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Information on EC 1.1.1.359 - aldose 1-dehydrogenase [NAD(P)+]
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1.1.1.359 aldose 1-dehydrogenase [NAD(P)+]IUBMB Comments
The enzyme from the archaeon Sulfolobus solfataricus shows broad specificity towards aldoses (D-glucose, D-galactose, D-xylose, L-arabinose, 6-deoxy-D-glucose, D-fucose) and can utilize NAD+ and NADP+ with similar catalytic efficiency. It is involved in aldose catabolism via the branched variant of the Entner-Doudoroff pathway.
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The enzyme appears in viruses and cellular organisms
Synonyms
gdh-1, glucose dehydrogenase, SsGDH, SSO3003, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an aldopyranose + NAD(P)+ = an aldono-1,5-lactone + NAD(P)H + H+
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
an aldopyranose:NAD(P)+ 1-oxidoreductase
The enzyme from the archaeon Sulfolobus solfataricus shows broad specificity towards aldoses (D-glucose, D-galactose, D-xylose, L-arabinose, 6-deoxy-D-glucose, D-fucose) and can utilize NAD+ and NADP+ with similar catalytic efficiency. It is involved in aldose catabolism via the branched variant of the Entner-Doudoroff pathway.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
beta-D-glucose + NAD+ + H2O
D-gluconate + NADH + 2 H+
-
-
-
ir
beta-D-glucose + NAD+ + H2O
D-gluconate + NADH + 2 H+
-
kcat/Km for beta-D-glucose in the reaction with NAD+ is 1.4fold higher than the kcat/Km value for beta-D-glucose in the reaction with NADP+
-
-
ir
beta-D-glucose + NAD+ + H2O
D-gluconate + NADH + 2 H+
when NAD+ serves as electron acceptor, D-glucose is oxidized at the highest rate among the substrates tested. No reverse reaction is evident, under various reaction conditions, when gluconic acid is used as substrate
-
-
ir
beta-D-glucose + NAD+ + H2O
D-gluconate + NADH + 2 H+
-
-
-
ir
beta-D-glucose + NADP+ + H2O
D-gluconate + NADPH + 2 H+
-
-
-
-
ir
beta-D-glucose + NADP+ + H2O
D-gluconate + NADPH + 2 H+
-
-
-
ir
beta-D-glucose + NADP+ + H2O
D-gluconate + NADPH + 2 H+
it is likely that the first product of this reaction is delta-gluconolactone, which is readily converted into the acid. The lactone hydrolysis is facilitated by the high temperature and the slight alkaline pH value of the standard reaction conditions, thus explaining why no reverse reaction is observed under these conditions when delta-gluconolactone is used as substrate. A very slow NADH-dependent reduction of delta-gluconolactone by glucose dehydrogenase is observed at pH 7.0 and 37°C
-
-
?
beta-D-glucose + NADP+ + H2O
D-gluconate + NADPH + 2 H+
-
kcat/Km for beta-D-glucose in the reaction with NADP+ is 1.4fold lower than the kcat/Km value for beta-D-glucose in the reaction with NAD+
-
-
ir
beta-D-glucose + NADP+ + H2O
D-gluconate + NADPH + 2 H+
-
-
-
ir
D-galactose + NAD+ + H2O
D-galactonate + NADH + 2 H+
-
-
-
?
D-galactose + NADP+ + H2O
D-galactonate + NADPH + 2 H+
-
-
-
?
D-galactose + NADP+ + H2O
D-galactonate + NADPH + 2 H+
-
-
-
-
?
D-galactose + NADP+ + H2O
D-galactonate + NADPH + 2 H+
-
-
-
?
D-galactose + NADP+ + H2O
D-galactonate + NADPH + 2 H+
the activity is 70% of the activity with beta-D-glucose + NADP+
-
-
?
additional information
?
-
the enzyme iss involved in aldose catabolism via the branched variant of the Entner–Doudoroff pathway
-
-
-
additional information
?
-
no activity with mannose or glucose 6-phosphate
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
Q7LYI9
the enzyme iss involved in aldose catabolism via the branched variant of the Entner–Doudoroff pathway
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
the enzyme is catalytically active with both NADP+ and NAD+. NADP+ and NAD+ bind at the same site on the enzyme
NAD+
-
when NAD+ serves as electron acceptor, D-glucose is oxidized at the highest rate among the substrates tested
NAD+
-
kcat/Km for beta-D-glucose in the reaction with NAD+ is 1.4fold higher than the kcat/Km value for beta-D-glucose in the reaction with NADP+
NADP+
-
the enzyme is catalytically active with both NADP+ and NAD+. NADP+ and NAD+ bind at the same site on the enzyme
NADP+
-
by using NADP+ as coenzyme D-xylose and 2-deoxy-D-glucose are oxidized at the highest rate
NADP+
-
kcat/Km for beta-D-glucose in the reaction with NADP+ is 1.4fold lower than the kcat/Km value for beta-D-glucose in the reaction with NAD+
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
20 mM, maximal activation of enzyme inactivated by dialysis against Mg2+-free 20 mM-triethanolamine/HCl buffer, pH 7.0
Mg2+
-
20 mM, maximal activation of enzyme inactivated by dialysis against Mg2+-free 20 mM-triethanolamine/HCl buffer, pH 7.0
Mn2+
-
20 mM, maximal activation of enzyme inactivated by dialysis against Mg2+-free 20 mM-triethanolamine/HCl buffer, pH 7.0
Zinc
-
the enzyme possess the catalytic zinc binding residues Cys-39 and His-66
additional information
additional information
-
Ni2+, Cd2+ and univalent cations are ineffective in promoting enzyme reactivation
additional information
-
no significant increase in the presence of ZnCl2, CaCl2, or MgCl2, at final concentrations of 0.1 mM
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
-
inhibits the NAD+-dependentcarbohydrate oxidations in a competitive manner with respect to NAD+
additional information
-
galactose (0.04 mM), mannose (0.04 mM) and ribose (0.04 mM) do not inhibit glucose oxidation by NAD+
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.2
NAD+
-
pH 9.0, 70°C, cosubstrate: beta-D-glucose; pH 9.0, 70°C, cosubstrate: D-xylose
additional information
NAD+
-
Km is superior to 30 mM. The Km value for NAD+ can not be defined precisely as it is impossible to reach saturation of the enzyme
1.3
beta-D-glucose
-
pH 7.5, 70°C, cosubstrate: NADP+, wild-type enzyme
1.5
beta-D-glucose
-
pH 7.5, 70°C, cosubstrate: NAD+, wild-type enzyme
24.8
beta-D-glucose
-
pH 7.5, 70°C, cosubstrate: NAD+, mutant enzyme T41A
33.3
beta-D-glucose
-
pH 7.5, 70°C, cosubstrate: NADP+, mutant enzyme T41A
59
beta-D-glucose
-
pH 7.5, 70°C, cosubstrate: NADP+, mutant enzyme T41V
72.5
beta-D-glucose
-
pH 7.5, 70°C, cosubstrate: NAD+, mutant enzyme T41V
0.44
D-galactose
-
pH 7.5, 70°C, cosubstrate: NADP+, wild-type enzyme
0.57
D-galactose
-
pH 7.5, 70°C, cosubstrate: NAD+, wild-type enzyme
109
D-galactose
-
pH 7.5, 70°C, cosubstrate: NADP+, mutant enzyme T41A
118
D-galactose
-
pH 7.5, 70°C, cosubstrate: NAD+, mutant enzyme T41A
175
D-galactose
-
pH 7.5, 70°C, cosubstrate: NADP+, mutant enzyme T41V
204
D-galactose
-
pH 7.5, 70°C, cosubstrate: NAD+, mutant enzyme T41V
0.18
D-xylose
-
pH 7.5, 70°C, cosubstrate: NADP+, wild-type enzyme
0.18
D-xylose
-
pH 8.0, 70°C, native enzyme from xylose-grown cell extract; pH 8.0, 70°C, recombinant enzyme
20.4
D-xylose
-
pH 7.5, 70°C, cosubstrate: NADP+, mutant enzyme T41A
29.2
D-xylose
-
pH 7.5, 70°C, cosubstrate: NAD+, mutant enzyme T41A
65.8
D-xylose
-
pH 7.5, 70°C, cosubstrate: NADP+, mutant enzyme T41V
76.3
D-xylose
-
pH 7.5, 70°C, cosubstrate: NAD+, mutant enzyme T41V
0.47
L-arabinose
-
pH 8.0, 70°C, native enzyme from xylose-grown cell extract
0.03
NADP+
-
pH 9.0, 70°C, cosubstrate: beta-D-glucose; pH 9.0, 70°C, cosubstrate: D-galactose; pH 9.0, 70°C, cosubstrate: D-xylose
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4
beta-D-glucose
-
pH 7.5, 70°C, cosubstrate: NADP+, mutant enzyme T41V
6
beta-D-glucose
-
pH 7.5, 70°C, cosubstrate: NAD+, mutant enzyme T41V
14
beta-D-glucose
-
pH 7.5, 70°C, cosubstrate: NADP+, mutant enzyme T41A
39
beta-D-glucose
-
pH 7.5, 70°C, cosubstrate: NAD+, mutant enzyme T41A
48
beta-D-glucose
-
pH 7.5, 70°C, cosubstrate: NADP+, wild-type enzyme
75
beta-D-glucose
-
pH 7.5, 70°C, cosubstrate: NAD+, wild-type enzyme
7
D-galactose
-
pH 7.5, 70°C, cosubstrate: NADP+, mutant enzyme T41V
8
D-galactose
-
pH 7.5, 70°C, cosubstrate: NAD+, mutant enzyme T41V
22
D-galactose
-
pH 7.5, 70°C, cosubstrate: NADP+, mutant enzyme T41A
37
D-galactose
-
pH 7.5, 70°C, cosubstrate: NADP+, wild-type enzyme
56
D-galactose
-
pH 7.5, 70°C, cosubstrate: NAD+, mutant enzyme T41A
61
D-galactose
-
pH 7.5, 70°C, cosubstrate: NAD+, wild-type enzyme
22
D-xylose
-
pH 7.5, 70°C, cosubstrate: NADP+, mutant enzyme T41A
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.07
beta-D-glucose
-
pH 7.5, 70°C, cosubstrate: NADP+, mutant enzyme T41V
0.09
beta-D-glucose
-
pH 7.5, 70°C, cosubstrate: NAD+, mutant enzyme T41V
0.4
beta-D-glucose
-
pH 7.5, 70°C, cosubstrate: NADP+, mutant enzyme T41A
1.6
beta-D-glucose
-
pH 7.5, 70°C, cosubstrate: NAD+, mutant enzyme T41A
37
beta-D-glucose
-
pH 7.5, 70°C, cosubstrate: NADP+, wild-type enzyme
50
beta-D-glucose
-
pH 7.5, 70°C, cosubstrate: NAD+, wild-type enzyme
0.04
D-galactose
-
pH 7.5, 70°C, cosubstrate: NAD+, mutant enzyme T41V; pH 7.5, 70°C, cosubstrate: NADP+, mutant enzyme T41V
0.2
D-galactose
-
pH 7.5, 70°C, cosubstrate: NADP+, mutant enzyme T41A
0.5
D-galactose
-
pH 7.5, 70°C, cosubstrate: NAD+, mutant enzyme T41A
85
D-galactose
-
pH 7.5, 70°C, cosubstrate: NADP+, wild-type enzyme
108
D-galactose
-
pH 7.5, 70°C, cosubstrate: NAD+, wild-type enzyme
0.11
D-xylose
-
pH 7.5, 70°C, cosubstrate: NADP+, mutant enzyme T41V
0.15
D-xylose
-
pH 7.5, 70°C, cosubstrate: NAD+, mutant enzyme T41V
1.1
D-xylose
-
pH 7.5, 70°C, cosubstrate: NADP+, mutant enzyme T41A
2.8
D-xylose
-
pH 7.5, 70°C, cosubstrate: NAD+, mutant enzyme T41A
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
in glucose catabolism via the branched Entner–Doudoroff pathway the enzyme might acquire important function at higher D-glucose concentrations and in the presence of NAD+. It seems to have additional functions in the catabolism of D-galactose via the same pathway as well as in degradation pathways of D-xylose and L-arabinose
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
GLCD1_SACS2
Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
366
0
40891
Swiss-Prot
GLCDH_THEAC
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
361
0
40250
Swiss-Prot
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
tetramer
-
4 * 40849, calculated from sequence; 4 * 41000, SDS-PAGE
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CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
hanging drop, vapor-diffusion method, crystal structure of the apo form of glucose dehydrogenase to a resolution of 1.8 A and a complex with its required cofactor, NADP+, to a resolution of 2.3 A. Complexes of the enzyme with D-glucose and D-xylose are presented to resolutions of 1.6 and 1.5 A. A T41A mutation is engineered to enable the trapping of substrate in the crystal
-
the best crystals to date diffract to 1.8 A on a synchrotron source, have orthorhombic symmetry and belong to space group P2(1)2(1)2
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
T41A
-
kcat/Km value of the mutant enzyme for beta-D-glucose (with NAD+) is about 30fold lower compared to wild-type enzyme, kcat/Km value of the mutant enzyme for beta-D-flucose (with NADP+) is about 90fold lower compared to wild-type enzyme
T41V
-
kcat/Km value of the mutant enzyme for beta-D-glucose (with NAD+) is about 555fold lower compared to wild-type enzyme, kcat/Km value of the mutant enzyme for beta-D-flucose (with NADP+) is about 530fold lower compared to wild-type enzyme
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 9
-
the enzyme stability does not vary significantly in the pH range 5-9
639110
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
protein concentration 0.2 mg/ml, 50% of the activity is lost after 40 days
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dehydrogenase preparations became inactivated irreversibly when stored in the absence of ethylene glycol and Mg2+, at very low protein concentration, or during freezing and thawing
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ethylene glycol
-
preparations became inactivated irreversibly when stored in the absence of ethylene glycol
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
37°C, protein concentration 0.2 mg/ml, 50% of the activity is lost after 40 days
-
4°C, 20 mM MgCl2 and 20% (v/v) ethylene glycol, stable for several months
-
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
enzyme from Sulfolobus solfataricus cell extract and recombinant enzyme expressed in Escherichia coli
-
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Smith, L.D.; Budgen, N.; Bungard, S.J.; Danson, M.J.; Hough, D.W.
Purification and characterization of glucose dehydrogenase from the thermoacidophilic archaebacterium Thermoplasma acidophilum
Biochem. J.
261
973-977
1989
Thermoplasma acidophilum (P13203)
brenda
Giardina, P.; DeBasia, M.G.; DeRosa, M.; Gambacort, A.; Buonocore, V.
Glucose dehydrogenase from the thermoacidophilic archaebacterium Sulfolobus solfataricus
Biochem. J.
239
517-522
1986
Saccharolobus solfataricus (O93715)
brenda
Lamble, H.J.; Heyer, N.I.; Bull, S.D.; Hough, D.W.; Danson, M.J.
Metabolic pathway promiscuity in the archaeon Sulfolobus solfataricus revealed by studies on glucose dehydrogenase and 2-keto-3-deoxygluconate aldolase
J. Biol. Chem.
278
34066-34072
2003
Saccharolobus solfataricus (O93715)
brenda
Milburn, C.C.; Lamble, H.J.; Theodossis, A.; Bull, S.D.; Hough, D.W.; Danson, M.J.; Taylor, G.L.
The structural basis of substrate promiscuity in glucose dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus
J. Biol. Chem.
281
14796-14804
2006
Saccharolobus solfataricus (O93715)
brenda
Nunn, C.E.; Johnsen, U.; Schoenheit, P.; Fuhrer, T.; Sauer, U.; Hough, D.W.; Danson, M.J.
Metabolism of pentose sugars in the hyperthermophilic archaea Sulfolobus solfataricus and Sulfolobus acidocaldarius
J. Biol. Chem.
285
33701-33709
2010
Saccharolobus solfataricus (O93715), Saccharolobus solfataricus P2 (O93715)
brenda
Theodossis, A.; Milburn, C.C.; Heyer, N.I.; Lamble, H.J.; Hough, D.W.; Danson, M.J.; Taylor, G.L.
Preliminary crystallographic studies of glucose dehydrogenase from the promiscuous Entner-Doudoroff pathway in the hyperthermophilic archaeon Sulfolobus solfataricus
Acta Crystallogr. Sect. F
61
112-115
2005
Saccharolobus solfataricus (O93715)
brenda
Haferkamp, P.; Kutschki, S.; Treichel, J.; Hemeda, H.; Sewczyk, K.; Hoffmann, D.; Zaparty, M.; Siebers, B.
An additional glucose dehydrogenase from Sulfolobus solfataricus: fine-tuning of sugar degradation?
Biochem. Soc. Trans.
39
77-81
2011
Saccharolobus solfataricus (Q7LYI9)
brenda
Bright, J.R.; Byrom, D.; Danson, M.J.; Hough, D.W.; Towner, P.
Cloning, sequencing and expression of the gene encoding glucose dehydrogenase from the thermophilic archaeon Thermoplasma acidophilum
Eur. J. Biochem.
211
549-554
1993
Thermoplasma acidophilum (P13203)
brenda
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