Information on EC 1.1.98.2 - glucose-6-phosphate dehydrogenase (coenzyme-F420)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.98.2
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RECOMMENDED NAME
GeneOntology No.
glucose-6-phosphate dehydrogenase (coenzyme-F420)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-glucose 6-phosphate + oxidized coenzyme F420 = 6-phospho-D-glucono-1,5-lactone + reduced coenzyme F420
show the reaction diagram
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-
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SYSTEMATIC NAME
IUBMB Comments
D-glucose-6-phosphate:F420 1-oxidoreductase
The enzyme is very specific for D-glucose 6-phosphate. No activity with NAD+, NADP+, FAD and FMN [1].
CAS REGISTRY NUMBER
COMMENTARY hide
176898-36-5
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9001-40-5
cf. EC 1.1.1.49
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
; formerly Nocardia amarae
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-
Manually annotated by BRENDA team
no activity in Actinomadura kijaniata
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-
-
Manually annotated by BRENDA team
no activity in Corynebacterium ammoniagenes
-
-
-
Manually annotated by BRENDA team
no activity in Corynebacterium glutamicum
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-
-
Manually annotated by BRENDA team
no activity in Corynebacterium matruchotii
-
-
-
Manually annotated by BRENDA team
no activity in Methanobacterium thermoautotrophicum
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-
-
Manually annotated by BRENDA team
no activity in Methanobacterium thermoautotrophicum Marburg
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-
-
Manually annotated by BRENDA team
no activity in Methanosarcina barkeri
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-
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Manually annotated by BRENDA team
no activity in Methanosarcina barkeri Fusaro
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-
-
Manually annotated by BRENDA team
no activity in Methanospirillum hungateii
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-
-
Manually annotated by BRENDA team
no activity in Streptomyces achromogenes
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-
-
Manually annotated by BRENDA team
no activity in Streptomyces aureofaciens
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-
-
Manually annotated by BRENDA team
no activity in Streptomyces avermitilis
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-
-
Manually annotated by BRENDA team
no activity in Streptomyces lincolnensis
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Manually annotated by BRENDA team
no activity in Streptomyces lividans
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-
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Manually annotated by BRENDA team
no activity in Streptomyces rimosus
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-fructose-6-phosphate + oxidized coenzyme F420
?
show the reaction diagram
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9% of the activity with 2 mM D-glucose 6-phosphate
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-
?
D-glucose 6-phosphate + oxidized coenzyme F420
6-phospho-D-glucono-1,5-lactone + reduced coenzyme F420
show the reaction diagram
D-glucose 6-phosphate + oxidized coenzyme F420
D-glucono-1,5-lactone 6-phosphate + reduced coenzyme F420
show the reaction diagram
D-mannose-6-phosphate + oxidized coenzyme F420
?
show the reaction diagram
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5% of the activity with 2 mM D-glucose 6-phosphate
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-
?
additional information
?
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intracellular glucose-6-phosphate in mycobacteria serves as a source of reducing power, and with the mycobacteria-specific F420-dependent glucose-6-phosphate dehydrogenase/F420 system, plays a protective role against oxidative stress imposed by host macrophages
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-glucose 6-phosphate + oxidized coenzyme F420
6-phospho-D-glucono-1,5-lactone + reduced coenzyme F420
show the reaction diagram
D-glucose 6-phosphate + oxidized coenzyme F420
D-glucono-1,5-lactone 6-phosphate + reduced coenzyme F420
show the reaction diagram
additional information
?
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intracellular glucose-6-phosphate in mycobacteria serves as a source of reducing power, and with the mycobacteria-specific F420-dependent glucose-6-phosphate dehydrogenase/F420 system, plays a protective role against oxidative stress imposed by host macrophages
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
coenzyme F420
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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no inhibition: D-fructose-1-phosphate, D-galactose-1-phosphate, D-galactose-6-phosphate, L-fucose-1-phosphate, D-glucose-1-phosphate, D-ribose-5-phosphate, D-ribose-1-phosphate, D-arabinose-5-phosphate, glyceraldehyde-3-phosphate, and glycerol-3-phosphate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.6
D-glucose 6-phosphate
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pH 7, 40C
0.004
oxidized coenzyme F420
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pH 7.0, 40C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.043
citrate
Mycobacterium tuberculosis
P9WNE1
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.008
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pH 7.0, 23C
0.014
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pH 7.0, 23C
0.02
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pH 7.0, 23C
0.025
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pH 7.0, 23C
0.076
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pH 7.0, 23C
0.083
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pH 7.0, 23C
0.088
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pH 7.0, 23C
0.093
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pH 7.0, 23C
0.117
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pH 7.0, 23C
0.152
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pH 7.0, 23C
0.154
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pH 7.0, 23C
0.156
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pH 7.0, 23C
0.313
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pH 7.0, 23C
0.418
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pH 7.0, 23C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
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maxima at pH 5.5 and pH 8.0
8
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maxima at pH 5.5 and pH 8.0
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8.5
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pH 5: about 60% of maximal activity, pH 5.5: maximum, pH 7: about 50% of maximal activity, pH 8.0: maximal activity, pH 8.5: about 60% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Rhodococcus jostii (strain RHA1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35200
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2 * 35200, SDS-PAGE, recombinant Rv0132c-D38 construct lacking the predicted N-terminal signal sequence
40000
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2 * 40000, SDS-PAGE
75000
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gel filtration, recombinant Rv0132c-D38 construct lacking the predicted N-terminal signal sequence
78000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 40000, SDS-PAGE
homodimer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and selenomethionine-labeled FGD1, sitting drop vapour diffusion, mixing of protein solution in a 1:1 ratio with precipitant solution containing 1.6 M tri-sodium citrate, pH 6.5, microseeding, X-ray diffraction structure determination and analysis at 2.1 A resolution, multiwavelength anomalous diffraction; sitting drop vapour diffusion method, native and selenomethionine-labeled FGD1 are successfully crystallized by vapor diffusion, with the crystals diffracting to 2.1 A resolution
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structure of the enzyme is determined by X-ray crystallography both in its apo state and in complex with F420 and citrate at resolutions of 1.90 and 1.95 A, respectively. The structure reveals a highly specific F420 binding mode, which is shared with several other F420-dependent enzymes. The competitive inhibitor citrate occupies the substrate binding pocket adjacent to F420. Modeling of the binding of the glucose 6-phosphate substrate identifies a positively charged phosphate binding pocket and shows that glucose 6-phosphate, like citrate, packs against the isoalloxazine moiety of F420 and helps promote a butterfly bend conformation that facilitates F420 reduction and catalysis
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
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denaturation above
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, 16 days, highly purified enzyme, retention of 60% and 20% of the original activity with and without glycerol, respectively
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; recombinant His-tagged wild-type and selenomethionine-labeled FGD1 from Mycobacterium smegmatis strain mc24517 by nickel affinity chromatography and gel filtration
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ammonium sulfate fractionation, phenyl-Sepharose column chromatography, F420ether-linked aminohexylSepharose 4B affinity chromatography, and quaternary aminoethyl-Sephadex column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli BL21(DE3), no significant homology with NADP+-dependent glucose-6-phosphate dehydrogenases
gene Rv0132c, sequence comparisons and homology modeling of Rv0132c, expression of Rv0132c-D38 construct lacking the predicted N-terminal signal sequence in Mycobacterium smegmatis by nickel affinity chromatography and gel filtration, co-expression with coenzyme F420
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initial attempts to produce recombinant FGD1 using Escherichia coli as a host is unsuccessful, but when the alternative host Mycobacterium smegmatis is used, soluble protein yields of 7 mg/l of culture are achieved; recombinant expression of His-tagged wild-type and selenomethionine-labeled FGD1 in Mycobacterium smegmatis strain mc24517
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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PA-824 is a compound for the treatment of tuberculosis (undergoing human trials). PA-824 is a prodrug of the nitroimidazole class, requiring bioreductive activation of an aromatic nitro group to exert an antitubercular effect. Resistance to PA-824 (a nitroimidazo-oxazine) and CGI-17341 (a nitroimidazo-oxazole) is most commonly mediated by loss of a specific glucose-6-phosphate dehydrogenase or its deazaflavin cofactor F420, which together provide electrons for the reductive activation of this class of molecules. Although glucose-6-phosphate dehydrogenase and F420 are necessary for sensitivity to these compounds, they are not sufficient and require additional accessory proteins that directly interact with the nitroimidazole. The sensitivity of Mtb to PA-824 and related compounds is mediated by a protein that is highly specific for subtle structural variations in these bicyclic nitroimidazoles
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