzes both the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin and the epimerization of 7,8-dihydroneopterin to 7,8-dihydromonapterin, reaction of EC 5.1.99.8
-
-
?
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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 + glycolaldehyde
7,8-dihydroneopterin + 7,8-dihydromonapterin
2-Amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
?
-
enzyme is involved in the biosynthetic pathway of tetrahydrofolate
-
-
?
2-Amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
?
-
enzyme is involved in the biosynthetic pathway of tetrahydrofolate
-
-
?
2-Amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
?
-
first enzyme in the folate synthesis pathway
-
-
?
2-Amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
?
-
the enzyme is involved in the de novo synthesis of folic acid from guanosine triphosphate
-
-
?
2-Amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
?
-
first enzyme in the folate synthesis pathway
-
-
?
6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
7,8-dihydroneopterin + 7,8-dihydromonapterin
-
-
-
r
6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
7,8-dihydroneopterin + 7,8-dihydromonapterin
-
-
-
-
r
6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
7,8-dihydroneopterin + 7,8-dihydromonapterin
-
-
-
-
r
6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
7,8-dihydroneopterin + 7,8-dihydromonapterin
-
-
-
r
6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
7,8-dihydroneopterin + 7,8-dihydromonapterin
-
-
-
r
7,8-dihydroneopterin
6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde
-
-
-
?
7,8-dihydroneopterin
6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde
-
-
-
r
7,8-dihydroneopterin
6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde
-
-
-
-
r
7,8-dihydroneopterin
6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde
-
-
-
-
r
7,8-dihydroneopterin
6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde
-
-
-
r
7,8-dihydroneopterin
6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde
-
-
-
r
7,8-dihydroneopterin
6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
-
-
-
-
?
7,8-dihydroneopterin
6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
-
-
-
-
?
7,8-dihydroneopterin
6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
-
-
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
the metal-independent enzyme is not influenced by Fe2+, Mn2+, Cu2+, Co2+, Ni2+, Mg2+, or Zn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-(5-amino-7-hydroxy-[1,2,3]triazolo[4,5-d]pyrimidin-2-yl)-N-(1-hydroxycyclohexylmethyl)benzamide
-
IC50: 0.00074 mM
3-(5-amino-7-hydroxy-[1,2,3]triazolo[4,5-d]pyrimidin-2-yl)-N-(2,2-bis-hydroxymethylbutyl)benzamide
-
IC50: 0.00095 mM
3-(5-amino-7-hydroxy-[1,2,3]triazolo[4,5-d]pyrimidin-2-yl)-N-(2,3-dihydrobenzofuran-5-ylmethyl)benzamide
-
IC50: 0.00055 mM
3-(5-amino-7-hydroxy-[1,2,3]triazolo[4,5-d]pyrimidin-2-yl)-N-(3,5-bistrifluoromethylbenzyl)benzamide
-
IC50: 0.001 mM
3-(5-amino-7-hydroxy-[1,2,3]triazolo[4,5-d]pyrimidin-2-yl)-N-(3,5-dichlorobenzyl)benzamid
-
IC50: 0.000068 mM
3-(5-amino-7-hydroxy-[1,2,3]triazolo[4,5-d]pyrimidin-2-yl)-N-(3-hydroxy-2,2-dimethylpropyl)benzamide
-
IC50: 0.00073 mM
3-(5-amino-7-hydroxy-[1,2,3]triazolo[4,5-d]pyrimidin-2-yl)-N-(3-hydroxypropyl)benzamide
-
IC50: 0.0023 mM
3-(5-amino-7-hydroxy-[1,2,3]triazolo[4,5-d]pyrimidin-2-yl)-N-(4-hydroxybutyl)benzamide
-
IC50: 0.002 mM
3-(5-amino-7-hydroxy-[1,2,3]triazolo[4,5-d]pyrimidin-2-yl)-N-(4-phenoxybenzyl)benzamide
-
IC50: 0.022 mM
3-(5-amino-7-hydroxy-[1,2,3]triazolo[4,5-d]pyrimidin-2-yl)-N-benzo[1,3]dioxol-5-ylmethylbenzamide
-
IC50: 0.00031 mM
3-(5-amino-7-hydroxy-[1,2,3]triazolo[4,5-d]pyrimidin-2-yl)-N-biphenyl-4-ylmethylbenzamide
-
IC50: 0.025 mM
3-(5-amino-7-hydroxy-[1,2,3]triazolo[4,5-d]pyrimidin-2-yl)-N-cis-(2-hydroxycycloheptylmethyl)benzamide
-
IC50: 0.00035 mM
3-(5-amino-7-hydroxy-[1,2,3]triazolo[4,5-d]pyrimidin-2-yl)-N-cis-(2-hydroxycyclohexylmethyl)benzamide
-
IC50: 0.00041 mM
3-(5-amino-7-hydroxy-[1,2,3]triazolo[4,5-d]pyrimidin-2-yl)-N-trans-(2-hydroxycyclohexylmethyl)benzamide
-
IC50: 0.00032 mM
3-(5-amino-7-hydroxy-[1,2,3]triazolo[4,5-d]pyrimidin-2-yl)-N-[2-(2-hydroxymethylphenylsulfanyl)benzyl]-benzamide
-
IC50: 0.00003 mM
3-(5-amino-7-hydroxy-[1,2,3]triazolo[4,5-d]pyrimidin-2-yl)benzoic acid
-
IC50: 0.0015 mM
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Pneumonia, Pneumocystis
Cloning of the Pneumocystis jirovecii trifunctional FAS gene and complementation of its DHPS activity in Escherichia coli.
Tuberculosis
8-Mercaptoguanine-based inhibitors of Mycobacterium tuberculosis dihydroneopterin aldolase: synthesis, in vitro inhibition and docking studies.
Tuberculosis
One substrate, five products: reactions catalyzed by the dihydroneopterin aldolase from Mycobacterium tuberculosis.
Tuberculosis
Structure based drug discovery for designing leads for the non-toxic metabolic targets in multi drug resistant Mycobacterium tuberculosis.
Tuberculosis
Using property based sequence motifs and 3D modeling to determine structure and functional regions of proteins.
Tuberculosis
Validation of Mycobacterium tuberculosis dihydroneopterin aldolase as a molecular target for anti-tuberculosis drug development.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0023 - 0.064
2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
0.0023
2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
-
-
0.009
2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
-
-
0.021
2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
-
cleavage
0.043
2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
-
epimerization
0.045
2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
-
epimerization
0.064
2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
-
cleavage
0.00076
7,8-dihydro-L-monapterin
-
mutant enzyme E21A, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)
0.0029
7,8-dihydro-L-monapterin
-
mutant enzyme K98A, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)
0.004
7,8-dihydro-L-monapterin
-
mutant enzyme E22A, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)
0.0055
7,8-dihydro-L-monapterin
-
wild type enzyme, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)
0.0095
7,8-dihydro-L-monapterin
-
mutant enzyme K100A, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)
8
7,8-dihydro-L-monapterin
-
wild type enzyme, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)
9.8
7,8-dihydro-L-monapterin
-
mutant enzyme E73A, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)
0.0016
7,8-dihydroneopterin
-
mutant enzyme E21A, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)
0.0024
7,8-dihydroneopterin
-
mutant enzyme K98A, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)
0.0039
7,8-dihydroneopterin
-
mutant enzyme E22A, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)
0.0046
7,8-dihydroneopterin
-
wild type enzyme, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)
0.0058
7,8-dihydroneopterin
-
mutant enzyme K100A, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)
0.0074
7,8-dihydroneopterin
-
wild type enzyme, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)
0.0084
7,8-dihydroneopterin
-
mutant enzyme Q61A, at pH 7.6 and 70°C
0.0099
7,8-dihydroneopterin
-
wild type enzyme, at pH 7.6 and 70°C
0.011
7,8-dihydroneopterin
-
mutant enzyme Y111F, at pH 7.6 and 70°C
0.021
7,8-dihydroneopterin
-
mutant enzyme H35N, at pH 7.6 and 70°C
0.03
7,8-dihydroneopterin
-
mutant enzyme Y78F, at pH 7.6 and 70°C
0.0645
7,8-dihydroneopterin
-
wild type enzyme, at pH 7.6 and 25°C
0.25
7,8-dihydroneopterin
-
Km above 0.25 mM, mutant enzyme E25Q, at pH 7.6 and 70°C
9.7
7,8-dihydroneopterin
-
mutant enzyme E73A, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000023
7,8-dihydro-L-monapterin
-
mutant enzyme E21A, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)
0.0000051
7,8-dihydro-L-monapterin
-
mutant enzyme K100A, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)
0.0000053
7,8-dihydro-L-monapterin
-
mutant enzyme K98A, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)
0.0000057
7,8-dihydro-L-monapterin
-
mutant enzyme K100Q, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)
0.000006
7,8-dihydro-L-monapterin
-
mutant enzyme E73A, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)
0.0000065
7,8-dihydro-L-monapterin
-
mutant enzyme E22A, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)
0.01
7,8-dihydro-L-monapterin
-
wild type enzyme, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)
0.089
7,8-dihydro-L-monapterin
-
wild type enzyme, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)
0.0000022
7,8-dihydroneopterin
-
mutant enzyme K100A, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)
0.0000043
7,8-dihydroneopterin
-
mutant enzyme K98A, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)
0.0000065
7,8-dihydroneopterin
-
mutant enzyme E21A, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3