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Information on EC 1.2.1.89 - D-glyceraldehyde dehydrogenase (NADP+)
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1.2.1.89 D-glyceraldehyde dehydrogenase (NADP+)IUBMB Comments
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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Word Map
- 1.2.1.89
- enolase
-
thermoplasma
- acidophilum
-
entner-doudoroff
- beta-sitosterol
- stigmasterol
- synthesis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
glyceraldehyde dehydrogenase, ta0809, taaldh, pto0332, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
GADH
GLD
glyceraldehyde dehydrogenase
Pto0332
Ta0809
TaAlDH
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-glyceraldehyde + NADP+ + H2O = D-glycerate + NADPH + H+
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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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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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+
-
-
?
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
-
?
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 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, 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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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
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+
the enzyme is involved in the non-phosphorylative Entner–Doudoroff pathway
-
-
?
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+
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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INHIBITOR
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
4-chloromercuribenzoic acid
1 mM, completely inhibits activity
4-hydroxymercuribenzoic acid
1 mM, completely inhibits activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
10.54
NAD+
mutant enzyme F34M/Y399C/S405N, at pH 7.0 and 50°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
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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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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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 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
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GADH_PICTO
Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)
493
0
55163
Swiss-Prot
-
GADH_THEAC
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
493
0
54782
Swiss-Prot
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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)
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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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
homotetramer
tetramer
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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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PROTEIN VARIANTS
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
F34M/S405N
enhances enzyme activity with the cofactor NAD+ by a factor of eight
F34M/S405N
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
Y399C
enhances the protein solubility after recombinant expression in Escherichia coli 6fold
Y399C
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
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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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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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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 (Q6L285), Picrophilus torridus, Thermoplasma acidophilum (Q9HK01), Thermoplasma acidophilum, Thermoplasma acidophilum JCM 9062 (Q9HK01), Picrophilus torridus DSM 9790 (Q6L285)
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.
Crystallization behaviour of glyceraldehyde dehydrogenase from Thermoplasma acidophilum
Acta Crystallogr. Sect. F
71
1475-1480
2015
Thermoplasma acidophilum (Q9HK01)
brenda
Wu, X.; Xu, L.; Yan, M.
A new NAD(+)-dependent glyceraldehyde dehydrogenase obtained by rational design of l-lactaldehyde dehydrogenase from Escherichia coli
Biosci. Biotechnol. Biochem.
80
2306-2310
2016
Escherichia coli (P25553), Escherichia coli
brenda
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