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EC Tree
The enzyme appears in viruses and cellular organisms
Synonyms
kgsadh, kgsadh-ii, kgsadh-iii, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-ketoglutarate semialdehyde dehydrogenase, kgsadh-i, ycbd protein,
more
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2-oxoglutarate semialdehyde dehydrogenase
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alpha-ketoglutarate semialdehyde dehydrogenase
alpha-ketoglutaric semialdehyde dehydrogenase
alpha-ketoglutarate semialdehyde dehydrogenase
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alpha-ketoglutarate semialdehyde dehydrogenase
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alpha-ketoglutaric semialdehyde dehydrogenase
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alpha-ketoglutaric semialdehyde dehydrogenase
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alpha-ketoglutaric semialdehyde dehydrogenase
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alpha-ketoglutaric semialdehyde dehydrogenase
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alpha-KGSA dehydrogenase
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alpha-KGSA dehydrogenase
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alphaKGSA dehydrogenase
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alphaKGSA dehydrogenase
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alphaKGSA dehydrogenase
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alphaKGSADH
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DopDH
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KGSADH-I
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KGSADH-II
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KGSADH-III
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SSO3117
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2,5-dioxopentanoate + NADP+ + H2O = 2-oxoglutarate + NADPH + 2 H+
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2,5-dioxopentanoate:NADP+ 5-oxidoreductase
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2,5-dioxopentanoate + NAD(P)+ + H2O
2-oxoglutarate + NAD(P)H
2,5-dioxopentanoate + NAD+ + H2O
2-oxoglutarate + NADH + H+
2,5-dioxopentanoate + NADP+ + H2O
2-oxoglutarate + NADPH + 2 H+
acetaldehyde + NAD(P)+ + H2O
acetate + NAD(P)H + H+
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?
alpha-ketoglutaric semialdehyde + NAD(P)+ + H2O
alpha-ketoglutarate + NAD(P)H + H+
alpha-ketoglutaric semialdehyde + NADP+ + H2O
alpha-ketoglutarate + NADPH + H+
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?
butyraldehyde + NAD(P)+ + H2O
n-butanoate + NAD(P)H + H+
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?
DL-glyceraldehyde + NADP+ + H2O
glycerate + NADPH + H+
glutaraldehyde + NAD(P)+ + H2O
glutarate + NAD(P)H + H+
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?
glutaric semialdehyde + NADP+ + H2O
glutarate + NADPH
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?
glycolaldehyde + NADP+ + H2O
glycolate + NADPH + H+
heptaldehyde + NAD(P)+ + H2O
n-heptanoate + NAD(P)H + H+
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?
hexylaldehyde + NAD(P)+ + H2O
n-hexanoate + NAD(P)H + H+
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?
octylaldehyde + NAD(P)+ + H2O
n-octanoate + NAD(P)H + H+
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?
propanal + NAD(P)+ + H2O
propionate + NAD(P)H + H+
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?
propionaldehyde + NAD(P)+ + H2O
propionate + NAD(P)H + H+
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?
succinate semialdehyde + NAD(P)+ + H2O
? + NAD(P)H + H+
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?
valeraldehyde + NAD(P)+ + H2O
n-pentanoate + NAD(P)H + H+
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?
2,5-dioxopentanoate + NAD(P)+ + H2O
2-oxoglutarate + NAD(P)H
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?
2,5-dioxopentanoate + NAD(P)+ + H2O
2-oxoglutarate + NAD(P)H
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?
2,5-dioxopentanoate + NAD(P)+ + H2O
2-oxoglutarate + NAD(P)H
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?
2,5-dioxopentanoate + NAD(P)+ + H2O
2-oxoglutarate + NAD(P)H
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?
2,5-dioxopentanoate + NAD(P)+ + H2O
2-oxoglutarate + NAD(P)H
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?
2,5-dioxopentanoate + NAD(P)+ + H2O
2-oxoglutarate + NAD(P)H
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?
2,5-dioxopentanoate + NAD(P)+ + H2O
2-oxoglutarate + NAD(P)H
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?
2,5-dioxopentanoate + NAD(P)+ + H2O
2-oxoglutarate + NAD(P)H
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?
2,5-dioxopentanoate + NAD+ + H2O
2-oxoglutarate + NADH + H+
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r
2,5-dioxopentanoate + NAD+ + H2O
2-oxoglutarate + NADH + H+
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r
2,5-dioxopentanoate + NAD+ + H2O
2-oxoglutarate + NADH + H+
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r
2,5-dioxopentanoate + NAD+ + H2O
2-oxoglutarate + NADH + H+
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r
2,5-dioxopentanoate + NAD+ + H2O
2-oxoglutarate + NADH + H+
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r
2,5-dioxopentanoate + NADP+ + H2O
2-oxoglutarate + NADPH + 2 H+
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?
2,5-dioxopentanoate + NADP+ + H2O
2-oxoglutarate + NADPH + 2 H+
the enzyme is involved in the conversion of D-arabinose into the tricarboxylic acid cycle intermediate 2-oxoglutarate via the pentose oxidation pathway
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2,5-dioxopentanoate + NADP+ + H2O
2-oxoglutarate + NADPH + 2 H+
the enzyme is specific for NADP+
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?
2,5-dioxopentanoate + NADP+ + H2O
2-oxoglutarate + NADPH + 2 H+
the enzyme is specific for NADP+
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?
2,5-dioxopentanoate + NADP+ + H2O
2-oxoglutarate + NADPH + 2 H+
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?
2,5-dioxopentanoate + NADP+ + H2O
2-oxoglutarate + NADPH + 2 H+
the enzyme is involved in the conversion of D-arabinose into the tricarboxylic acid cycle intermediate 2-oxoglutarate via the pentose oxidation pathway
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?
alpha-ketoglutaric semialdehyde + NAD(P)+ + H2O
alpha-ketoglutarate + NAD(P)H + H+
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alpha-ketoglutaric semialdehyde + NAD(P)+ + H2O
alpha-ketoglutarate + NAD(P)H + H+
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alpha-ketoglutaric semialdehyde + NAD(P)+ + H2O
alpha-ketoglutarate + NAD(P)H + H+
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alpha-ketoglutaric semialdehyde + NAD(P)+ + H2O
alpha-ketoglutarate + NAD(P)H + H+
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DL-glyceraldehyde + NADP+ + H2O
glycerate + NADPH + H+
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DL-glyceraldehyde + NADP+ + H2O
glycerate + NADPH + H+
the enzyme is specific for NADP+
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DL-glyceraldehyde + NADP+ + H2O
glycerate + NADPH + H+
the enzyme is specific for NADP+
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DL-glyceraldehyde + NADP+ + H2O
glycerate + NADPH + H+
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glycolaldehyde + NADP+ + H2O
glycolate + NADPH + H+
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glycolaldehyde + NADP+ + H2O
glycolate + NADPH + H+
the enzyme is specific for NADP+
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glycolaldehyde + NADP+ + H2O
glycolate + NADPH + H+
the enzyme is specific for NADP+
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glycolaldehyde + NADP+ + H2O
glycolate + NADPH + H+
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?
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2,5-dioxopentanoate + NAD(P)+ + H2O
2-oxoglutarate + NAD(P)H
2,5-dioxopentanoate + NADP+ + H2O
2-oxoglutarate + NADPH + 2 H+
2,5-dioxopentanoate + NAD(P)+ + H2O
2-oxoglutarate + NAD(P)H
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2,5-dioxopentanoate + NAD(P)+ + H2O
2-oxoglutarate + NAD(P)H
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2,5-dioxopentanoate + NAD(P)+ + H2O
2-oxoglutarate + NAD(P)H
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2,5-dioxopentanoate + NAD(P)+ + H2O
2-oxoglutarate + NAD(P)H
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2,5-dioxopentanoate + NAD(P)+ + H2O
2-oxoglutarate + NAD(P)H
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2,5-dioxopentanoate + NAD(P)+ + H2O
2-oxoglutarate + NAD(P)H
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2,5-dioxopentanoate + NAD(P)+ + H2O
2-oxoglutarate + NAD(P)H
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2,5-dioxopentanoate + NAD(P)+ + H2O
2-oxoglutarate + NAD(P)H
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2,5-dioxopentanoate + NADP+ + H2O
2-oxoglutarate + NADPH + 2 H+
the enzyme is involved in the conversion of D-arabinose into the tricarboxylic acid cycle intermediate 2-oxoglutarate via the pentose oxidation pathway
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2,5-dioxopentanoate + NADP+ + H2O
2-oxoglutarate + NADPH + 2 H+
the enzyme is involved in the conversion of D-arabinose into the tricarboxylic acid cycle intermediate 2-oxoglutarate via the pentose oxidation pathway
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?
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NAD+
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NAD+
no significant preference between NAD+ and NADP+ in activity
NAD+
prefered cofactor of KGSADH-II
NADP+
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NADP+
alpha-KGSA dehydrogenase is an NADP+-preferring enzyme, since it is 58times more efficient with NADP+ than with NAD+
NADP+
prefered cofactor of KGSADH-III
NADP+
the enzyme is specific for NADP+
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4-Hydroxy-alpha-ketoglutaric semialdehyde
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additional information
no inhibitory effect with alpha-ketoglutarate or glutamate
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D-galactarate
induces KGSADH-II
D-glucarate
induces KGSADH-II
hydroxy-L-proline
induces KGSADH-III
L-arabinose
induces KGSADH-I
NADP+
the enzyme prefers NADP+ over NAD+
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0.05 - 0.1
2,5-dioxopentanoate
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3.9
acetaldehyde
with NADP+ as cofactor
0.0065 - 0.5569
alpha-Ketoglutaric semialdehyde
0.1 - 0.31
Glutaraldehyde
0.016
Glutaric semialdehyde
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0.37
glycolaldehyde
pH 6.0, 70°C, native enzyme form xylose-grown cells
0.45 - 1.66
succinate semialdehyde
0.0065
alpha-Ketoglutaric semialdehyde
with NAD+ as cofactor
0.0075
alpha-Ketoglutaric semialdehyde
with NADP+ as cofactor
0.011
alpha-Ketoglutaric semialdehyde
with NADP+ as cofactor
0.014
alpha-Ketoglutaric semialdehyde
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0.0246
alpha-Ketoglutaric semialdehyde
with NAD+ as cofactor
0.094
alpha-Ketoglutaric semialdehyde
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with NADP+ as cofactor
0.5569
alpha-Ketoglutaric semialdehyde
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with NAD+ as cofactor
0.1
Glutaraldehyde
with NADP+ as cofactor
0.31
Glutaraldehyde
with NAD+ as cofactor
0.1169
NAD+
-
0.0149
NADP+
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0.3
propanal
with NADP+ as cofactor
1.05
propanal
with NAD+ as cofactor
0.45
succinate semialdehyde
with NAD+ as cofactor
1.66
succinate semialdehyde
with NADP+ as cofactor
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8.6
2,5-dioxopentanoate
pH 7.5, 70°C
0.41
acetaldehyde
with NADP+ as cofactor
1.12 - 197
alpha-Ketoglutaric semialdehyde
4.8
DL-glyceraldehyde
pH 7.5, 70°C
0.65 - 4.13
Glutaraldehyde
5.3
glycolaldehyde
pH 7.5, 70°C
0.05 - 0.06
succinate semialdehyde
1.12
alpha-Ketoglutaric semialdehyde
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with NAD+ as cofactor
2.75
alpha-Ketoglutaric semialdehyde
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with NADP+ as cofactor
15.4
alpha-Ketoglutaric semialdehyde
with NADP+ as cofactor
21.3
alpha-Ketoglutaric semialdehyde
with NAD+ as cofactor
23
alpha-Ketoglutaric semialdehyde
with NADP+ as cofactor
53.9
alpha-Ketoglutaric semialdehyde
with NAD+ as cofactor
197
alpha-Ketoglutaric semialdehyde
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0.65
Glutaraldehyde
with NADP+ as cofactor
4.13
Glutaraldehyde
with NAD+ as cofactor
0.74
NAD+
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1.08
NADP+
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-
0.58
propanal
with NADP+ as cofactor
2.07
propanal
with NAD+ as cofactor
0.05
succinate semialdehyde
with NADP+ as cofactor
0.06
succinate semialdehyde
with NAD+ as cofactor
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8.5
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2,5-dioxopentanoate + NADP+
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5.2
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not active below, 2,5-dioxopentanoate + NADP+
6.7 - 8.2
more than 50% of maximal activity
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UniProt
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UniProt
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SwissProt
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SwissProt
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strain ATCC29145
UniProt
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strain ATCC29145
SwissProt
brenda
strain ATCC29145
UniProt
brenda
strain ATCC29145
SwissProt
brenda
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brenda
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brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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115000
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sucrose density gradient centrifugation
52290
4 * 52290, calculated from sequence
54351
2 * 57000 or 2 * 54351, gel filtration
55185
2 * 57000 or 2 * 55185, gel filtration
62000
2 * 62000, SDS-PAGE
57000
2 * 57000 or 2 * 54351, gel filtration
57000
2 * 57000 or 2 * 55185, gel filtration
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homodimer
2 * 62000, SDS-PAGE
dimer
2 * 57000 or 2 * 54351, gel filtration
dimer
2 * 57000 or 2 * 55185, gel filtration
dimer
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2 * 57000 or 2 * 55185, gel filtration
dimer
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2 * 57000 or 2 * 54351, gel filtration
tetramer
gel filtration
tetramer
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gel filtration
tetramer
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gel filtration
tetramer
4 * 52290, calculated from sequence
tetramer
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4 * 52290, calculated from sequence
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additional information
alpha-KGSA dehydrogenase activity in cell extracts from the mutant DELTAACIAD0131 grown on succinate as the sole carbon source is undetectable
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86
half-life time: 18 min
90
half-life time: below 10 min
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-35°C, buffer E, pH 8.0, 250 mM imidazole
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KGSADH-II purified on nickel-nitrilotriacetic acid spin column and by gel filtration
KGSADH-III purified on nickel-nitrilotriacetic acid spin column and by gel filtration
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expressed as His6-tagged ycbD protein
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expression in Escherichia coli
expression in Escherichia coli BL21 (DE3)
KGSADH-II overexpressed as His6-tagged protein in Escherichia coli DH5alpha
KGSADH-III overexpressed as His6-tagged protein in Escherichia coli DH5alpha
expression in Escherichia coli
expression in Escherichia coli
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degradation
involved in an alternative pathway of D-glucarate metabolism
degradation
involved in an alternative pathway of D-glucarate metabolism
additional information
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the ALDH branch including ycbD protein is designated the KGSADH subclass (type III)
additional information
three different types of KGSADH appear in the bacterial evolutional stage convergently
additional information
three different types of KGSADH appear in the bacterial evolutional stage convergently
additional information
three different types of KGSADH appear in the bacterial evolutional stage convergently
additional information
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three different types of KGSADH appear in the bacterial evolutional stage convergently
additional information
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three different types of KGSADH appear in the bacterial evolutional stage convergently
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Schimz, K.L.; Kurz, G.
Regulation of L-arabinose metabolism in Pseudomonas fluorescens
Biochem. Soc. Trans.
3
1087-1089
1975
Pseudomonas fluorescens
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Dilworth, M.J.; Arwas, R.; McKay, I.A.; Saroso, S.; Glenn, A.R.
Pentose metabolism in Rhizobium leguminosarum MNF300 and in cowpea Rhizobium NGR234
J. Gen. Microbiol.
132
2733-2742
1986
Bradyrhizobium japonicum, Bradyrhizobium sp., Rhizobium leguminosarum, Sinorhizobium meliloti, Rhizobium sp.
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brenda
Adams, E.; Rosso, G.
alpha-Ketoglutaric semialdehyde dehydrogenase of Pseudomonas. Properties of the purified enzyme induced by hydroxyproline and of the glucarate-induced and constitutive enzymes
J. Biol. Chem.
242
1802-1814
1967
Pseudomonas sp.
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Watanabe, S.; Yamada, M.; Ohtsu, I.; Makino, K.
alpha-ketoglutaric semialdehyde dehydrogenase isozymes involved in metabolic pathways of D-glucarate, D-galactarate, and hydroxy-L-proline. Molecular and metabolic convergent evolution
J. Biol. Chem.
282
6685-6695
2007
Bacillus subtilis, Azospirillum brasilense (Q08IB7), Azospirillum brasilense (Q08IC0), Azospirillum brasilense (Q1JUP4), Azospirillum brasilense, Azospirillum brasilense ATCC 29145 (Q08IB7), Azospirillum brasilense ATCC 29145 (Q08IC0), Azospirillum brasilense ATCC 29145 (Q1JUP4)
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Aghaie, A.; Lechaplais, C.; Sirven, P.; Tricot, S.; Besnard-Gonnet, M.; Muselet, D.; de Berardinis, V.; Kreimeyer, A.; Gyapay, G.; Salanoubat, M.; Perret, A.
New Insights into the Alternative D-Glucarate Degradation Pathway
J. Biol. Chem.
283
15638-15646
2008
Acinetobacter baylyi (Q6FFQ0), Pseudomonas putida (Q88GW5)
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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 (Q97UA1), Saccharolobus solfataricus P2 (Q97UA1)
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Brouns, S.J.; Walther, J.; Snijders, A.P.; van de Werken, H.J.; Willemen, H.L.; Worm, P.; de Vos, M.G.; Andersson, A.; Lundgren, M.; Mazon, H.F.; van den Heuvel, R.H.; Nilsson, P.; Salmon, L.; de Vos, W.M.; Wright, P.C.; Bernander, R.; van der Oost, J.
Identification of the missing links in prokaryotic pentose oxidation pathways: evidence for enzyme recruitment
J. Biol. Chem.
281
27378-27388
2006
Saccharolobus solfataricus (Q97UA1), Saccharolobus solfataricus P2 (Q97UA1)
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