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Information on EC 5.1.99.7 - dihydroneopterin triphosphate 2'-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
                5.1.99.7 dihydroneopterin triphosphate 2'-epimerase
IUBMB Comments
The enzyme, found in gammaproteobacteria, has almost no activity with 7,8-dihydroneopterin .
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This record set is specific for:
Escherichia coli
UNIPROT: P0AC19
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
dihydroneopterin triphosphate epimerase, dihydroneopterin-triphosphate epimerase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H2NTP 2'-epimerase
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D-erythro-7,8-dihydroneopterin triphosphate epimerase
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-
-
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dihydroneopterin triphosphate epimerase
-
-
dihydroneopterin-triphosphate epimerase
-
-
folX
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
7,8-dihydroneopterin 3'-triphosphate = 7,8-dihydromonapterin 3'-triphosphate
show the reaction diagram
reaction mechanism of the epimerase, overview. The reaction can be initiated by protonation of N-5 followed by deprotonation at the acidic C-19 of dihydroneopterin- or dihydromonapterin-type substrates. Epimerization at C-2 might result from reversal of the cleavage reaction without stereochemical control
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PATHWAY SOURCE
PATHWAYS
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-
SYSTEMATIC NAME
IUBMB Comments
7,8-dihydroneopterin 3'-triphosphate 2'-epimerase
The enzyme, found in gammaproteobacteria, has almost no activity with 7,8-dihydroneopterin [2].
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
7,8-dihydromonapterin 3'-triphosphate
show the reaction diagram
-
-
-
r
7,8-dihydromonapterin
7,8-dihydroneopterin
show the reaction diagram
-
-
-
-
r
7,8-dihydroneopterin
7,8-dihydromonapterin
show the reaction diagram
-
-
-
-
r
7,8-dihydroneopterin 3'-triphosphate
7,8-dihydromonapterin 3'-triphosphate
show the reaction diagram
-
-
-
-
r
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
7,8-dihydroneopterin 3'-triphosphate
7,8-dihydromonapterin 3'-triphosphate
show the reaction diagram
-
-
-
r
7,8-dihydroneopterin 3'-triphosphate
7,8-dihydromonapterin 3'-triphosphate
show the reaction diagram
-
-
-
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r
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
potassium iodide
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.066
7,8-dihydromonapterin
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pH 6.2, 37°C, recombinant enzyme
0.149
7,8-dihydroneopterin
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pH 6.2, 37°C, recombinant enzyme
0.013
7,8-dihydroneopterin 3'-triphosphate
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pH 6.2, 37°C, recombinant enzyme
additional information
additional information
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steady-state kinetic analysis, overview
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
505
purified native enzyme, substrate 7,8-dihydroneopterin 3'-triphosphate, pH 6.2, 50°C
7.68
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purified recombinant enzyme, pH 6.2, 55°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37 - 55
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-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
in Escherichia coli, L-monapterin is made from dihydromonapterin triphosphate after successive dephosphorylation and oxidation. Dihydromonapterin triphosphate is formed by an epimerase acting on C2' carbon of dihydroneopterin triphosphate, which is made from GTP by GTP cyclohydrolase I (EC 3.5.4.16)
malfunction
metabolism
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
13700
6 * 13700, SDS-PAGE, 6 * 13993, sequence calculation
13993
6 * 13700, SDS-PAGE, 6 * 13993, sequence calculation
82600
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homohexamer
6 * 13700, SDS-PAGE, 6 * 13993, sequence calculation
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme 954fold by ammonium sulfate fractionation, Cibacron blue 3GA affinity chromatography, hydrophobic interaction chromatography, methotrexate affinity chromatography, and ge filtration, to homogeneity
recombinant enzyme 2.7fold from Escherichia coli strain M15 by anion exchange chromatography, ultrafiltration, heat treatment at 80°C for 4 min, and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis
gene folX, genetic structure and phylogenetic analysis
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gene folX, recombinant expression in Escherichia coli strain M15
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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, Escherichia coli XL1-Blue
Manually annotated by BRENDA team
Pribat, A.; Blaby, I.K.; Lara-Nunez, A.; Gregory, J.F.; de Crecy-Lagard, V.; Hanson, A.D.
FolX and FolM are essential for tetrahydromonapterin synthesis in Escherichia coli and Pseudomonas aeruginosa
J. Bacteriol.
192
475-482
2010
Escherichia coli, Pseudomonas aeruginosa (Q9HYG7), Pseudomonas aeruginosa
Manually annotated by BRENDA team
Ahn, C.; Byun, J.; Yim, J.
Purification, cloning, and functional expression of dihydroneopterin triphosphate 2'-epimerase from Escherichia coli
J. Biol. Chem.
272
15323-15328
1997
Escherichia coli (P0AC19), Escherichia coli
Manually annotated by BRENDA team