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Information on EC 1.5.1.34 - 6,7-dihydropteridine reductase and Organism(s) Dictyostelium discoideum and UniProt Accession Q86A17

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EC Tree
IUBMB Comments
The substrate is the quinonoid form of dihydropteridine. Not identical with EC 1.5.1.3 dihydrofolate reductase.
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This record set is specific for:
Dictyostelium discoideum
UNIPROT: Q86A17
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The taxonomic range for the selected organisms is: Dictyostelium discoideum
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
dihydropteridine reductase, quinoid dihydropteridine reductase, nadph-specific dihydropteridine reductase, bmdhpr, dicdhpr, 6,7-dihydropteridine reductase, npra nitroreductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DHPR
-
-
-
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dihydropteridine reductase
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dihydropteridine reductase (NADH)
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-
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NADH-dihydropteridine reductase
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-
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NADPH-dihydropteridine reductase
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-
-
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NADPH-specific dihydropteridine reductase
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-
-
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reductase, dihydropteridine (reduced nicotinamide adenine dinucleotide)
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-
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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-
-
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oxidation
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-
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reduction
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-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
5,6,7,8-tetrahydropteridine:NAD(P)+ oxidoreductase
The substrate is the quinonoid form of dihydropteridine. Not identical with EC 1.5.1.3 dihydrofolate reductase.
CAS REGISTRY NUMBER
COMMENTARY hide
70851-99-9
-
9074-11-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(6R)-L-erythro-dihydrobiopterin + NADH + H+
?
show the reaction diagram
-
-
-
?
6,7-dimethyldihydropterin + NADH + H+
6,7-dimethyltetrahydropterin + NAD+
show the reaction diagram
-
-
-
?
quinonoid (6R)-D-threo-dihydrobiopterin + NADH + H+
?
show the reaction diagram
-
-
-
?
quinonoid dihydrobiopterin + NADH + H+
6R-(1'R,2'R)-5,6,7,8-tetrahydrobiopterin + NAD+
show the reaction diagram
-
-
-
-
?
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
quinonoid dihydrobiopterin + NADH + H+
6R-(1'R,2'R)-5,6,7,8-tetrahydrobiopterin + NAD+
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.04651
NADH
apparent value, in 50 mM Tris-HCl, pH 7.5, at 25°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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enzyme catalyzes the last step of tetrahydrobiopterin recycling
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DHPR_DICDI
231
0
24651
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24600
-
calculated, monomer
25000
-
SDS-PAGE, monomer
50000
-
gel-filtration chromatography (Superdex 200 column), dimer
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 25000, four molecules form 2 dimers in the asymmetric unit in crystals
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
complexed with NAD+, hanging drop vapor diffusion method, using 17% (w/v) polyethylene glycol 3350 and 100 mM Bis-Tris at pH 6.5
dicDHPR-NAD complex by incubation in 20 mM Tris-HCl, pH 8.0, hanging-drop vapor diffusion (4 microl drops), 18°C (291 K), screening solution (0.1 M bis-tris, pH 6.5, 17% PEG 3350), hexahistidine tag not removed, x-ray diffraction
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
nickel-affinity column chromatography
cells centrifuged, washed with PBS (pH 7.4), resuspended in lysis buffer (50 mM Tris-HCl, pH 7.5), disrupted by sonication, centrifugation, supernatant filtered (0.45 microm), applied to a column with nickel-NTA beads, eluted (50 mM Tris-HCl, pH 7.5), active fractions pooled, concentrated, and exchanged into 50 mM sodium phosphate, pH 6.8, ultrafiltration, applied to a cation-exchange chromatography HS20 column, eluted with salt gradient at pH 6.8, concentration by ultrafiltration, gel-filtration chromatography with Superdex 200 column in 50 mM Tris-HCl, pH 8.0, concentration of eluted fractions in 20 mM Tris-HCl, pH 8.0, by ultrafiltration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
dicDHPR gene (residues 1-231) cloned into pET-28b expression plasmid with hexahistidine tag and thrombin cleavage site, expression in Escherichia coli BL21 (DE3)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chen, C.; Seo, K.H.; Kim, H.L.; Zhuang, N.; Park, Y.S.; Lee, K.H.
Crystallization and preliminary characterization of dihydropteridine reductase from Dictyostelium discoideum
Acta Crystallogr. Sect. F
64
1013-1015
2008
Dictyostelium discoideum
Manually annotated by BRENDA team
Chen, C.; Kim, H.L.; Zhuang, N.; Seo, K.H.; Park, K.H.; Han, C.D.; Park, Y.S.; Lee, K.H.
Structural insights into the dual substrate specificities of mammalian and Dictyostelium dihydropteridine reductases toward two stereoisomers of quinonoid dihydrobiopterin
FEBS Lett.
585
2640-2646
2011
Dictyostelium discoideum (Q86A17), Dictyostelium discoideum
Manually annotated by BRENDA team