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Literature summary for 1.1.1.202 extracted from

  • Qi, X.; Yun, J.; Qi, Y.; Zhang, H.; Wang, F.; Guo, Q.; Cao, Z.
    Expression and characterization of a novel 1,3-propanediol dehydrogenase from Lactobacillus brevis (2016), Appl. Biochem. Biotechnol., 179, 959-972.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene dhaT, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain JM109 Levilactobacillus brevis

Inhibitors

Inhibitors Comment Organism Structure
Ca2+ slight inhibition at 5 mM Levilactobacillus brevis
EDTA 91% inhibition at 5 mM Levilactobacillus brevis
PMSF 85% inhibition at 5 mM Levilactobacillus brevis
Zn2+ slight inhibition at 5 mM Levilactobacillus brevis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0116
-
NADH pH 7.5, 37°C Levilactobacillus brevis
0.0904
-
NAD+ pH 9.5, 25°C Levilactobacillus brevis
1.25
-
3-hydroxypropanal pH 7.5, 37°C Levilactobacillus brevis
2.26
-
Propane-1,3-diol pH 9.5, 25°C Levilactobacillus brevis

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ activates to 150% at 5 mM, the enzyme contains two Fe2+-binding motifs, amino acid residues Asp189, Gln193, His258, and His272, are involved in the Fe2+ binding Levilactobacillus brevis
Mn2+ activates to 280% at 5 mM Levilactobacillus brevis
additional information addition of Co2+, Ni2+, or Mg2+ do not significantly affect PDOR activity at 5 mM Levilactobacillus brevis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
42000
-
-
Levilactobacillus brevis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3-hydroxypropanal + NADH + H+ Levilactobacillus brevis reduction of the aldehyde is the preferred reaction propane-1,3-diol + NAD+
-
r
3-hydroxypropanal + NADH + H+ Levilactobacillus brevis 6239 reduction of the aldehyde is the preferred reaction propane-1,3-diol + NAD+
-
r
propane-1,3-diol + NAD+ Levilactobacillus brevis
-
3-hydroxypropanal + NADH + H+
-
r

Organism

Organism UniProt Comment Textmining
Levilactobacillus brevis A0A0C1Q6R1
-
-
Levilactobacillus brevis 6239 A0A0C1Q6R1
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme 7.1-7.3fold from Escherichia coli strain JM109 by nickel affinity chromatography and gel filtration Levilactobacillus brevis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
32.6
-
purified recombinant His-tagged enzyme, substrate propane-1,3-diol, pH 9.5, 25°C Levilactobacillus brevis
52.7
-
purified recombinant His-tagged enzyme, substrate 3-hydroxypropanal, pH 7.5, 37°C Levilactobacillus brevis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1,4-butanediol + NAD+
-
Levilactobacillus brevis 4-hydroxybutanal + NADH + H+
-
r
1-butanol + NAD+
-
Levilactobacillus brevis 1-butanal + NADH + H+
-
r
1-propanol + NAD+
-
Levilactobacillus brevis 1-propanal + NADH + H+
-
r
3-hydroxypropanal + NADH + H+ reduction of the aldehyde is the preferred reaction Levilactobacillus brevis propane-1,3-diol + NAD+
-
r
3-hydroxypropanal + NADH + H+ reduction of the aldehyde is the preferred reaction, 3-hydroxypropanal is the preferred substrate Levilactobacillus brevis propane-1,3-diol + NAD+
-
r
3-hydroxypropanal + NADH + H+ reduction of the aldehyde is the preferred reaction Levilactobacillus brevis 6239 propane-1,3-diol + NAD+
-
r
3-hydroxypropanal + NADH + H+ reduction of the aldehyde is the preferred reaction, 3-hydroxypropanal is the preferred substrate Levilactobacillus brevis 6239 propane-1,3-diol + NAD+
-
r
acetone + NADH + H+
-
Levilactobacillus brevis ? + NAD+
-
r
dihydroxyacetone + NADH + H+
-
Levilactobacillus brevis ? + NAD+
-
r
ethanol + NAD+
-
Levilactobacillus brevis acetaldehyde + NADH + H+
-
r
ethanol + NAD+
-
Levilactobacillus brevis 6239 acetaldehyde + NADH + H+
-
r
glyceraldehyde + NADH + H+
-
Levilactobacillus brevis ? + NAD+
-
r
glycerol + NAD+
-
Levilactobacillus brevis dihydroxyacetone + NADH + H+
-
r
glycerol + NAD+
-
Levilactobacillus brevis 6239 dihydroxyacetone + NADH + H+
-
r
hydroxyacetone + NADH + H+
-
Levilactobacillus brevis ? + NAD+
-
r
additional information the enzyme shows a broad substrate specificity, PDOR can help reduce a broad range of aldehydes and ketones including 3-HPA, propionaldehyde, glyceraldehyde, acetone, hydroxyacetone, and dihydroxyacetone. No activity with acrolein. PDOR can also help oxidize many kinds of alcohols to generate the corresponding aldehydes, and this enzyme is most active with diols containing two primary hydroxy groups separated by one or two carbon atoms. Structure modeling, overview Levilactobacillus brevis ?
-
?
additional information the enzyme shows a broad substrate specificity, PDOR can help reduce a broad range of aldehydes and ketones including 3-HPA, propionaldehyde, glyceraldehyde, acetone, hydroxyacetone, and dihydroxyacetone. No activity with acrolein. PDOR can also help oxidize many kinds of alcohols to generate the corresponding aldehydes, and this enzyme is most active with diols containing two primary hydroxy groups separated by one or two carbon atoms. Structure modeling, overview Levilactobacillus brevis 6239 ?
-
?
propane-1,2-diol + NAD+
-
Levilactobacillus brevis 2-hydroxypropanal + NADH + H+
-
r
propane-1,3-diol + NAD+
-
Levilactobacillus brevis 3-hydroxypropanal + NADH + H+
-
r

Subunits

Subunits Comment Organism
? x * 42500, recombinant His-tagged enzyme, SDS-PAGE, x * 41993, sequence calculation Levilactobacillus brevis

Synonyms

Synonyms Comment Organism
DhaT
-
Levilactobacillus brevis
PDOR
-
Levilactobacillus brevis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
alcohol oxidation Levilactobacillus brevis
37
-
aldehyde reduction Levilactobacillus brevis

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
15 40 activity range, aldehyde reduction, profile overview Levilactobacillus brevis
25 45 activity range, alcohol oxidation, profile overview Levilactobacillus brevis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
15 45 purified recombinant His-tagged enzyme, 50% activity remaining after 3 h and 30% after 5 h at 30-37°C, inactivation after 2 h at 45°C Levilactobacillus brevis
37
-
60% of enzyme relative activity remain after a 2h incubation at 37°C Levilactobacillus brevis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
aldehyde reduction Levilactobacillus brevis
9.5
-
alcohol oxidation Levilactobacillus brevis

pH Range

pH Minimum pH Maximum Comment Organism
6 10 activity range, aldehyde reduction, profile overview Levilactobacillus brevis
8 10.5 activity range, alcohol oxidation, profile overview Levilactobacillus brevis

pH Stability

pH Stability pH Stability Maximum Comment Organism
additional information
-
PDOR is more stable in acid buffer than in alkaline condition Levilactobacillus brevis
6 10 purified recombinant His-tagged enzyme, 50% activityy remaining after 1 h and inactivation aafter 5 h at pH 6.0, 50% activity remaining after 3 h and 30% after 5 h at pH 7.5, inactivation after 1 h at pH 10.0 Levilactobacillus brevis

Cofactor

Cofactor Comment Organism Structure
NAD+ the enzyme contains a cofactor motif, the conserved sequence G-GG-S-X-X-D. The binding site for cofactor NAD(H) is located in the deep hydrophilic pocket between the PDOR two domains Levilactobacillus brevis
NADH
-
Levilactobacillus brevis

General Information

General Information Comment Organism
evolution the enzyme belongs to the type III alcohol dehydrogenases Levilactobacillus brevis
additional information the active site of PDOR is composed of the following amino acid residues, Asp32, Gly92, Gly93, Ser94, Thr134, Thr135, Thr138, Val146, Lys155, Leu177, Asp189, Leu182, Gln193, His258, and His272, which include the binding sites of Fe2+ and the cofactor NAD(H) Levilactobacillus brevis