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Information on EC 1.2.1.89 - D-glyceraldehyde dehydrogenase (NADP+) for references in articles please use BRENDA:EC1.2.1.89Word Map on EC 1.2.1.89
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The expected taxonomic range for this enzyme is: Bacteria, Archaea
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D-glyceraldehyde dehydrogenase (NADP+)
-
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D-glyceraldehyde + NADP+ + H2O = D-glycerate + NADPH + H+
-
-
-
-
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Entner Doudoroff pathway
-
-
Pentose phosphate pathway
-
-
Microbial metabolism in diverse environments
-
-
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D-glyceraldehyde:NADP+ oxidoreductase
The enzyme from the archaea Thermoplasma acidophilum and Picrophilus torridus is involved in the non-phosphorylative Entner-Doudoroff pathway. cf. EC 1.2.99.8, glyceraldehyde dehydrogenase (FAD-containing).
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glyceraldehyde dehydrogenase
GADH
-
GLD
gene name
glyceraldehyde dehydrogenase
-
glyceraldehyde dehydrogenase
-
-
Pto0332
locus name
Ta0809
gene name
Ta0809
locus name; locus name; locus name
-
TaAlDH
-
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cf. EC 1.2.1.22
SwissProt
brenda
-
UniProt
brenda
-
UniProt
brenda
-
UniProt
brenda
-
UniProt
brenda
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physiological function
-
the enzyme is involved in downstream portion of the non-phosphorylated Entner–Doudoroff pathway
physiological function
the enzyme is involved in the non-phosphorylative Entner–Doudoroff pathway
physiological function
-
the enzyme is involved in the non-phosphorylative Entner–Doudoroff pathway
physiological function
-
the enzyme is involved in the non-phosphorylative Entner–Doudoroff pathway
-
physiological function
-
the enzyme is involved in downstream portion of the non-phosphorylated Entner–Doudoroff pathway; the enzyme is involved in the non-phosphorylative Entner–Doudoroff pathway
-
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D-glyceraldehyde + NAD+
D-glycerate + NADH + H+
-
NAD+ is a very poor cofactor for wild-type
-
-
?
D-glyceraldehyde + NAD+ + H2O
D-glycerate + NADH + H+
activity of mutants N286E, N286H, N286T. No substrate for wild-type
-
-
?
D-glyceraldehyde + NADP+ + H2O
D-glycerate + NADPH + H+
D-glyceraldehyde 3-phosphate + NADP+ + H2O
D-glycerate 3-phosphate + NADPH + H+
glyceraldehyde + NAD+ + H2O
glycerate + NADH + H+
-
-
-
-
?
glycolaldehyde + NADP+
glycolate + NADPH + H+
additional information
?
-
D-glyceraldehyde + NADP+ + H2O
D-glycerate + NADPH + H+
the enzyme is involved in the non-phosphorylative Entner–Doudoroff pathway
-
-
?
D-glyceraldehyde + NADP+ + H2O
D-glycerate + NADPH + H+
completely inactive with NAD+
-
-
?
D-glyceraldehyde + NADP+ + H2O
D-glycerate + NADPH + H+
the enzyme is involved in the non-phosphorylative Entner–Doudoroff pathway
-
-
?
D-glyceraldehyde + NADP+ + H2O
D-glycerate + NADPH + H+
completely inactive with NAD+
-
-
?
D-glyceraldehyde + NADP+ + H2O
D-glycerate + NADPH + H+
-
-
-
-
?
D-glyceraldehyde + NADP+ + H2O
D-glycerate + NADPH + H+
the enzyme is involved in downstream portion of the non-phosphorylated Entner–Doudoroff pathway
-
-
?
D-glyceraldehyde + NADP+ + H2O
D-glycerate + NADPH + H+
-
the enzyme is involved in the non-phosphorylative Entner–Doudoroff pathway
-
-
?
D-glyceraldehyde + NADP+ + H2O
D-glycerate + NADPH + H+
-
also accepts NAD+ under technically relevant conditions, cofactor above 1 mM
-
-
?
D-glyceraldehyde + NADP+ + H2O
D-glycerate + NADPH + H+
completely inactive when NAD+ is substituted for NADP+
-
-
?
D-glyceraldehyde + NADP+ + H2O
D-glycerate + NADPH + H+
-
completely inactive with NAD+
-
-
?
D-glyceraldehyde + NADP+ + H2O
D-glycerate + NADPH + H+
the enzyme is involved in downstream portion of the non-phosphorylated Entner–Doudoroff pathway
-
-
?
D-glyceraldehyde + NADP+ + H2O
D-glycerate + NADPH + H+
completely inactive when NAD+ is substituted for NADP+
-
-
?
D-glyceraldehyde + NADP+ + H2O
D-glycerate + NADPH + H+
-
the enzyme is involved in the non-phosphorylative Entner–Doudoroff pathway
-
-
?
D-glyceraldehyde + NADP+ + H2O
D-glycerate + NADPH + H+
-
completely inactive with NAD+
-
-
?
D-glyceraldehyde + NADP+ + H2O
D-glycerate + NADPH + H+
-
also accepts NAD+ under technically relevant conditions, cofactor above 1 mM
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
D-glycerate 3-phosphate + NADPH + H+
catalytic efficiency (kcat/Km) for D-glyceraldehyde 3-phosphate is 1.4% compared to the catalytic efficiency with D-glyceraldehyde
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
D-glycerate 3-phosphate + NADPH + H+
catalytic efficiency (kcat/Km) for D-glyceraldehyde 3-phosphate is 1.4% compared to the catalytic efficiency with D-glyceraldehyde
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
D-glycerate 3-phosphate + NADPH + H+
activity is 33% compared to the activity with D-glyceraldehyde
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
D-glycerate 3-phosphate + NADPH + H+
-
catalytic efficiency (kcat/Km) for glyceraldehyde 3-phosphate is less than 1% compared to the catalytic efficiency with D-glyceraldehyde
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
D-glycerate 3-phosphate + NADPH + H+
activity is 33% compared to the activity with D-glyceraldehyde
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
D-glycerate 3-phosphate + NADPH + H+
-
catalytic efficiency (kcat/Km) for glyceraldehyde 3-phosphate is less than 1% compared to the catalytic efficiency with D-glyceraldehyde
-
-
?
glycolaldehyde + NADP+
glycolate + NADPH + H+
catalytic efficiency (kcat/Km) for glycolaldehyde is 1% compared to the catalytic efficiency with D-glyceraldehyde
-
-
?
glycolaldehyde + NADP+
glycolate + NADPH + H+
catalytic efficiency (kcat/Km) for glycolaldehyde is 1% compared to the catalytic efficiency with D-glyceraldehyde
-
-
?
glycolaldehyde + NADP+
glycolate + NADPH + H+
activity is 14% compared to the activity with D-glyceraldehyde
-
-
?
glycolaldehyde + NADP+
glycolate + NADPH + H+
-
catalytic efficiency (kcat/Km) for glycolaldehyde is about 2% compared to the catalytic efficiency with D-glyceraldehyde
-
-
?
glycolaldehyde + NADP+
glycolate + NADPH + H+
activity is 14% compared to the activity with D-glyceraldehyde
-
-
?
glycolaldehyde + NADP+
glycolate + NADPH + H+
-
catalytic efficiency (kcat/Km) for glycolaldehyde is about 2% compared to the catalytic efficiency with D-glyceraldehyde
-
-
?
additional information
?
-
-
no activity with: acetaldehyde, crotonaldehyde, benzaldehyde, succinate semialdehyde, and dihydroxyacetone
-
-
-
additional information
?
-
no activity with: acetaldehyde, crotonaldehyde, benzaldehyde, succinate semialdehyde, and dihydroxyacetone
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-
-
additional information
?
-
no activity with: acetaldehyde, crotonaldehyde, benzaldehyde, succinate semialdehyde, and dihydroxyacetone
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-
-
additional information
?
-
no activity towards ketoaldehyde (methylglyoxal), alkyl aldehydes (formaldehyde, acetaldehyde and propionaldehyde) or aromatic aldehydes (phenylacetaldehyde and 4-nitrobenzaldehyde)
-
-
-
additional information
?
-
-
no activity with acetaldehyde, propionaldehyde, n-butyraldehyde, pyruvaldehyde, isobutyraldehyde or D-glucose
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-
-
additional information
?
-
-
no activity with acetaldehyde and isobutyraldehyde
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-
-
additional information
?
-
no activity towards ketoaldehyde (methylglyoxal), alkyl aldehydes (formaldehyde, acetaldehyde and propionaldehyde) or aromatic aldehydes (phenylacetaldehyde and 4-nitrobenzaldehyde)
-
-
-
additional information
?
-
-
no activity with acetaldehyde, propionaldehyde, n-butyraldehyde, pyruvaldehyde, isobutyraldehyde or D-glucose
-
-
-
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D-glyceraldehyde + NADP+ + H2O
D-glycerate + NADPH + H+
D-glyceraldehyde + NADP+ + H2O
D-glycerate + NADPH + H+
Q6L285
the enzyme is involved in the non-phosphorylative Entner–Doudoroff pathway
-
-
?
D-glyceraldehyde + NADP+ + H2O
D-glycerate + NADPH + H+
Q6L285
the enzyme is involved in the non-phosphorylative Entner–Doudoroff pathway
-
-
?
D-glyceraldehyde + NADP+ + H2O
D-glycerate + NADPH + H+
Q9HK01
the enzyme is involved in downstream portion of the non-phosphorylated Entner–Doudoroff pathway
-
-
?
D-glyceraldehyde + NADP+ + H2O
D-glycerate + NADPH + H+
-
the enzyme is involved in the non-phosphorylative Entner–Doudoroff pathway
-
-
?
D-glyceraldehyde + NADP+ + H2O
D-glycerate + NADPH + H+
Q9HK01
the enzyme is involved in downstream portion of the non-phosphorylated Entner–Doudoroff pathway
-
-
?
D-glyceraldehyde + NADP+ + H2O
D-glycerate + NADPH + H+
-
the enzyme is involved in the non-phosphorylative Entner–Doudoroff pathway
-
-
?
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NADPH
-
NADPH is preferred over NADH
NAD+
-
-
NAD+
mutants N286E, N286H, N286T, but not wild-type show activtiy with NAD+
NADP+
-
completely inactive when NAD+ is substituted for NADP+
NADP+
completely inactive with NAD+
NADP+
-
completely inactive with NAD+
NADP+
-
also accepts NAD+ under technically relevant conditions, cofactor above 1 mM, Km for NADP+: 0.022 mM, Km for NAD+ is 22.13 mM, at H 6.2, 50°C
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Ca2+
-
1 mM, 12 h, 4°C, complete loss of activity
Cd2+
-
1 mM, 12 h, 4°C, 93% loss of activity
Cu2+
-
1 mM, 12 h, 4°C, complete loss of activity
D-glyceraldehyde
slight substrate inhibition, 25% inhibition at 2 mM
Hg2+
-
1 mM, 12 h, 4°C, 99% loss of activity
Mg2+
-
1 mM, 12 h, 4°C, 24% loss of activity
Mn2+
-
1 mM, 12 h, 4°C, 44% loss of activity
Ni2+
-
1 mM, 12 h, 4°C, 58% loss of activity
Zn2+
-
1 mM, 12 h, 4°C, 46% loss of activity
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2-mercaptoethanol
-
1 mM, activity is enhanced more than 2fold
4-chloromercuribenzoic acid
-
1 mM, completely inhibits activity
4-hydroxymercuribenzoic acid
-
1 mM, completely inhibits activity
DTT
-
1 mM, activity is enhanced more than 2fold
glutathione
-
1 mM, activity is enhanced more than 2fold
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0.06 - 2.2
D-glyceraldehyde
11.1 - 12.3
glycolaldehyde
0.06
D-glyceraldehyde
pH 6.9, 58°C
0.2
D-glyceraldehyde
-
pH 6.9, 58°C
0.33
D-glyceraldehyde
-
pH 8.0, 50°C
1.14
D-glyceraldehyde
mutant N286H, pH 7.0, 37°C
1.97
D-glyceraldehyde
mutant N286H, pH 7.0, 37°C
2.2
D-glyceraldehyde
mutant N286H, pH 7.0, 37°C
5.1
D-glycerate
pH 6.9, 58°C
18.3
D-glycerate
-
pH 6.9, 58°C
11.1
glycolaldehyde
pH 6.9, 58°C
12.3
glycolaldehyde
-
pH 6.9, 58°C
16.7
NAD+
-
mutant enzyme F34M/Y399C/S405N, at pH 7.0 and 50°C; mutant F34M/Y399C/S405N, pH 7.0, 50°C
17.6
NAD+
-
mutant enzyme F34M/S405N, at pH 7.0 and 50°C; mutant F34M/S405N, pH 7.0, 50°C
22.7
NAD+
-
wild type enzyme, at pH 7.0 and 50°C; wild-type, pH 7.0, 50°C
0.017
NADP+
-
pH 8.0, 50°C
0.021
NADP+
-
wild-type, pH 7.0, 50°C
0.022
NADP+
-
pH 6.2, 50°C
0.031
NADP+
-
mutant F34M/Y399C/S405N, pH 7.0, 50°C
0.036
NADP+
-
mutant F34M/S405N, pH 7.0, 50°C
0.36
NADP+
-
pH 6.9, 58°C
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10 - 957
D-glyceraldehyde
10
D-glyceraldehyde
pH 6.9, 58°C
26
D-glyceraldehyde
-
pH 6.9, 58°C
69.6
D-glyceraldehyde
mutant N286H, pH 7.0, 37°C
113.1
D-glyceraldehyde
mutant N286H, pH 7.0, 37°C
957
D-glyceraldehyde
mutant N286H, pH 7.0, 37°C
12
D-glycerate
pH 6.9, 58°C
20
D-glycerate
-
pH 6.9, 58°C
20
glycolaldehyde
pH 6.9, 58°C
37
glycolaldehyde
-
pH 6.9, 58°C
1.64
NAD+
-
wild type enzyme, at pH 7.0 and 50°C; wild-type, pH 7.0, 50°C
10.54
NAD+
-
mutant enzyme F34M/Y399C/S405N, at pH 7.0 and 50°C; mutant F34M/Y399C/S405N, pH 7.0, 50°C
10.99
NAD+
-
mutant enzyme F34M/S405N, at pH 7.0 and 50°C; mutant F34M/S405N, pH 7.0, 50°C
10
NADP+
pH 6.9, 58°C
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31.64 - 485.8
D-glyceraldehyde
31.64
D-glyceraldehyde
mutant N286H, pH 7.0, 37°C
99.2
D-glyceraldehyde
mutant N286H, pH 7.0, 37°C
130
D-glyceraldehyde
-
pH 6.9, 58°C
167
D-glyceraldehyde
pH 6.9, 58°C
485.8
D-glyceraldehyde
mutant N286H, pH 7.0, 37°C
1.1
D-glycerate
-
pH 6.9, 58°C
2.4
D-glycerate
pH 6.9, 58°C
1.8
glycolaldehyde
pH 6.9, 58°C
3
glycolaldehyde
-
pH 6.9, 58°C
0.07
NAD+
-
wild type enzyme, at pH 7.0 and 50°C; wild-type, pH 7.0, 50°C
0.62
NAD+
-
mutant enzyme F34M/S405N, at pH 7.0 and 50°C; mutant F34M/S405N, pH 7.0, 50°C
0.63
NAD+
-
mutant enzyme F34M/Y399C/S405N, at pH 7.0 and 50°C; mutant F34M/Y399C/S405N, pH 7.0, 50°C
24
NADP+
pH 6.9, 58°C
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0.08
mutant N286H, pH 7.0, 37°C
0.13
mutant N286H, pH 7.0, 37°C
1.1
mutant N286H, pH 7.0, 37°C
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4.3 - 8.1
pH 4.3: about 50% of maximal activity, pH 8.1: about 50% of maximal activity
5.8 - 8.7
-
pH 5.8: about 50% of maximal activity, pH 8.7: about 50% of maximal activity
6 - 10
-
pH 6.0: about 65% of maximal activity, pH 10.0: about 70% of maximal activity
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58
assay at
63
-
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30 - 70
-
30°C: about 50% of maximal activity, 70°C: about 60% of maximal activity
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Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
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53000
-
4 * 53000, SDS-PAGE
54700
-
2 * 54700, calculated from sequence
54782
-
4 * 54782, calculated from sequence
55000
-
x * 55000, SDS-PAGE
55200
2 * 55200, calculated from sequence
56000
2 * 56000, SDS-PAGE
56000
-
2 * 56000, SDS-PAGE
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homodimer
2 * 55200, calculated from sequence; 2 * 56000, SDS-PAGE
homodimer
-
2 * 55200, calculated from sequence; 2 * 56000, SDS-PAGE
-
homodimer
-
2 * 54700, calculated from sequence; 2 * 56000, SDS-PAGE
homodimer
-
2 * 54700, calculated from sequence; 2 * 56000, SDS-PAGE
-
homotetramer
-
4 * 53000, SDS-PAGE
homotetramer
-
4 * 53000, SDS-PAGE
-
tetramer
-
4 * 54782, calculated from sequence
tetramer
-
4 * 54782, calculated from sequence
-
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structures of wild-type and mutant F34M/S405N, to 1.95 A resolution for wild-type and 2.14 and 2.10 A resolution for the mutant
-
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6 - 8
-
24 h, stable
724216
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55
1 h, 70% residual activity for mutant N286T
80
-
activity is decreased to less than 50% within 20 min
60
2 h, stable
70
half-life: 15 min
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guanidine-HCl
-
the stability of the enzyme is ca. 28 kJ/mol both at 25°C and 40°C
guanidine-HCl
-
the stability of the enzyme is ca. 28 kJ/mol both at 25°C and 40°C
-
isobutanol
-
the stability of the enzyme is ca. 28 kJ/mol both at 25°C and 40°C
isobutanol
-
wild-type, 50% residual activity at 3.1%, mutant F34M/S405N at 3.6%, mutant F34M/Y399C/S405N at 3.5%, respectively
isobutanol
-
the stability of the enzyme is ca. 28 kJ/mol both at 25°C and 40°C
-
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HiTrap column chromatography
-
-
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; expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
the gene of TaAlDH is synthesized and cloned into a T7 based vector system for recombinant expression in Escherichia coli. Using matrix-assisted refolding of inclusion bodies the yield of enzyme production is enhanced 43fold
-
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N286E
engineering of L-lactaldehyde dehydrogenase. Contrary to wild-type, mutant is able to oxidate glyceraldehyde
N286H
engineering of L-lactaldehyde dehydrogenase. Contrary to wild-type, mutant is able to oxidate glyceraldehyde
N286T
engineering of L-lactaldehyde dehydrogenase. Contrary to wild-type, mutant is able to oxidate glyceraldehyde. Compared to L-lactaldehyde, N286T has a one-third lower Km value to glyceraldehyde.
34M/Y399C/S405N
-
the mutations enhance enzyme activity with the cofactor NAD+ by a factor of 55.7
F34L
-
the mutation enhances enzyme activity with the cofactor NAD+ by a factor of 3.2
F34M/D372N/S405N
-
the mutations enhance enzyme activity with the cofactor NAD+ by a factor of 7.2
F34M/D372N/Y399C/S405N
-
the mutations enhance enzyme activity with the cofactor NAD+ by a factor of 35.1
F34M/W271R/S405N
-
the mutations enhance enzyme activity with the cofactor NAD+ by a factor of 22.6
F34M/W271S/S405N
-
the mutations enhance enzyme activity with the cofactor NAD+ by a factor of 42.5
F34M/W271S/Y399C/S405N
-
the mutations enhance enzyme activity with the cofactor NAD+ by a factor of 1.1
F34M/Y399C/S405N
-
enhances enzyme activity with the cofactor NAD+ by a factor of eight and enhances solubilty
S405C
-
the mutation enhances enzyme activity with the cofactor NAD+ by a factor of 6
S405N
-
the mutation enhances enzyme activity with the cofactor NAD+ by a factor of 7.4
W271S
-
the mutations enhance enzyme activity with the cofactor NAD+ by a factor of 17.1
Y399C
-
enhances the protein solubility after recombinant expression in Escherichia coli 6fold; the mutation enhances the protein solubility after recombinant expression in Escherichia coli 6fold and enhances enzyme activity with the cofactor NAD+ by a factor of 6.4
F34M/S405N
-
enhances enzyme activity with the cofactor NAD+ by a factor of eight; the mutations enhance enzyme activity with the cofactor NAD+ by a factor of 8.5 while impacts on enzyme stability and substrate specificity are negligible
F34M/S405N
-
crystallization data
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synthesis
-
the enzyme accept NAD+ as cofactor under technically relevant conditions, making it suitable for application in the artificial glycolysis by synthetic cascade biomanufacturing
synthesis
-
the enzyme accept NAD+ as cofactor under technically relevant conditions, making it suitable for application in the artificial glycolysis by synthetic cascade biomanufacturing
-
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GADH_PICTO
Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)
493
55163
Swiss-Prot
GADH_THEAC
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
493
54782
Swiss-Prot
ALDA_ECOLI
Escherichia coli (strain K12)
479
52273
Swiss-Prot
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Jung, J.H.; Lee, S.B.
Identification and characterization of Thermoplasma acidophilum glyceraldehyde dehydrogenase: a new class of NADP+-specific aldehyde dehydrogenase
Biochem. J.
397
131-138
2006
Thermoplasma acidophilum (Q9HK01), Thermoplasma acidophilum, Thermoplasma acidophilum JCM 9062 (Q9HK01)
brenda
Reher, M.; Schönheit, P.
Glyceraldehyde dehydrogenases from the thermoacidophilic euryarchaeota Picrophilus torridus and Thermoplasma acidophilum, key enzymes of the non-phosphorylative Entner-Doudoroff pathway, constitute a novel enzyme family within the aldehyde dehydrogenase superfamily
FEBS Lett.
580
1198-1204
2006
Picrophilus torridus, Picrophilus torridus (Q6L285), Picrophilus torridus DSM 9790 (Q6L285), Thermoplasma acidophilum (Q9HK01), Thermoplasma acidophilum, Thermoplasma acidophilum JCM 9062 (Q9HK01)
brenda
Steffler, F.; Sieber, V.
Refolding of a thermostable glyceraldehyde dehydrogenase for application in synthetic cascade biomanufacturing
PLoS One
8
e70592
2013
Thermoplasma acidophilum (Q9HK01), Thermoplasma acidophilum, Thermoplasma acidophilum JCM 9062 (Q9HK01)
brenda
Steffler, F.; Guterl, J.K.; Sieber, V.
Improvement of thermostable aldehyde dehydrogenase by directed evolution for application in Synthetic Cascade Biomanufacturing
Enzyme Microb. Technol.
53
307-314
2013
Thermoplasma acidophilum (Q9HK01)
brenda
Iermak, I.; Degtjarik, O.; Steffler, F.; Sieber, V.; Kuta Smatanova, I.
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Thermoplasma acidophilum (Q9HK01)
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Wu, X.; Xu, L.; Yan, M.
A new NAD(+)-dependent glyceraldehyde dehydrogenase obtained by rational design of l-lactaldehyde dehydrogenase from Escherichia coli
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Escherichia coli, Escherichia coli (P25553)
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