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Information on EC 5.1.99.8 - 7,8-dihydroneopterin epimerase and Organism(s) Escherichia coli and UniProt Accession P0AC19

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EC Tree
     5 Isomerases
         5.1 Racemases and epimerases
             5.1.99 Acting on other compounds
                5.1.99.8 7,8-dihydroneopterin epimerase
IUBMB Comments
The enzyme, which has been characterized in bacteria and plants, also has the activity of EC 4.1.2.25, dihydroneopterin aldolase. The enzyme from the bacterium Mycobacterium tuberculosis has an additional oxygenase function (EC 1.13.11.81, 7,8-dihydroneopterin oxygenase) .
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This record set is specific for:
Escherichia coli
UNIPROT: P0AC19
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
At3g11750, At5g62980, dihydroneopterin triphosphate 2'-epimerase, FolB, FolB1, FolB2, folX, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dihydroneopterin triphosphate 2'-epimerase
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
7,8-dihydroneopterin 2'-epimerase
The enzyme, which has been characterized in bacteria and plants, also has the activity of EC 4.1.2.25, dihydroneopterin aldolase. The enzyme from the bacterium Mycobacterium tuberculosis has an additional oxygenase function (EC 1.13.11.81, 7,8-dihydroneopterin oxygenase) [4].
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-dihydromonapterin
7,8-dihydroneopterin
show the reaction diagram
-
-
-
?
7,8-dihydroneopterin
7,8-dihydromonapterin
show the reaction diagram
-
-
-
r
7,8-dihydroneopterin triphosphate
7,8-dihydromonapterin triphosphate
show the reaction diagram
additional information
?
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.066
7,8-dihydromonapterin
pH 8.0, 55°C
0.149
7,8-dihydroneopterin
pH 8.0, 55°C
0.013
7,8-dihydroneopterin triphosphate
pH 8.0, 55°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
11
pH not specified in the publication, temperature not specified in the publication
5.8
pH 8.0, 55°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
a folX deletion mutant has normal growth properties on complete medium as well as on minimal medium
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
111600
sedimentation equilibrium analysis
13988
8 * 13988, calculated, 8 * 14000, SDS-PAGE
14000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 14000, SDS-PAGE
octamer
8 * 13988, calculated, 8 * 14000, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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 (P0AC19)
Manually annotated by BRENDA team
Haussmann, C.; Rohdich,F.; Lottspeich,F.; Eberhardt, S.; Scheuring,J.; Mackamul,S.; Bacher, A.
Dihydroneopterin triphosphate epimerase of Escherichia coli: Purification, genetic cloning, and expression
J. Bacteriol.
179
949-951
1997
Escherichia coli (P0AC19)
Manually annotated by BRENDA team