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Enzyme Nomenclature
Information on EC 1.2.1.89 - D-glyceraldehyde dehydrogenase (NADP+)
for references in articles please use BRENDA:EC1.2.1.89
Word Map on EC 1.2.1.89
- 1.2.1.89
- enolase
- acidophilum
-
thermoplasma
-
entner-doudoroff
-
gadhs
-
thermoacidophilic
- isobutanol
- d-glycerate
- euryarchaeota
- synthesis
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The expected taxonomic range for this enzyme is: Bacteria, Archaea
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EC NUMBER 
COMMENTARY 
1.2.1.89
-
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RECOMMENDED NAME
GeneOntology No.
D-glyceraldehyde dehydrogenase (NADP+)
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-glyceraldehyde + NADP+ + H2O = D-glycerate + NADPH + H+
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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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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
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+
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+
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
-
-
-
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
-
-
-
additional information
?
-
-
no activity with acetaldehyde and isobutyraldehyde
-
-
-
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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-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
mutants N286E, N286H, N286T, but not wild-type show activtiy 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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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-glyceraldehyde
slight substrate inhibition, 25% inhibition at 2 mM
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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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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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
58
63
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 70
-
30°C: about 50% of maximal activity, 70°C: about 60% of maximal activity
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
56000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
homotetramer
tetramer
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
-
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
70
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
guanidine-HCl
isobutanol
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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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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/S405N
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
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
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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LINKS TO OTHER DATABASES (specific for EC-Number 1.2.1.89)
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