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(R)-2-hydroxy-4-methylpentanoate + NAD+
4-methyl-2-oxopentanoate + NADH + H+
-
i.e. (R)-2-hydroxyisocaproate
i.e. 2-oxoisocaproate
-
r
(R)-2-hydroxycarboxylate + NAD+
a 2-oxocarboxylate + NADH + H+
(R)-mandelate + NAD+
phenylglyoxylate + NADH + H+
2-formylbutanethioate + NADH + H+
?
2-hydroxyhexanoate + NAD+
2-oxohexanoate + NADH + H+
-
-
-
-
r
2-hydroxyoctanoate + NAD+
2-oxooctanoate + NADH + H+
-
-
-
-
r
2-hydroxypentanoate + NAD+
2-oxopentanoate + NADH + H+
-
-
-
-
r
2-oxo-3-phenylpropanoate + NADH + H+
2-hydroxy-3-phenylpropanoate + NAD+
2-oxobutanoate + NADH + H+
2-hydroxybutanoate + NAD+
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
2-oxobutyrate + NADH + H+
?
2-oxobutyrate + NADH + H+
? + NAD+
2-oxobutyrate + NADH + H+
D-2-hydroxybutyrate + NAD+
2-oxocaproate + NADH + H+
?
2-oxocaproate + NADH + H+
? + NAD+
2-oxocarboxylate + NADH + H+
(R)-2-hydroxycarboxylate + NAD+
2-oxohexanoate + NADH + H+
2-hydroxyhexanoate + NAD+
2-oxoisocaproate + NADH + H+
?
2-oxoisocaproate + NADH + H+
? + NAD+
2-oxoisocaproate + NADH + H+
L-2-hydroxyisocaproate + NAD+
2-oxoisovalerate + NADH + H+
?
2-oxoisovalerate + NADH + H+
? + NAD+
-
-
-
-
r
2-oxomethylthiobutyrate + NADH + H+
? + NAD+
-
-
-
-
r
2-oxomethylvalerate + NADH + H+
? + NAD+
-
-
-
-
r
2-oxooctanoate + NADH + H+
2-hydroxyoctanoate + NAD+
-
-
-
-
r
2-oxopentanoate + NADH + H+
2-hydroxypentanoate + NAD+
2-oxovalerate + NADH + H+
?
-
-
-
-
?
2-oxovalerate + NADH + H+
? + NAD+
-
-
-
-
r
3-(4-hydroxyphenyl)-2-oxopropanoate + NADH + H+
2-hydroxy-3-(4-hydroxyphenyl)propanoate + NAD+
-
-
-
-
?
3-hydroxypyruvate + NADH + H+
?
-
-
-
-
?
3-methyl-2-oxobutanoate + NADH + H+
2-hydroxy-3-methylbutanoate + NAD+
3-methyl-2-oxobutanoate + NADH + H+
3-methyl-2-hydroxybutanoate + NAD+
3-methyl-2-oxopentanoate + NADH + H+
2-hydroxy-3-methylpentanoate + NAD+
4-methyl-2-oxopentanoate + NADH + H+
(R)-2-hydroxy-4-methylpentanoate + NAD+
4-methyl-2-oxopentanoate + NADH + H+
4-methyl-2-hydroxypentanoate + NAD+
-
highest Vmax/Km value of all substrates tested
-
-
?
benzoylformate + NADH + H+
?
benzoylformate + NADH + H+
? + NAD+
-
-
-
-
r
D-2-hydroxybutyrate + NAD+
2-oxobutyrate + NADH + H+
D-lactate + NAD+
pyruvate + NADH + H+
-
-
-
-
r
D-malate + NAD+
oxaloacetate + NADH + H+
D-mandelate + NADH + H+
? + NAD+
-
-
-
-
r
DL-2-hydroxyisocaproate + NADH + H+
? + NAD+
-
-
-
-
r
L-2-hydroxycaproate + NAD+
2-oxocaproate + NADH + H+
-
-
-
-
r
oxaloacetate + NADH + H+
D-malate + NAD+
phenylglyoxylate + NADH + H+
hydroxy(phenyl)acetic acid + NAD+
phenylpyruvate + NADH + H+
?
-
-
-
-
?
phenylpyruvate + NADH + H+
? + NAD+
phenylpyruvate + NADH + H+
phenyl-D-lactate + NAD+
phenylpyruvate + NADH + H+
phenyllactate + NAD+
pyruvate + NADH + H+
D-lactate + NAD+
pyruvate + NADH + H+
lactate + NAD+
additional information
?
-
(R)-2-hydroxycarboxylate + NAD+
a 2-oxocarboxylate + NADH + H+
-
-
-
r
(R)-2-hydroxycarboxylate + NAD+
a 2-oxocarboxylate + NADH + H+
-
-
-
r
(R)-mandelate + NAD+
phenylglyoxylate + NADH + H+
-
Vmax/Km is 0.4% compared to 4-methyl-2-oxopentanoate
-
-
?
(R)-mandelate + NAD+
phenylglyoxylate + NADH + H+
-
Vmax/Km is 1% compared to 4-methyl-2-oxopentanoate
-
-
?
(R)-mandelate + NAD+
phenylglyoxylate + NADH + H+
-
Vmax/KM is less than 1% compared to 4-methyl-2-oxopentanoate
-
-
?
2-formylbutanethioate + NADH + H+
?
-
i.e. 2-ketomethylthiobutyrate
-
-
?
2-formylbutanethioate + NADH + H+
?
-
i.e. 2-ketomethylthiobutyrate
-
-
?
2-oxo-3-phenylpropanoate + NADH + H+
2-hydroxy-3-phenylpropanoate + NAD+
-
Vmax/KM is 1.9% compared to 4-methyl-2-oxopentanoate
-
-
?
2-oxo-3-phenylpropanoate + NADH + H+
2-hydroxy-3-phenylpropanoate + NAD+
-
Vmax/Km is 2.7% compared to 4-methyl-2-oxopentanoate
-
-
?
2-oxobutanoate + NADH + H+
2-hydroxybutanoate + NAD+
-
Vmax/Km is 0.25% compared to 4-methyl-2-oxopentanoate
-
-
?
2-oxobutanoate + NADH + H+
2-hydroxybutanoate + NAD+
-
Vmax/KM is less than 1% compared to 4-methyl-2-oxopentanoate
-
-
?
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
-
-
-
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
-
-
-
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
-
-
-
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
-
-
-
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
-
-
-
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
-
-
-
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
-
-
-
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
-
-
-
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
-
-
-
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
-
-
-
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
-
-
-
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
-
-
-
r
2-oxobutyrate + NADH + H+
?
-
-
-
-
?
2-oxobutyrate + NADH + H+
?
-
-
-
-
?
2-oxobutyrate + NADH + H+
? + NAD+
-
-
-
-
r
2-oxobutyrate + NADH + H+
? + NAD+
-
-
-
-
r
2-oxobutyrate + NADH + H+
D-2-hydroxybutyrate + NAD+
-
55% activity compared to pyruvate
-
-
r
2-oxobutyrate + NADH + H+
D-2-hydroxybutyrate + NAD+
-
55% activity compared to pyruvate
-
-
r
2-oxocaproate + NADH + H+
?
-
-
-
-
?
2-oxocaproate + NADH + H+
?
-
-
-
-
?
2-oxocaproate + NADH + H+
? + NAD+
-
-
-
-
r
2-oxocaproate + NADH + H+
? + NAD+
-
-
-
-
r
2-oxocarboxylate + NADH + H+
(R)-2-hydroxycarboxylate + NAD+
-
-
-
-
r
2-oxocarboxylate + NADH + H+
(R)-2-hydroxycarboxylate + NAD+
-
-
-
-
r
2-oxohexanoate + NADH + H+
2-hydroxyhexanoate + NAD+
-
Vmax/KM is 3% compared to 4-methyl-2-oxopentanoate
-
-
?
2-oxohexanoate + NADH + H+
2-hydroxyhexanoate + NAD+
-
Vmax/Km is 4.1% compared to 4-methyl-2-oxopentanoate
-
-
?
2-oxohexanoate + NADH + H+
2-hydroxyhexanoate + NAD+
-
Vmax/Km is 5.1% compared to 4-methyl-2-oxopentanoate
-
-
?
2-oxohexanoate + NADH + H+
2-hydroxyhexanoate + NAD+
-
i.e. 2-oxovalerate
-
-
r
2-oxohexanoate + NADH + H+
2-hydroxyhexanoate + NAD+
i.e. 2-oxocaproate
-
-
r
2-oxohexanoate + NADH + H+
2-hydroxyhexanoate + NAD+
i.e. 2-oxocaproate
-
-
?
2-oxoisocaproate + NADH + H+
?
-
-
-
-
?
2-oxoisocaproate + NADH + H+
?
-
-
-
-
?
2-oxoisocaproate + NADH + H+
? + NAD+
-
-
-
-
r
2-oxoisocaproate + NADH + H+
? + NAD+
-
-
-
-
r
2-oxoisocaproate + NADH + H+
L-2-hydroxyisocaproate + NAD+
-
29% activity compared to pyruvate
-
-
r
2-oxoisocaproate + NADH + H+
L-2-hydroxyisocaproate + NAD+
-
29% activity compared to pyruvate
-
-
r
2-oxoisovalerate + NADH + H+
?
-
-
-
-
?
2-oxoisovalerate + NADH + H+
?
-
-
-
-
?
2-oxopentanoate + NADH + H+
2-hydroxypentanoate + NAD+
-
Vmax/KM is 10.6% compared to 4-methyl-2-oxopentanoate
-
-
?
2-oxopentanoate + NADH + H+
2-hydroxypentanoate + NAD+
-
Vmax/Km is 5.8% compared to 4-methyl-2-oxopentanoate
-
-
?
2-oxopentanoate + NADH + H+
2-hydroxypentanoate + NAD+
-
Vmax/Km is 7.6% compared to 4-methyl-2-oxopentanoate
-
-
?
2-oxopentanoate + NADH + H+
2-hydroxypentanoate + NAD+
-
i.e. 2-oxocaproate
-
-
r
2-oxopentanoate + NADH + H+
2-hydroxypentanoate + NAD+
i.e. 2-oxovalerate
-
-
r
2-oxopentanoate + NADH + H+
2-hydroxypentanoate + NAD+
i.e. 2-oxovalerate
-
-
?
3-methyl-2-oxobutanoate + NADH + H+
2-hydroxy-3-methylbutanoate + NAD+
-
i.e.2-oxoisovalerate
-
-
?
3-methyl-2-oxobutanoate + NADH + H+
2-hydroxy-3-methylbutanoate + NAD+
-
i.e.2-oxoisovalerate
-
-
?
3-methyl-2-oxobutanoate + NADH + H+
3-methyl-2-hydroxybutanoate + NAD+
-
Vmax/Km is 51% compared to 4-methyl-2-oxopentanoate
-
-
?
3-methyl-2-oxobutanoate + NADH + H+
3-methyl-2-hydroxybutanoate + NAD+
-
Vmax/KM is 56% compared to 4-methyl-2-oxopentanoate
-
-
?
3-methyl-2-oxobutanoate + NADH + H+
3-methyl-2-hydroxybutanoate + NAD+
-
Vmax/Km is 85.7% compared to 4-methyl-2-oxopentanoate
-
-
?
3-methyl-2-oxopentanoate + NADH + H+
2-hydroxy-3-methylpentanoate + NAD+
-
i.e. 2-oxomethylvalerate
-
-
?
3-methyl-2-oxopentanoate + NADH + H+
2-hydroxy-3-methylpentanoate + NAD+
-
i.e. 2-oxomethylvalerate
-
-
?
4-methyl-2-oxopentanoate + NADH + H+
(R)-2-hydroxy-4-methylpentanoate + NAD+
-
i.e. 2-oxoisocaproate
i.e. (R)-2-hydroxyisocaproate
-
r
4-methyl-2-oxopentanoate + NADH + H+
(R)-2-hydroxy-4-methylpentanoate + NAD+
i.e. 2-oxoisocaproate
i.e. (R)-2-hydroxyisocaproate
-
r
4-methyl-2-oxopentanoate + NADH + H+
(R)-2-hydroxy-4-methylpentanoate + NAD+
i.e. 2-oxoisocaproate
i.e. (R)-2-hydroxyisocaproate
-
?
4-methyl-2-oxopentanoate + NADH + H+
(R)-2-hydroxy-4-methylpentanoate + NAD+
-
i.e. 2-oxoisocaproate. The apparent Vmax/Km ratio for the reverse reaction is about 0.5% of that for the forward reaction
i.e. (R)-2-hydroxyisocaproate
-
r
4-methyl-2-oxopentanoate + NADH + H+
(R)-2-hydroxy-4-methylpentanoate + NAD+
-
i.e. 2-oxoisocaproate. The apparent Vmax/Km ratio for the reverse reaction is about 0.5% of that for the forward reaction
i.e. (R)-2-hydroxyisocaproate
-
r
benzoylformate + NADH + H+
?
-
-
-
-
?
benzoylformate + NADH + H+
?
-
-
-
-
?
D-2-hydroxybutyrate + NAD+
2-oxobutyrate + NADH + H+
-
-
-
-
r
D-2-hydroxybutyrate + NAD+
2-oxobutyrate + NADH + H+
-
-
-
-
r
D-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
D-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
D-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
D-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
D-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
D-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
D-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
D-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
D-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
D-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
D-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
D-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
oxaloacetate + NADH + H+
D-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
D-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
D-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
D-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
D-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
D-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
D-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
D-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
D-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
D-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
D-malate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
D-malate + NAD+
-
-
-
r
phenylglyoxylate + NADH + H+
hydroxy(phenyl)acetic acid + NAD+
-
Vmax/Km is 16.7% compared to 4-methyl-2-oxopentanoate
-
-
?
phenylglyoxylate + NADH + H+
hydroxy(phenyl)acetic acid + NAD+
-
Vmax/Km is 44% compared to 4-methyl-2-oxopentanoate
-
-
?
phenylglyoxylate + NADH + H+
hydroxy(phenyl)acetic acid + NAD+
-
Vmax/KM is 54% compared to 4-methyl-2-oxopentanoate
-
-
?
phenylpyruvate + NADH + H+
? + NAD+
-
-
-
-
r
phenylpyruvate + NADH + H+
? + NAD+
-
-
-
-
r
phenylpyruvate + NADH + H+
phenyl-D-lactate + NAD+
-
-
-
r
phenylpyruvate + NADH + H+
phenyl-D-lactate + NAD+
-
-
-
r
phenylpyruvate + NADH + H+
phenyllactate + NAD+
-
-
-
-
?
phenylpyruvate + NADH + H+
phenyllactate + NAD+
-
-
-
r
phenylpyruvate + NADH + H+
phenyllactate + NAD+
-
-
-
?
phenylpyruvate + NADH + H+
phenyllactate + NAD+
-
-
-
-
?
pyruvate + NADH + H+
D-lactate + NAD+
-
100% activity
-
-
r
pyruvate + NADH + H+
D-lactate + NAD+
-
100% activity
-
-
r
pyruvate + NADH + H+
lactate + NAD+
-
-
-
-
?
pyruvate + NADH + H+
lactate + NAD+
-
-
-
-
?
additional information
?
-
-
both enzymes (D-mandelate dehydrogenase D-ManDH1 and D-mandelate dehydrogenase D-ManDH2) exhibit no or very little activity toward small 2-ketoacid substrates, such as pyruvate, hydroxypyruvate, and 2-ketobutyrate, and much higher activity toward substrates with larger aliphatic or aromatic side chains. The two enzymes exhibit higher activity (smaller Km and larger Vmax) for 2-ketoacid substrates branched at the C3 or C4 position than for unbranched substrates; i.e., 2-ketoisovalerate and 2-ketoisocaproate are more favorable than 2-ketovalerate and 2-ketocaproate, respectively. Among aromatic substrates, the two enzymes preferr benzoylformate to phenylpyruvate by 9- and 17-fold, respectively
-
-
?
additional information
?
-
-
both enzymes (D-mandelate dehydrogenase D-ManDH1 and D-mandelate dehydrogenase D-ManDH2) exhibit no or very little activity toward small 2-oxoacid substrates, such as pyruvate, hydroxypyruvate, and 2-oxobutyrate, and much higher activity toward substrates with larger aliphatic or aromatic side chains. The two enzymes exhibit higher activity (smaller Km and larger Vmax) for 2-ketoacid substrates branched at the C3 or C4 position than for unbranched substrates; i.e., 2-oxoisovalerate and 2-oxoisocaproate are more favorable than 2-oxovalerate and 2-oxocaproate, respectively. Among aromatic substrates, the two enzymes prefer benzoylformate to phenylpyruvate by 9- and 17-fold, respectively
-
-
?
additional information
?
-
-
the recombinant enzyme exhibits high catalytic activity toward various 2-oxoacid substrates with bulky hydrophobic side chains, particularly C3-branched substrates such as benzoylformate and 2-oxoisovalerate
-
-
?
additional information
?
-
-
no significant activity with L-lactate, L-2-hydroxybutyrate, L-hydroxyisocaproate, phenylpyruvate, 2-oxomethyl-n-valerate, and 2-oxoisovalerate
-
-
?
additional information
?
-
-
no significant activity with L-lactate, L-2-hydroxybutyrate, L-hydroxyisocaproate, phenylpyruvate, 2-oxomethyl-n-valerate, and 2-oxoisovalerate
-
-
?
additional information
?
-
very low specificity regarding size and chemical constitution of the accepted D-2-hydroxycarboxylates
-
-
?
additional information
?
-
-
the enzyme accepts D-2-hydroxyacids but not L-2-hydroxyacids and shows no NADP-dependent 2-ketopantoate reductase activity. No reactions are observed with 10 mM L-2-hydroxyisocaproate and 1 mM NAD+, 10 mM pyruvate and 0.3 mM NADH, 10 mM 2-oxooisocaproate and 0.3 mM NADPH, and 10 mM 2-oxopantoate and 0.3 mM NADH or NADPH
-
-
?
additional information
?
-
-
the enzyme accepts D-2-hydroxyacids but not L-2-hydroxyacids and shows no NADP-dependent 2-ketopantoate reductase activity. No reactions are observed with 10 mM L-2-hydroxyisocaproate and 1 mM NAD+, 10 mM pyruvate and 0.3 mM NADH, 10 mM 2-oxooisocaproate and 0.3 mM NADPH, and 10 mM 2-oxopantoate and 0.3 mM NADH or NADPH
-
-
?
additional information
?
-
the recombinant the proteins derived from the Escherichia coli cells harboring plasmids pET28a/ldh0076, pET28a/ldh1837, and pET28a/ldh2043 do not show any enzymatic activity toward pyruvate, D-lactate, or L-lactate, indicating that they are not LDHs that catalyze the interconversion of pyruvate and lactate. All three proteins exhibit NADH-oxidation activity toward oxaloacetate and 2-oxobutyrate, producing malate and 2-hydroxybutyrate, respectively. The protein encoded by LEUM_0076 shows clear NAD+-reduction activity toward L-malate, producing oxaloacetate, whereas the other two proteins encoded by LEUM_1837 and LEUM_2043 display NAD+-reduction activity toward D-malate, producing oxaloacetate
-
-
-
additional information
?
-
the recombinant the proteins derived from the Escherichia coli cells harboring plasmids pET28a/ldh0076, pET28a/ldh1837, and pET28a/ldh2043 do not show any enzymatic activity toward pyruvate, D-lactate, or L-lactate, indicating that they are not LDHs that catalyze the interconversion of pyruvate and lactate. All three proteins exhibit NADH-oxidation activity toward oxaloacetate and 2-oxobutyrate, producing malate and 2-hydroxybutyrate, respectively. The protein encoded by LEUM_0076 shows clear NAD+-reduction activity toward L-malate, producing oxaloacetate, whereas the other two proteins encoded by LEUM_1837 and LEUM_2043 display NAD+-reduction activity toward D-malate, producing oxaloacetate
-
-
-
additional information
?
-
the recombinant the proteins derived from the Escherichia coli cells harboring plasmids pET28a/ldh0076, pET28a/ldh1837, and pET28a/ldh2043 do not show any enzymatic activity toward pyruvate, D-lactate, or L-lactate, indicating that they are not LDHs that catalyze the interconversion of pyruvate and lactate. All three proteins exhibit NADH-oxidation activity toward oxaloacetate and 2-oxobutyrate, producing malate and 2-hydroxybutyrate, respectively. The protein encoded by LEUM_0076 shows clear NAD+-reduction activity toward L-malate, producing oxaloacetate, whereas the other two proteins encoded by LEUM_1837 and LEUM_2043 display NAD+-reduction activity toward D-malate, producing oxaloacetate
-
-
-
additional information
?
-
the recombinant the proteins derived from the Escherichia coli cells harboring plasmids pET28a/ldh0076, pET28a/ldh1837, and pET28a/ldh2043 do not show any enzymatic activity toward pyruvate, D-lactate, or L-lactate, indicating that they are not LDHs that catalyze the interconversion of pyruvate and lactate. All three proteins exhibit NADH-oxidation activity toward oxaloacetate and 2-oxobutyrate, producing malate and 2-hydroxybutyrate, respectively. The protein encoded by LEUM_0076 shows clear NAD+-reduction activity toward L-malate, producing oxaloacetate, whereas the other two proteins encoded by LEUM_1837 and LEUM_2043 display NAD+-reduction activity toward D-malate, producing oxaloacetate
-
-
-
additional information
?
-
the recombinant the proteins derived from the Escherichia coli cells harboring plasmids pET28a/ldh0076, pET28a/ldh1837, and pET28a/ldh2043 do not show any enzymatic activity toward pyruvate, D-lactate, or L-lactate, indicating that they are not LDHs that catalyze the interconversion of pyruvate and lactate. All three proteins exhibit NADH-oxidation activity toward oxaloacetate and 2-oxobutyrate, producing malate and 2-hydroxybutyrate, respectively. The protein encoded by LEUM_0076 shows clear NAD+-reduction activity toward L-malate, producing oxaloacetate, whereas the other two proteins encoded by LEUM_1837 and LEUM_2043 display NAD+-reduction activity toward D-malate, producing oxaloacetate
-
-
-
additional information
?
-
the recombinant the proteins derived from the Escherichia coli cells harboring plasmids pET28a/ldh0076, pET28a/ldh1837, and pET28a/ldh2043 do not show any enzymatic activity toward pyruvate, D-lactate, or L-lactate, indicating that they are not LDHs that catalyze the interconversion of pyruvate and lactate. All three proteins exhibit NADH-oxidation activity toward oxaloacetate and 2-oxobutyrate, producing malate and 2-hydroxybutyrate, respectively. The protein encoded by LEUM_0076 shows clear NAD+-reduction activity toward L-malate, producing oxaloacetate, whereas the other two proteins encoded by LEUM_1837 and LEUM_2043 display NAD+-reduction activity toward D-malate, producing oxaloacetate
-
-
-
additional information
?
-
the recombinant the proteins derived from the Escherichia coli cells harboring plasmids pET28a/ldh0076, pET28a/ldh1837, and pET28a/ldh2043 do not show any enzymatic activity toward pyruvate, D-lactate, or L-lactate, indicating that they are not LDHs that catalyze the interconversion of pyruvate and lactate. All three proteins exhibit NADH-oxidation activity toward oxaloacetate and 2-oxobutyrate, producing malate and 2-hydroxybutyrate, respectively. The protein encoded by LEUM_0076 shows clear NAD+-reduction activity toward L-malate, producing oxaloacetate, whereas the other two proteins encoded by LEUM_1837 and LEUM_2043 display NAD+-reduction activity toward D-malate, producing oxaloacetate
-
-
-
additional information
?
-
the recombinant the proteins derived from the Escherichia coli cells harboring plasmids pET28a/ldh0076, pET28a/ldh1837, and pET28a/ldh2043 do not show any enzymatic activity toward pyruvate, D-lactate, or L-lactate, indicating that they are not LDHs that catalyze the interconversion of pyruvate and lactate. All three proteins exhibit NADH-oxidation activity toward oxaloacetate and 2-oxobutyrate, producing malate and 2-hydroxybutyrate, respectively. The protein encoded by LEUM_0076 shows clear NAD+-reduction activity toward L-malate, producing oxaloacetate, whereas the other two proteins encoded by LEUM_1837 and LEUM_2043 display NAD+-reduction activity toward D-malate, producing oxaloacetate
-
-
-
additional information
?
-
the recombinant the proteins derived from the Escherichia coli cells harboring plasmids pET28a/ldh0076, pET28a/ldh1837, and pET28a/ldh2043 do not show any enzymatic activity toward pyruvate, D-lactate, or L-lactate, indicating that they are not LDHs that catalyze the interconversion of pyruvate and lactate. All three proteins exhibit NADH-oxidation activity toward oxaloacetate and 2-oxobutyrate, producing malate and 2-hydroxybutyrate, respectively. The protein encoded by LEUM_0076 shows clear NAD+-reduction activity toward L-malate, producing oxaloacetate, whereas the other two proteins encoded by LEUM_1837 and LEUM_2043 display NAD+-reduction activity toward D-malate, producing oxaloacetate
-
-
-
additional information
?
-
the recombinant the proteins derived from the Escherichia coli cells harboring plasmids pET28a/ldh0076, pET28a/ldh1837, and pET28a/ldh2043 do not show any enzymatic activity toward pyruvate, D-lactate, or L-lactate, indicating that they are not LDHs that catalyze the interconversion of pyruvate and lactate. All three proteins exhibit NADH-oxidation activity toward oxaloacetate and 2-oxobutyrate, producing malate and 2-hydroxybutyrate, respectively. The protein encoded by LEUM_0076 shows clear NAD+-reduction activity toward L-malate, producing oxaloacetate, whereas the other two proteins encoded by LEUM_1837 and LEUM_2043 display NAD+-reduction activity toward D-malate, producing oxaloacetate
-
-
-
additional information
?
-
the recombinant the proteins derived from the Escherichia coli cells harboring plasmids pET28a/ldh0076, pET28a/ldh1837, and pET28a/ldh2043 do not show any enzymatic activity toward pyruvate, D-lactate, or L-lactate, indicating that they are not LDHs that catalyze the interconversion of pyruvate and lactate. All three proteins exhibit NADH-oxidation activity toward oxaloacetate and 2-oxobutyrate, producing malate and 2-hydroxybutyrate, respectively. The protein encoded by LEUM_0076 shows clear NAD+-reduction activity toward L-malate, producing oxaloacetate, whereas the other two proteins encoded by LEUM_1837 and LEUM_2043 display NAD+-reduction activity toward D-malate, producing oxaloacetate
-
-
-
additional information
?
-
the recombinant the proteins derived from the Escherichia coli cells harboring plasmids pET28a/ldh0076, pET28a/ldh1837, and pET28a/ldh2043 do not show any enzymatic activity toward pyruvate, D-lactate, or L-lactate, indicating that they are not LDHs that catalyze the interconversion of pyruvate and lactate. All three proteins exhibit NADH-oxidation activity toward oxaloacetate and 2-oxobutyrate, producing malate and 2-hydroxybutyrate, respectively. The protein encoded by LEUM_0076 shows clear NAD+-reduction activity toward L-malate, producing oxaloacetate, whereas the other two proteins encoded by LEUM_1837 and LEUM_2043 display NAD+-reduction activity toward D-malate, producing oxaloacetate
-
-
-
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2.3
(R)-2-hydroxy-4-methylpentanoate
-
pH 7.0, temperature not specified in the publication
1.26
2-formylbutanethioate
-
pH 7.0, 37°C
2.7
2-hydroxyhexanoate
-
pH 7.0, temperature not specified in the publication
1.6
2-Hydroxyoctanoate
-
pH 7.0, temperature not specified in the publication
3.3
2-hydroxypentanoate
-
pH 7.0, temperature not specified in the publication
3.4 - 5.7
2-oxo-3-phenylpropanoate
0.02 - 1.5
2-Oxohexanoate
0.3 - 71
2-oxoisocaproate
0.29 - 46
2-oxoisovalerate
0.21
2-oxomethylvalerate
-
at pH 7.0 and 37°C
0.12
2-oxooctanoate
-
pH 7.0, temperature not specified in the publication
0.057 - 0.4
2-oxopentanoate
0.6
3-(4-hydroxyphenyl)-2-oxopropanoate
-
pH 7.0, temperature not specified in the publication
2.9
3-hydroxypyruvate
-
in 100 mM Tris-HC1 buffer, pH 8.0, at 30°C
0.15 - 0.29
3-methyl-2-oxobutanoate
0.21
3-methyl-2-oxopentanoate
-
pH 7.0, 37°C
0.022 - 0.4
4-methyl-2-oxopentanoate
1.26
4-methylthio-2-oxobutanoate
-
at pH 7.0 and 37°C
0.14
D-lactate
-
in 0.1 M acetate buffer, pH 5.0, 4 M NaCl, at 52°C
3
D-mandelate
-
at pH 7.0 and 37°C
3
DL-2-hydroxyisocaproate
-
at pH 7.0 and 37°C
0.25 - 0.26
phenylglyoxylate
0.031 - 20
phenylpyruvate
additional information
additional information
Michaelis-Menten kinetics, recombinant enzyme
-
0.76
(R)-mandelate
-
pH 7.5, 30°C, D-mandelate dehydrogenase D-ManDH2
0.9
(R)-mandelate
-
pH 7.5, 30°C
3.4
2-oxo-3-phenylpropanoate
-
pH 7.5, 30°C, D-mandelate dehydrogenase D-ManDH2
5.7
2-oxo-3-phenylpropanoate
-
pH 7.5, 30°C
4
2-oxobutanoate
-
pH 7.5, 30°C, D-mandelate dehydrogenase D-ManDH2
9.5
2-oxobutanoate
-
pH 7.5, 30°C
0.36
2-oxobutyrate
-
in 0.1 M glycine-NaOH buffer, pH 9.0, 4 M NaCl, at 52°C
28
2-oxobutyrate
-
in 100 mM Tris-HC1 buffer, pH 8.0, at 30°C
2.4
2-oxocaproate
-
at pH 7.0 and 37°C
40
2-oxocaproate
-
in 100 mM Tris-HC1 buffer, pH 8.0, at 30°C
0.02
2-Oxohexanoate
pH 7.5, 25°C
0.11
2-Oxohexanoate
pH 7.0, 25°C
0.13
2-Oxohexanoate
-
pH 7.0, temperature not specified in the publication
0.6
2-Oxohexanoate
-
pH 7.5, 30°C, D-mandelate dehydrogenase D-ManDH2
1.5
2-Oxohexanoate
-
pH 7.5, 30°C
0.3
2-oxoisocaproate
-
at pH 7.0 and 37°C
2.3
2-oxoisocaproate
-
in 0.1 M glycine-NaOH buffer, pH 9.0, 4 M NaCl, at 52°C
71
2-oxoisocaproate
-
in 100 mM Tris-HC1 buffer, pH 8.0, at 30°C
0.29
2-oxoisovalerate
-
at pH 7.0 and 37°C
46
2-oxoisovalerate
-
in 100 mM Tris-HC1 buffer, pH 8.0, at 30°C
0.057
2-oxopentanoate
pH 7.5, 25°C
0.11
2-oxopentanoate
pH 7.0, 25°C
0.12
2-oxopentanoate
-
pH 7.0, temperature not specified in the publication
0.3
2-oxopentanoate
-
pH 7.5, 30°C
0.4
2-oxopentanoate
-
pH 7.5, 30°C, D-mandelate dehydrogenase D-ManDH2
0.53
2-oxovalerate
-
at pH 7.0 and 37°C
62
2-oxovalerate
-
in 100 mM Tris-HC1 buffer, pH 8.0, at 30°C
0.15
3-methyl-2-oxobutanoate
-
pH 7.5, 30°C, D-mandelate dehydrogenase D-ManDH2
0.18
3-methyl-2-oxobutanoate
-
pH 7.5, 30°C
0.29
3-methyl-2-oxobutanoate
-
pH 7.0, 37°C
0.022
4-methyl-2-oxopentanoate
pH 7.5, 25°C
0.06
4-methyl-2-oxopentanoate
pH 7.0, 25°C
0.11
4-methyl-2-oxopentanoate
-
pH 7.5, 30°C, D-mandelate dehydrogenase D-ManDH2
0.13
4-methyl-2-oxopentanoate
-
pH 7.5, 30°C
0.3
4-methyl-2-oxopentanoate
-
pH 7.0, 37°C
0.4
4-methyl-2-oxopentanoate
-
pH 7.0, temperature not specified in the publication
1.5
benzoylformate
-
pH 7.0, 37°C
1.5
benzoylformate
-
at pH 7.0 and 37°C
0.01
NADH
pH 7.0, 25°C
0.05
NADH
-
with 2-oxobutyrate as cosubstrate, in 0.1 M glycine-NaOH buffer, pH 9.0, 4 M NaCl, at 52°C
0.086
NADH
-
with 2-oxoisocaproate as cosubstrate, in 0.1 M glycine-NaOH buffer, pH 9.0, 4 M NaCl, at 52°C
0.096
NADH
-
with pyruvate as cosubstrate, in 0.1 M glycine-NaOH buffer, pH 9.0, 4 M NaCl, at 52°C
0.14
NADH
-
at pH 7.0 and 37°C
0.25
phenylglyoxylate
-
pH 7.5, 30°C
0.26
phenylglyoxylate
-
pH 7.5, 30°C, D-mandelate dehydrogenase D-ManDH2
0.031
phenylpyruvate
pH 7.5, 25°C
0.0591
phenylpyruvate
recombinant His-tagged enzyme, pH and temperature not specified in the publication
0.15
phenylpyruvate
pH 7.0, 25°C
0.2
phenylpyruvate
-
pH 7.0, temperature not specified in the publication
5.4
phenylpyruvate
-
pH 7.0, 37°C
5.4
phenylpyruvate
-
at pH 7.0 and 37°C
20
phenylpyruvate
-
in 100 mM Tris-HC1 buffer, pH 8.0, at 30°C
0.56
pyruvate
-
in 0.1 M glycine-NaOH buffer, pH 9.0, 4 M NaCl, at 52°C
1.2
pyruvate
-
in 100 mM Tris-HC1 buffer, pH 8.0, at 30°C
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evolution
the enzyme belongs to the the NAD-dependent dehydrogenase family. Comparison with closely related members of the NAD-dependent dehydrogenase family reveals that whilst the D2-HDH core fold is structurally conserved, the substrate-binding site has a number of non-canonical features that may influence substrate selection and thus dictate the physiological function of the enzyme. The protein, 2-hydroxyisocaproate dehydrogenase (HO-HxoDH), is virtually identical to the D2-HDH, with only three amino-acid differences between the two proteins, all at sites not known to be biologically relevant
evolution
-
the enzyme belongs to the the NAD-dependent dehydrogenase family. Comparison with closely related members of the NAD-dependent dehydrogenase family reveals that whilst the D2-HDH core fold is structurally conserved, the substrate-binding site has a number of non-canonical features that may influence substrate selection and thus dictate the physiological function of the enzyme. The protein, 2-hydroxyisocaproate dehydrogenase (HO-HxoDH), is virtually identical to the D2-HDH, with only three amino-acid differences between the two proteins, all at sites not known to be biologically relevant
-
malfunction
-
the inactivation of panE does not affect the total percentage of leucine degraded but totally prevents KIC reduction to 2-hydroxyisocaproate and slightly decreases the production of isovalerate
malfunction
-
the inactivation of panE does not affect the total percentage of leucine degraded but totally prevented 4-methyl-2-oxopentanoate reduction to 2-hydroxyisocaproate and slightly decreased the production of isovalerate
malfunction
-
the inactivation of panE does not affect the total percentage of leucine degraded but totally prevents KIC reduction to 2-hydroxyisocaproate and slightly decreases the production of isovalerate
-
malfunction
-
the inactivation of panE does not affect the total percentage of leucine degraded but totally prevented 4-methyl-2-oxopentanoate reduction to 2-hydroxyisocaproate and slightly decreased the production of isovalerate
-
metabolism
-
its probable physiological role is to regenerate the NAD+ necessary to catabolize branched-chain amino acids, leading to the production of ATP and aroma compounds responsible for the reduction of the 2-keto acids derived from leucine, isoleucine, and valine
metabolism
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
metabolism
-
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
metabolism
-
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
metabolism
-
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
metabolism
-
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
metabolism
-
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
metabolism
-
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
metabolism
-
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
metabolism
-
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
metabolism
-
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
metabolism
-
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
metabolism
-
its probable physiological role is to regenerate the NAD+ necessary to catabolize branched-chain amino acids, leading to the production of ATP and aroma compounds responsible for the reduction of the 2-keto acids derived from leucine, isoleucine, and valine
-
metabolism
-
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
physiological function
the substrate-binding site has a number of non-canonical features that may influence substrate selection and thus dictate the physiological function of the enzyme
physiological function
-
the substrate-binding site has a number of non-canonical features that may influence substrate selection and thus dictate the physiological function of the enzyme
-
additional information
enzyme three-dimensional structure analysis, active site and cofactor binding site structures, overview
additional information
-
enzyme three-dimensional structure analysis, active site and cofactor binding site structures, overview
-
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Huang, T.; Yang, W.; Pereira, A.C.; Craigen, W.J.; Shih, V.E.
Cloning and characterization of a putative human D-2-hydroxyacid dehydrogenase in chromosome 9q
Biochem. Biophys. Res. Commun.
268
298-301
2000
Homo sapiens
brenda
Bonete, M.J.; Ferrer, J.; Pire, C.; Penades, M.; Ruiz, J.L.
2-Hydroxyacid dehydrogenase from Haloferax mediteranii, a D-isomer-specific member of the 2-dehydrogenase family
Biochimie
82
1143-1150
2000
Haloferax mediterranei, Haloferax mediterranei R4, ATCC 33500
brenda
Wada, Y.; Iwai, S.; Tamura, Y.; Ando, T.; Shinoda, T.; Arai, K.; Taguchi, H.
A new family of D-2-hydroxyacid dehydrogenases that comprises D-mandelate dehydrogenases and 2-ketopantoate reductases
Biosci. Biotechnol. Biochem.
72
1087-1094
2008
Enterococcus faecalis
brenda
Domenech, J.; Baker, P.; Sedelnikova, S.; Rodgers, H.; Rice, D.; Ferrer, J.
Crystallization and preliminary X-ray analysis of D-2-hydroxyacid dehydrogenase from Haloferax mediterranei
Acta Crystallogr. Sect. F
65
415-418
2009
Haloferax mediterranei, Haloferax mediterranei ATCC 335500
brenda
Chambellon, E.; Rijnen, L.; Lorquet, F.; Gitton, C.; Van Hylckama Vlieg, J.; Wouters, J.; Yvon, M.
The D-2-hydroxyacid dehydrogenase incorrectly annotated PanE is the sole reduction system for branched-chain 2-keto acids in Lactococcus lactis
J. Bacteriol.
191
873-881
2009
Lactococcus lactis, Lactococcus cremoris, Lactococcus lactis IL1403, Lactococcus cremoris TIL46
brenda
Taguchi, H.; Ohta, T.
D-lactate dehydrogenase is a member of the D-isomer-specific 2-hydroxyacid dehydrogenase family: Cloning, sequencing, and expression in Escherichia coli of the D-lactate dehydrogenase gene of Lactobacillus plantarum
J. Biol. Chem.
266
12588-12594
1991
Lactiplantibacillus plantarum, Lactiplantibacillus plantarum ATCC 8041
brenda
Niefind, K.; Hecht, H.J.; Schomburg, D.
Crystallization and preliminary characterization of crystals of D-2-hydroxyisocaproate dehydrogenase from Lactobacillus casei
J. Mol. Biol.
240
400-402
1994
Lacticaseibacillus paracasei (P17584)
brenda
Dengler, U.; Niefind, K.; Kiess, M.; Schomburg, D.
Crystal structure of a ternary complex of D-2-hydroxyisocaproate dehydrogenase from Lactobacillus casei, NAD+ and 2-oxoisocaproate at 1.9 A resolution
J. Mol. Biol.
267
640-660
1997
Lacticaseibacillus paracasei (P17584)
brenda
Tamura, Y.; Ohkubo, A.; Iwai, S.; Wada, Y.; Shinoda, T.; Arai, K.; Mineki, S.; Iida, M.; Taguchi, H.
Two forms of NAD-dependent D-mandelate dehydrogenase in Enterococcus faecalis IAM 10071
Appl. Environ. Microbiol.
68
947-951
2002
Enterococcus faecalis
brenda
Miyanaga, A.; Fujisawa, S.; Furukawa, N.; Arai, K.; Nakajima, M.; Taguchi, H.
The crystal structure of D-mandelate dehydrogenase reveals its distinct substrate and coenzyme recognition mechanisms from those of 2-ketopantoate reductase
Biochem. Biophys. Res. Commun.
439
109-114
2013
Enterococcus faecium (E3USM3)
brenda
Hummel, W.; Schtte, H.; Kula, M.-R.
D-2-Hydroxyisocaproate dehydrogenase from Lactobacillus casei
Appl. Microbiol. Biotechnol.
21
7-15
1985
Lacticaseibacillus paracasei (P17584)
-
brenda
Kallwass, H.K.W.
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