Information on EC 5.1.99.8 - 7,8-dihydroneopterin epimerase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
5.1.99.8
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RECOMMENDED NAME
GeneOntology No.
7,8-dihydroneopterin epimerase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
7,8-dihydroneopterin = 7,8-dihydromonapterin
show the reaction diagram
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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].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
bifunctional epimerase and aldolase, EC 4.1.2.25
Uniprot
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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a folX deletion mutant has normal growth properties on complete medium as well as on minimal medium
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
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?
7,8-dihydroneopterin
7,8-dihydromonapterin
show the reaction diagram
7,8-dihydroneopterin triphosphate
7,8-dihydromonapterin triphosphate
show the reaction diagram
additional information
?
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.066
7,8-dihydromonapterin
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pH 8.0, 55°C
0.149
7,8-dihydroneopterin
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pH 8.0, 55°C
0.013
7,8-dihydroneopterin triphosphate
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pH 8.0, 55°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.8
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pH 8.0, 55°C
11
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pH not specified in the publication, temperature not specified in the publication
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
13600
x * 14685, calculated, x * 13600, SDS-PAGE
13988
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8 * 13988, calculated, 8 * 14000, SDS-PAGE
14100
x * 16300, calculated, x * 14100, SDS-PAGE of truncated recombinant protein
14600
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x * 14600, SDS-PAGE
14685
x * 14685, calculated, x * 13600, SDS-PAGE
16300
x * 16300, calculated, x * 14100, SDS-PAGE of truncated recombinant protein
111600
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sedimentation equilibrium analysis
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
octamer
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8 * 13988, calculated, 8 * 14000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with neopterin, an analog of dihydroneopterin, and with monapterin, to 1.7 A and 1.68 A resolution, respectively. Active site residues E22, K100, and Y54 function coordinately during catalysis
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli; expression in Escherichia coli