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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 EntnerDoudoroff 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 EntnerDoudoroff 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+
-
-
-
-
?
D-glyceraldehyde + NADP+ + H2O
D-glycerate + NADPH + H+
the enzyme is involved in downstream portion of the non-phosphorylated EntnerDoudoroff pathway
-
-
?
D-glyceraldehyde + NADP+ + H2O
D-glycerate + NADPH + H+
the enzyme is involved in the non-phosphorylative EntnerDoudoroff 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+
-
-
-
?
D-glyceraldehyde + NADP+ + H2O
D-glycerate + NADPH + H+
the enzyme is involved in downstream portion of the non-phosphorylated EntnerDoudoroff 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 EntnerDoudoroff 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
?
-
NAD+ is a poor substrate
-
-
-
additional information
?
-
-
NAD+ is a poor substrate
-
-
-
additional information
?
-
no activity with acetaldehyde and isobutyraldehyde
-
-
?
additional information
?
-
NAD+ is a poor substrate
-
-
-
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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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
F34M/S405N
-
the mutant shows a slight increase in NAD+ acceptance and a 9fold improvement in catalytic efficiency with NAD+ compared with the wild type enzyme
-
F34M/S405N
crystallization data
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
F34M/S405N
the mutant shows a slight increase in NAD+ acceptance and a 9fold improvement in catalytic efficiency with NAD+ compared with the wild type enzyme
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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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.; Schnheit, 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
Iermak, I.; Degtjarik, O.; Steffler, F.; Sieber, V.; Kuta Smatanova, I.
Crystallization behaviour of glyceraldehyde dehydrogenase from Thermoplasma acidophilum
Acta Crystallogr. F Struct. Biol. Commun.
71
1475-1480
2015
Thermoplasma acidophilum (Q9HK01), Thermoplasma acidophilum, Thermoplasma acidophilum ATCC 25905 (Q9HK01)
brenda