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Information on EC 3.6.1.67 - dihydroneopterin triphosphate diphosphatase and Organism(s) Arabidopsis thaliana

for references in articles please use BRENDA:EC3.6.1.67
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EC Tree
IUBMB Comments
The enzyme participates in a folate biosynthesis pathway, which is found in bacteria, fungi, and plants. Requires Mg2+.
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This record set is specific for:
Arabidopsis thaliana
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Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
orf17 protein, atnudt1, dhntpase, dhntp pyrophosphohydrolase, dihydroneopterin triphosphate pyrophosphatase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
At1g68760 protein
-
DHNTP pyrophosphohydrolase
-
dihydroneopterin triphosphate pyrophosphohydrolase
folQ
-
-
-
-
nudB
-
-
-
-
NUDT1
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
7,8-dihydroneopterin 3'-triphosphate diphosphohydrolase
The enzyme participates in a folate biosynthesis pathway, which is found in bacteria, fungi, and plants. Requires Mg2+.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
7,8-dihydroneopterin 3'-triphosphate + H2O
7,8-dihydroneopterin 3'-phosphate + diphosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0021 - 0.147
7,8-dihydroneopterin 3'-triphosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0006 - 0.21
7,8-dihydroneopterin 3'-triphosphate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0041 - 100
7,8-dihydroneopterin 3'-triphosphate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0017
substrate: 7,8-dihydroneopterin 3'-triphosphate, pH 8.0, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NUDT1_ARATH
147
0
16357
Swiss-Prot
Secretory Pathway (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20400
1 * 20400, calculated from sequence
24200
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 20400, calculated from sequence
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli with and without a C-terminal His tag
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Klaus, S.M.; Wegkamp, A.; Sybesma, W.; Hugenholtz, J.; Gregory, J.F. 3rd, Hanson, A.D.
A nudix enzyme removes pyrophosphate from dihydroneopterin triphosphate in the folate synthesis pathway of bacteria and plants
J. Biol. Chem.
280
5274-5280
2004
Arabidopsis thaliana (Q9CA40), Lactococcus lactis (D8KIT5), Lactococcus lactis, Lactococcus lactis NZ9000 (D8KIT5)
Manually annotated by BRENDA team