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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-(L-threo-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
?
6-hydroxymethyl-7,8-dihydropterin
?
6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
7,8-dihydroneopterin + 7,8-dihydromonapterin
7,8-dihydro-L-monapterin
?
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
additional information
?
-
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
-
-
-
?
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
?
-
-
-
-
?
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
?
-
-
-
-
?
6-hydroxymethyl-7,8-dihydropterin
?
-
-
-
-
?
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-dihydro-L-monapterin
?
-
-
-
-
?
7,8-dihydro-L-monapterin
?
-
-
-
-
?
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-Dihydromonapterin
?
-
-
-
-
?
7,8-Dihydromonapterin
?
-
-
-
-
?
7,8-Dihydromonapterin
?
-
-
-
-
?
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
?
-
-
enzyme in folate biosynthesis
-
?
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
?
-
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-Amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
?
6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
7,8-dihydroneopterin + 7,8-dihydromonapterin
7,8-dihydroneopterin
6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde
7,8-dihydroneopterin
6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
additional information
?
-
-
enzyme in folate biosynthesis
-
?
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
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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2-Amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine
-
competitive
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
6-Formyl-dihydropterin
-
-
6-Methyl-dihydropterin
-
-
7,8-dihydrobiopterin
-
builds a complex with the enzyme
Dihydropteroic acid
-
slight
additional information
-
not inhibited by EDTA
-
dihydrofolic acid
-
slight
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.0023 - 0.064
2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
0.00076 - 9.8
7,8-dihydro-L-monapterin
0.00017 - 0.057
7,8-dihydromonapterin
0.00016 - 9.7
7,8-dihydroneopterin
10
glycoaldehyde
-
apparent value
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)
0.00017
7,8-dihydromonapterin
pH 7.0, 22°C
0.016
7,8-dihydromonapterin
-
cleavage
0.019
7,8-dihydromonapterin
-
epimerization
0.036
7,8-dihydromonapterin
-
cleavage
0.057
7,8-dihydromonapterin
-
epimerization
0.00016
7,8-dihydroneopterin
pH 7.0, 22°C
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)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0000023 - 0.089
7,8-dihydro-L-monapterin
0.006
7,8-dihydromonapterin
pH 7.0, 22°C
0.0000022 - 1
7,8-dihydroneopterin
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)
0.0000093
7,8-dihydroneopterin
-
mutant enzyme E22A, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)
0.000016
7,8-dihydroneopterin
-
mutant enzyme K100Q, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)
0.00073
7,8-dihydroneopterin
-
mutant enzyme E73A, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)
0.0054
7,8-dihydroneopterin
pH 7.0, 22°C
0.045
7,8-dihydroneopterin
-
wild type enzyme, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)
0.048
7,8-dihydroneopterin
-
mutant enzyme Q61A, at pH 7.6 and 70°C
0.054
7,8-dihydroneopterin
-
mutant enzyme Y78F, at pH 7.6 and 70°C
0.055
7,8-dihydroneopterin
-
mutant enzyme H35N, at pH 7.6 and 70°C
0.07
7,8-dihydroneopterin
-
wild type enzyme, at pH 7.6 and 25°C
0.082
7,8-dihydroneopterin
-
wild type enzyme, in 100 mM Tris-HCl, 1 mM EDTA, and 5 mM dithiothreitol (pH 8.3)
0.64
7,8-dihydroneopterin
-
mutant enzyme Y111F, at pH 7.6 and 70°C
0.68
7,8-dihydroneopterin
-
mutant enzyme E25Q, at pH 7.6 and 70°C
1
7,8-dihydroneopterin
-
wild type enzyme, at pH 7.6 and 70°C
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0.00074
3-(5-amino-7-hydroxy-[1,2,3]triazolo[4,5-d]pyrimidin-2-yl)-N-(1-hydroxycyclohexylmethyl)benzamide
Staphylococcus aureus
-
IC50: 0.00074 mM
0.00095
3-(5-amino-7-hydroxy-[1,2,3]triazolo[4,5-d]pyrimidin-2-yl)-N-(2,2-bis-hydroxymethylbutyl)benzamide
Staphylococcus aureus
-
IC50: 0.00095 mM
0.00055
3-(5-amino-7-hydroxy-[1,2,3]triazolo[4,5-d]pyrimidin-2-yl)-N-(2,3-dihydrobenzofuran-5-ylmethyl)benzamide
Staphylococcus aureus
-
IC50: 0.00055 mM
0.001
3-(5-amino-7-hydroxy-[1,2,3]triazolo[4,5-d]pyrimidin-2-yl)-N-(3,5-bistrifluoromethylbenzyl)benzamide
Staphylococcus aureus
-
IC50: 0.001 mM
0.000068
3-(5-amino-7-hydroxy-[1,2,3]triazolo[4,5-d]pyrimidin-2-yl)-N-(3,5-dichlorobenzyl)benzamid
Staphylococcus aureus
-
IC50: 0.000068 mM
0.00073
3-(5-amino-7-hydroxy-[1,2,3]triazolo[4,5-d]pyrimidin-2-yl)-N-(3-hydroxy-2,2-dimethylpropyl)benzamide
Staphylococcus aureus
-
IC50: 0.00073 mM
0.0023
3-(5-amino-7-hydroxy-[1,2,3]triazolo[4,5-d]pyrimidin-2-yl)-N-(3-hydroxypropyl)benzamide
Staphylococcus aureus
-
IC50: 0.0023 mM
0.002
3-(5-amino-7-hydroxy-[1,2,3]triazolo[4,5-d]pyrimidin-2-yl)-N-(4-hydroxybutyl)benzamide
Staphylococcus aureus
-
IC50: 0.002 mM
0.022
3-(5-amino-7-hydroxy-[1,2,3]triazolo[4,5-d]pyrimidin-2-yl)-N-(4-phenoxybenzyl)benzamide
Staphylococcus aureus
-
IC50: 0.022 mM
0.00031
3-(5-amino-7-hydroxy-[1,2,3]triazolo[4,5-d]pyrimidin-2-yl)-N-benzo[1,3]dioxol-5-ylmethylbenzamide
Staphylococcus aureus
-
IC50: 0.00031 mM
0.025
3-(5-amino-7-hydroxy-[1,2,3]triazolo[4,5-d]pyrimidin-2-yl)-N-biphenyl-4-ylmethylbenzamide
Staphylococcus aureus
-
IC50: 0.025 mM
0.00035
3-(5-amino-7-hydroxy-[1,2,3]triazolo[4,5-d]pyrimidin-2-yl)-N-cis-(2-hydroxycycloheptylmethyl)benzamide
Staphylococcus aureus
-
IC50: 0.00035 mM
0.00041
3-(5-amino-7-hydroxy-[1,2,3]triazolo[4,5-d]pyrimidin-2-yl)-N-cis-(2-hydroxycyclohexylmethyl)benzamide
Staphylococcus aureus
-
IC50: 0.00041 mM
0.00032
3-(5-amino-7-hydroxy-[1,2,3]triazolo[4,5-d]pyrimidin-2-yl)-N-trans-(2-hydroxycyclohexylmethyl)benzamide
Staphylococcus aureus
-
IC50: 0.00032 mM
0.00003
3-(5-amino-7-hydroxy-[1,2,3]triazolo[4,5-d]pyrimidin-2-yl)-N-[2-(2-hydroxymethylphenylsulfanyl)benzyl]-benzamide
Staphylococcus aureus
-
IC50: 0.00003 mM
0.0015
3-(5-amino-7-hydroxy-[1,2,3]triazolo[4,5-d]pyrimidin-2-yl)benzoic acid
Staphylococcus aureus
-
IC50: 0.0015 mM
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110000
-
sedimentation equilibrium centrifugation
119000
-
independent monofunctional activity FasAB-Met23, gel filtration
12456
-
8 * 12456, calculation from nucleotide sequence
13577
-
8 * 13577, calculation from nucleotide sequence
13600
x * 14685, calculated, x * 13600, SDS-PAGE
13751
-
8 * 13751, calculation from nucleotide sequence
14000
8 * 14000, gel filtration
14100
x * 16300, calculated, x * 14100, SDS-PAGE of truncated recombinant protein
14685
x * 14685, calculated, x * 13600, SDS-PAGE
16300
x * 16300, calculated, x * 14100, SDS-PAGE of truncated recombinant protein
16585
apo-enzyme, 4 * 16585, and octamer for 7,8-dihydroxanthopterin-bound form, 8 * 16585, mass spectrometry
29689
-
4 * 29689, independent monofunctional activity FasAB-Met23, mass spectrometry
62300
apo-enzyme, mass spectrometry
71500
-
x * 71500, Fas multifunctional enzyme with the activity of the first three enzymes of the folate synthesis pathway: dihydroneopterin aldolase, hydroxymethyldihydropterin pyrophosphokinase and dihydropteroate synthase, SDS-PAGE
83979
-
x * 83979, multifunctional Fas enzyme with the activity of the first three enzymes of the folate synthesis pathway: dihydroneopterin aldolase, hydroxymethyldihydropterin pyrophosphokinase and dihydropteroate synthase, calculation from nucleotide sequence
100000
-
gel filtration
100000
-
x * 100000, SDS-PAGE
104000
-
equilibrium sedimentation
104000
-
equilibrium sedimentation
14600
-
8 * 14600, gel filtration
14600
-
x * 14600, SDS-PAGE
31000
-
or tetramer, 4 * or 3 * 31000, bifunctional enzyme with dihydroneopterin aldolase activity and hydroxymethyldihydropterin pyrophosphokinase activity, dihydroneopterin aldolase activity requires the multimeric protein, whereas pyrophosphokinase is expressed by the monomeric form, SDS-PAGE
31000
-
or trimer, 3 * or 4 * 31000, bifunctional enzyme with dihydroneopterin aldolase activity and hydroxymethyldihydropterin pyrophosphokinase activity, dihydroneopterin aldolase activity requires the multimeric protein, whereas pyrophosphokinase is expressed by the monomeric form, SDS-PAGE
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Mathis, J.B.; Brown, G.M.
Dihydroneopterin aldolase from Escherichia coli
Methods Enzymol.
66
556-560
1980
Escherichia coli
brenda
Mathis, J.B.; Brown, G.M.
The biosynthesis of folic acid. XI. Purification and properties of dihydroneopterin aldolase
J. Biol. Chem.
245
3015-3025
1970
Escherichia coli, Escherichia coli B / ATCC 11303
brenda
Volpe, F.; Ballantine, S.P.; Delves, C.J.
Two domains with amino-acid sequence similarity are required for dihydroneopterin aldolase function in the multifunctional folic acid synthesis Fas protein of Pneumocystis carnii
Gene
160
41-46
1995
Pneumocystis carinii
brenda
Thomas, M.C.; Ballantine, S.P.; Bethell, S.S.; Bains, S.; Kellam, P.; Delves, C.J.
Single amino acid substitutions dirupts tetramer formation in the dihydroneopterin aldolase enzyme of Pneumocystis carnii
Biochemistry
37
11629-11636
1998
Pneumocystis carinii
brenda
Lopez, P.; Lacks, S.A.
A bifunctional protein in the folate biosynthetic pathway of Streptococcus pneumoniae with dihydroneopterin aldolase and hydroxymethyldihydropterin pyrophosphokinase activities
J. Bacteriol.
175
2214-2220
1993
Streptococcus pneumoniae
brenda
Volpe, F.; Ballantine, S.P.; Delves, C.J.
The multifunctional folic acid synthesis fas gene of Pneumocystis carinii encodes dihydroneopterin aldolase, hydroxymethyldihydropterin pyrophosphokinase and dihydropteroate synthase
Eur. J. Biochem.
216
449-458
1993
no activity in mammalia, Pneumocystis carinii
brenda
Haumann, C.; Rohdich, F.; Schmidt, E.; Bacher, A.; Richter, G.
Biosynthesis of pteridines in Escherichia coli. Structural and mechanistic similarity of dihydroneopterin-triphosphate epimerase and dihydroneopterin aldolase
J. Biol. Chem.
273
17418-17424
1998
Escherichia coli, Haemophilus influenzae
brenda
Hennig, M.; D'Arcy, A.; Hampele, I.C.; Page, M.G.P.; Oefner, C.; Dale, G.E.
Crystal structure and reaction mechanism of 7,8-dihydroneopterin aldolase from Staphylococcus aureus
Nat. Struct. Biol.
5
357-362
1998
Staphylococcus aureus
brenda
Deng, H.; Callender, R.; Dale, G.E.
A vibrational structure of 7,8-dihydrobiopterin bound to dihydroneopterin aldolase
J. Biol. Chem.
275
30139-30143
2000
Escherichia coli
brenda
Illarionova, V.; Eisenreich, W.; Fischer, M.; Haussmann, C.; Romisch, W.; Richter, G.; Bacher, A.
Biosynthesis of tetrahydrofolate. Stereochemistry of dihydroneopterin aldolase
J. Biol. Chem.
277
28841-28847
2002
Escherichia coli
brenda
Goyer, A.; Illarionova, V.; Roje, S.; Fischer, M.; Bacher, A.; Hanson, A.D.
Folate biosynthesis in higher plants. cDNA cloning, heterologous expression, and characterization of Dihydroneopterin aldolases
Plant Physiol.
135
103-111
2004
Arabidopsis thaliana, Arabidopsis thaliana (Q9FM54), Arabidopsis thaliana (Q9SF23), Solanum lycopersicum
brenda
Scherperel, G.; Yan, H.; Wang, Y.; Reid, G.E.
'Top-down' characterization of site-directed mutagenesis products of Staphylococcus aureus dihydroneopterin aldolase by multistage tandem mass spectrometry in a linear quadrupole ion trap
Analyst
131
291-302
2006
Staphylococcus aureus
brenda
Sanders, W.J.; Nienaber, V.L.; Lerner, C.G.; McCall, J.O.; Merrick, S.M.; Swanson, S.J.; Harlan, J.E.; Stoll, V.S.; Stamper, G.F.; Betz, S.F.; Condroski, K.R.; Meadows, R.P.; Severin, J.M.; Walter, K.A.; Magdalinos, P.; Jakob, C.G.; Wagner, R.; Beutel, B.A.
Discovery of potent inhibitors of dihydroneopterin aldolase using CrystaLEAD high-throughput X-ray crystallographic screening and structure-directed lead optimization
J. Med. Chem.
47
1709-1718
2004
Staphylococcus aureus
brenda
Bauer, S.; Schott, A.K.; Illarionova, V.; Bacher, A.; Huber, R.; Fischer, M.
Biosynthesis of tetrahydrofolate in plants: crystal structure of 7,8-dihydroneopterin aldolase from Arabidopsis thaliana reveals a novel adolase class
J. Mol. Biol.
339
967-979
2004
Arabidopsis thaliana (Q9SF23), Arabidopsis thaliana
brenda
Garcon, A.; Levy, C.; Derrick, J.P.
Crystal structure of the bifunctional dihydroneopterin aldolase/6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase from Streptococcus pneumoniae
J. Mol. Biol.
360
644-653
2006
Streptococcus pneumoniae
brenda
Wang, Y.; Li, Y.; Yan, H.
Mechanism of dihydroneopterin aldolase: functional roles of the conserved active site glutamate and lysine residues
Biochemistry
45
15232-15239
2006
Escherichia coli, Staphylococcus aureus
brenda
Wang, Y.; Li, Y.; Wu, Y.; Yan, H.
Mechanism of dihydroneopterin aldolase. NMR, equilibrium and transient kinetic studies of the Staphylococcus aureus and Escherichia coli enzymes
FEBS J.
274
2240-2252
2007
Escherichia coli, Staphylococcus aureus
brenda
Wang, Y.; Scherperel, G.; Roberts, K.D.; Jones, A.D.; Reid, G.E.; Yan, H.
A point mutation converts dihydroneopterin aldolase to a cofactor-independent oxygenase
J. Am. Chem. Soc.
128
13216-13223
2006
Escherichia coli, Staphylococcus aureus
brenda
Blaszczyk, J.; Li, Y.; Gan, J.; Yan, H.; Ji, X.
Structural basis for the aldolase and epimerase activities of Staphylococcus aureus dihydroneopterin aldolase
J. Mol. Biol.
368
161-169
2007
Staphylococcus aureus (P56740), Staphylococcus aureus
brenda
Yao, L.; Yan, H.; Cukier, R.I.
Mechanism of dihydroneopterin aldolase: a molecular dynamics study of the apo enzyme and its product complex
J. Phys. Chem. B
110
1443-1456
2006
Staphylococcus aureus
brenda
Dittrich, S.; Mitchell, S.L.; Blagborough, A.M.; Wang, Q.; Wang, P.; Sims, P.F.; Hyde, J.E.
An atypical orthologue of 6-pyruvoyltetrahydropterin synthase can provide the missing link in the folate biosynthesis pathway of malaria parasites
Mol. Microbiol.
67
609-618
2008
Escherichia coli, no activity in Plasmodium falciparum
brenda
Hyde, J.E.; Dittrich, S.; Wang, P.; Sims, P.F.; de Crecy-Lagard, V.; Hanson, A.D.
Plasmodium falciparum: a paradigm for alternative folate biosynthesis in diverse microorganisms?
Trends Parasitol.
24
502-508
2008
Plasmodium falciparum
brenda
Pribat, A.; Jeanguenin, L.; Lara-Nunez, A.; Ziemak, M.J.; Hyde, J.E.; de Crecy-Lagard, V.; Hanson, A.D.
6-Pyruvoyltetrahydropterin synthase paralogs replace the folate synthesis enzyme dihydroneopterin aldolase in diverse bacteria
J. Bacteriol.
191
4158-4165
2009
Escherichia coli, Escherichia coli MG1655
brenda
Waller, J.C.; Akhtar, T.A.; Lara-Nunez, A.; Gregory, J.F.; McQuinn, R.P.; Giovannoni, J.J.; Hanson, A.D.
Developmental and feedforward control of the expression of folate biosynthesis genes in tomato fruit
Mol. Plant
3
66-77
2010
Solanum lycopersicum
brenda
Almeida, R.; Loss, O.; Colabardini, A.; Brown, N.; Bignell, E.; Savoldi, M.; Pantano, S.; Goldman, M.; Arst Jr., E.; Goldman, G.
Genetic bypass of Aspergillus nidulans crzA function in calcium homeostasis
G3 (Bethesda)
3
1129-1141
2013
Aspergillus nidulans
brenda
Czekster, C.M.; Blanchard, J.S.
One substrate, five products: reactions catalyzed by the dihydroneopterin aldolase from Mycobacterium tuberculosis
J. Am. Chem. Soc.
134
19758-19771
2012
Mycobacterium tuberculosis (P9WNC5), Mycobacterium tuberculosis
brenda
Falcao, V.C.; Villela, A.D.; Rodrigues-Junior, V.S.; Pissinate, K.; Eichler, P.; Pinto, A.F.; Basso, L.A.; Santos, D.S.; Bizarro, C.V.
Validation of Mycobacterium tuberculosis dihydroneopterin aldolase as a molecular target for anti-tuberculosis drug development
Biochem. Biophys. Res. Commun.
485
814-819
2017
Mycobacterium tuberculosis (P9WNG5), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WNG5)
brenda
Chaudhary, B.; Singh, N.; Pandey, D.K.
Bioengineering of crop plants for improved tetrahydrofolate production
Bioengineered
9
152-158
2018
Escherichia coli (P0AC16)
brenda
Blaszczyk, J.; Lu, Z.; Li, Y.; Yan, H.; Ji, X.
Crystallographic and molecular dynamics simulation analysis of Escherichia coli dihydroneopterin aldolase
Cell Biosci.
4
52
2014
Escherichia coli (P0AC16), Escherichia coli
brenda
Wang, Y.; Xu, H.; Grochowski, L.L.; White, R.H.
Biochemical characterization of a dihydroneopterin aldolase used for methanopterin biosynthesis in methanogens
J. Bacteriol.
196
3191-3198
2014
Methanocaldococcus jannaschii, Methanocaldococcus jannaschii MJ0408
brenda
Pandey, D.K.; Kumar, A.; Rathore, J.S.; Singh, N.; Chaudhary, B.
Recombinant overexpression of dihydroneopterin aldolase catalyst potentially regulates folate-biofortification
J. Basic Microbiol.
57
517-524
2017
Escherichia coli (P0AC16)
brenda