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Information on EC 1.3.1.20 - trans-1,2-dihydrobenzene-1,2-diol dehydrogenase and Organism(s) Macaca fascicularis and UniProt Accession Q9TQS6

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Macaca fascicularis
UNIPROT: Q9TQS6 not found.
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The taxonomic range for the selected organisms is: Macaca fascicularis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
trans-1,2-dihydrobenzene-1,2-diol dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dihydrodiol dehydrogenase
-
dehydrogenase, trans-1,2-dihydrobenzene-1,2-diol
-
-
-
-
dihydrodiol dehydrogenase
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dehydrogenation
-
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
dehydrogenation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
trans-1,2-dihydrobenzene-1,2-diol:NADP+ oxidoreductase
-
CAS REGISTRY NUMBER
COMMENTARY hide
37255-32-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
camphorquinone + NADPH + H+
?
show the reaction diagram
enzyme has dehydrogenase and reductase activities, enzyme is identical to NADP+-dependent D-xylose dehydrogenase
-
-
?
(R)-tetralol + NADP+
?
show the reaction diagram
-
-
-
?
(R)-tetralol + NADP+
? + NADPH
show the reaction diagram
dehydrogenase activity
-
-
r
(S)-indan-1-ol + NADP+
?
show the reaction diagram
-
-
-
?
(S)-indan-1-ol + NADP+
? + NADPH
show the reaction diagram
dehydrogenase activity
-
-
r
(S)-tetralol + NADP+
?
show the reaction diagram
-
-
-
?
(S)-tetralol + NADP+
? + NADPH
show the reaction diagram
dehydrogenase activity
-
-
r
4-chromanol + NADP+
?
show the reaction diagram
-
-
-
r
4-chromanol + NADP+
? + NADPH
show the reaction diagram
dehydrogenase activity
-
-
r
camphorquinone + NAD(P)H
(1R)-1,7,7-trimethylbicyclo[2.2.1]heptane-2,3-diol + NADP+
show the reaction diagram
-
-
-
-
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
show the reaction diagram
-
-
-
-
?
S-(+)-1,2,3,4-tetrahydronaphth-1-ol + NADP+
? + NADPH
show the reaction diagram
trans-1,2-dihydrobenzene-1,2-diol + NAD(P)+
catechol + NAD(P)H
show the reaction diagram
trans-benzene dihydrodiol + NADP+
? + NADPH
show the reaction diagram
dehydrogenase activity
-
-
r
additional information
?
-
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
camphorquinone + NADPH + H+
?
show the reaction diagram
enzyme has dehydrogenase and reductase activities, enzyme is identical to NADP+-dependent D-xylose dehydrogenase
-
-
?
trans-1,2-dihydrobenzene-1,2-diol + NAD(P)+
catechol + NAD(P)H
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
activates
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-hydroxyacetophenone
-
isoascorbic acid
competitive inhibitor
2,6-dihydroxyanthraquinone
-
competitive inhibitor
4-hydroxyacetophenone
isoascorbic acid
-
competitive inhibitor
L-ascorbic acid
-
competitive inhibitor
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.84 - 21
Camphorquinone
0.056
(R)-tetralol
pH 7.4, 25°C
0.076
(S)-indan-1-ol
pH 7.4, 25°C
0.029
(S)-tetralol
pH 7.4, 25°C
0.073
4-chromanol
pH 7.4, 25°C
0.72
trans-benzene dihydrodiol
pH 7.4, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.004 - 20
Camphorquinone
84
(R)-tetralol
pH 7.4, 25°C
2040
(S)-indan-1-ol
pH 7.4, 25°C
1320
(S)-tetralol
pH 7.4, 25°C
2880
4-chromanol
pH 7.4, 25°C
24.6
trans-benzene dihydrodiol
pH 7.4, 25°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00097 - 0.136
4-hydroxyacetophenone
0.038 - 4.176
isoascorbic acid
0.00097
4-hydroxyacetophenone
Macaca fascicularis
-
wild type enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.04
R148A and R202A mutant, 25 mM Tris-HCl, pH 7.5, 0.25 mM NADP+
0.05
wild type enzyme in dimeric form, 25 mM Tris-HCl, pH 7.5, 0.25 mM NADP+
1.2
monomeric form
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DHDH_MACFA
334
0
36435
Swiss-Prot
Secretory Pathway (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70000
determined by gel filtration
36000
x * 36000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
?
x * 36000, SDS-PAGE
dimer
additional information
the dissociation of DD into the monomer largely affects the stability rather than catalytic activity
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals are obtained at 19.9°C in a culture plate via the vapour-diffusion method, crystal structure of dimeric dihydrodiol dehydrogenase complexed with the inhibitor isoascorbic acid is determined at 2.59 A resolution
dimeric apoenzyme (at 2.0 A resolution) and enzyme-inhibitor complex (at 2.9 A resolution), crystals are grown using droplets consisting of the dihydrodiol dehydrogenase/NADPH solution mixed with a matching volume containing 1.5 M ammonium phosphate and 0.1 M sodium citrate at pH 5.6, tertiary structure is formed by a classical dinucleotide binding fold comprising of 2 beta-alpha-beta-alpha-beta motifs at the N-terminus and an eight-stranded, predominantly antiparallel beta-sheet at the C-terminus
vapour diffusion method with 2 M ammonium phosphate and 0.1 M sodium citrate buffer (pH 5.6) and 20% glycerol
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A36D
production by site-directed mutagenesis
D280A
production by site-directed mutagenesis
F154A
production by site-directed mutagenesis
F279A
production by site-directed mutagenesis
H76Q
production by site-directed mutagenesis
H79Q
production by site-directed mutagenesis
K97M
production by site-directed mutagenesis
K97R
production by site-directed mutagenesis
R148A
mutagenesis is performed using a QuickChange site-directed mutagenesis kit, dehydrogenase activity is comparable to that of the wild type
R148A/R202A
mutagenesis is performed using a QuickChange site-directedmutagenesis kit
R202A
mutagenesis is performed using a QuickChange site-directed mutagenesis kit, dehydrogenase activity is comparable to that of the wild type
R37A
production by site-directed mutagenesis
R37D
production by site-directed mutagenesis
R41A
production by site-directed mutagenesis
R41D
production by site-directed mutagenesis
W125Y
production by site-directed mutagenesis
W254A
production by site-directed mutagenesis
W254Y
production by site-directed mutagenesis
F279A
-
the mutation affects inhibition and substrate affinity
K97M
-
mutant shows almost complete abrogation in activity for D-xylose oxidation and NADP+, and very poor activity with camphorquinone reduction and NADPH
K97R
-
mutant shows almost complete abrogation in activity for D-xylose oxidation and NADP+, and very poor activity with camphorquinone reduction and NADPH
R148A
-
activity and temperature stability are similar to the wild type enzyme
R148A/R202A
-
very low activity, the Vmax value of the mutant enzyme is 3.7fold lower than the wild type enzyme, displays significant temperature sensitivity
R202A
-
activity and temperature stability are similar to the wild type enzyme
W125A
-
the mutation affects inhibition and substrate affinity
W254A
-
the mutation affects inhibition and substrate affinity
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
no activity of the 37°C-inactivated R148A/R202A mutant is recovered by the addition of 0.1 mM NADP+ and 40% glycerol
37
-
the wild type enzyme and mutant enzymes R148A and R202A are stable at 37°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzymes are purified from the 12000g supernatants of the homogenates of the cells, the single mutant enzymes are partially purified by the ammonium sulphate fractionation and chromatography on a Sephadex G-100 column, the wild type and double mutant enzyme are further purified by chromatography on a Red Sepharose column
the recombinant enzymes are purified from the 12000g supernatants of the homogenates of the cells
ammonium sulfate precipitation, Red Sepharose column chromatography, and Sephadex G-100 gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
in Escherichia coli BL21(DE3)
wild-type protein and mutants are expressed in Escherichia coli BL21 (DE3)
expressed in Escherichia coli BL21(DE3) cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nakagawa, M.; Matsuura, K.; Hara, A.; Sawada, H.; Bunai, H.; Ohya, I.
Dimeric dihydrodiol dehydrogenase in monkey kidney. Substrate specificity, stereospecificity of hydrogen transfer, and distribution
J. Biochem.
106
1104-1109
1989
Macaca fascicularis, Macaca fuscata
Manually annotated by BRENDA team
Higaki, Y.; Kamiya, T.; Usami, N.; Shintani, S.; Shiraishi, H.; Ishikura, S.; Yamamoto, I.; Hara, A.
Molecular characterization of two monkey dihydrodiol dehydrogenases
Drug Metab. Pharmacokinet.
17
348-356
2002
Macaca fascicularis (Q95JH5), Macaca fascicularis (Q95JH7), Macaca fuscata fuscata (Q95JH4), Macaca fuscata fuscata (Q95JH6)
Manually annotated by BRENDA team
Carbone, V.; Sumii, R.; Ishikura, S.; Asada, Y.; Hara, A.; El-Kabbani, O.
Structure of monkey dimeric dihydrodiol dehydrogenase in complex with isoascorbic acid
Acta Crystallogr. Sect. D
64
532-542
2008
Macaca fascicularis (Q9TQS6), Macaca fuscata
Manually annotated by BRENDA team
Carbone, V.; Hara, A.; El-Kabbani, O.
Structural and functional features of dimeric dihydrodiol dehydrogenase
Cell. Mol. Life Sci.
65
1464-1474
2008
Bos taurus (Q148L6), Macaca fascicularis, Mus musculus (Q9DBB8), Pongo abelii (Q5R5J5), Sus scrofa
Manually annotated by BRENDA team
Carbone, V.; Endo, S.; Sumii, R.; Chung, R.P.; Matsunaga, T.; Hara, A.; El-Kabbani, O.
Structures of dimeric dihydrodiol dehydrogenase apoenzyme and inhibitor complex: probing the subunit interface with site-directed mutagenesis
Proteins Struct. Funct. Bioinform.
70
176-187
2007
Macaca fascicularis
-
Manually annotated by BRENDA team
Carbone, V.; Endo, S.; Sumii, R.; Chung, R.; Matsunaga, T.; Hara, A.; El-Kabbani, O.
Structures of dimeric dihydrodiol dehydrogenase apoenzyme and inhibitor complex: Probing the subunit interface with site-directed mutagenesis
Proteins Struct. Funct. Genet.
70
176-187
2008
Macaca fascicularis (Q9TQS6)
Manually annotated by BRENDA team