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Information on EC 4.1.2.25 - dihydroneopterin aldolase and Organism(s) Mycobacterium tuberculosis and UniProt Accession P9WNG5

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.2 Aldehyde-lyases
                4.1.2.25 dihydroneopterin aldolase
IUBMB 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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This record set is specific for:
Mycobacterium tuberculosis
UNIPROT: P9WNG5
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Word Map
The taxonomic range for the selected organisms is: Mycobacterium tuberculosis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
dihydroneopterin aldolase, dhna-hppk, rv3607c, dihydroneopterin aldolase/epimerase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dihydroneopterin aldolase/epimerase
-
aldolase, dihydroneopterin
-
-
-
-
FASA
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
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].
CAS REGISTRY NUMBER
COMMENTARY hide
37290-59-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
7,8-dihydroneopterin + 7,8-dihydromonapterin
show the reaction diagram
-
-
-
r
7,8-dihydroneopterin
6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde
show the reaction diagram
-
-
-
r
6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
7,8-dihydroneopterin + 7,8-dihydromonapterin
show the reaction diagram
-
reaction is reversible, and C-C bond formation has both 7,8-dihydroneopterin and 7,8-dihydromonapterin as products plus 7,8-dihydroxanthopterin
-
r
7,8-dihydromonapterin
6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
show the reaction diagram
-
-
-
r
7,8-dihydroneopterin
6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
show the reaction diagram
-
-
-
r
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
7,8-dihydroneopterin + 7,8-dihydromonapterin
show the reaction diagram
-
-
-
r
7,8-dihydroneopterin
6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde
show the reaction diagram
-
-
-
r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00017
7,8-dihydromonapterin
pH 7.0, 22°C
0.00016
7,8-dihydroneopterin
pH 7.0, 22°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.006
7,8-dihydromonapterin
pH 7.0, 22°C
0.0054
7,8-dihydroneopterin
pH 7.0, 22°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
38
7,8-dihydromonapterin
pH 7.0, 22°C
36
7,8-dihydroneopterin
pH 7.0, 22°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16585
apo-enzyme, 4 * 16585, and octamer for 7,8-dihydroxanthopterin-bound form, 8 * 16585, mass spectrometry
62300
apo-enzyme, mass spectrometry
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 14412, calculated from amino acid sequence
tetramer
apo-enzyme, 4 * 16585, and octamer for 7,8-dihydroxanthopterin-bound form, 8 * 16585, mass spectrometry
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team