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Literature summary 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)

EC Number Cloned (Comment) Organism
1.1.1.202 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

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.202 0.0116
-
 NADH pH 7.5, 37°C Levilactobacillus brevis
1.1.1.202 0.0904
-
 NAD+ pH 9.5, 25°C Levilactobacillus brevis
1.1.1.202 1.25
-
 3-hydroxypropanal pH 7.5, 37°C Levilactobacillus brevis
1.1.1.202 2.26
-
 Propane-1,3-diol pH 9.5, 25°C Levilactobacillus brevis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.202 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
1.1.1.202 Mn2+ activates to 280% at 5 mM Levilactobacillus brevis
1.1.1.202 additional information addition of Co2+, Ni2+, or Mg2+ do not significantly affect PDOR activity at 5 mM Levilactobacillus brevis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.202 42000
-
-
 Levilactobacillus brevis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.202 3-hydroxypropanal + NADH + H+ Levilactobacillus brevis reduction of the aldehyde is the preferred reaction propane-1,3-diol + NAD+
-
 r
1.1.1.202 3-hydroxypropanal + NADH + H+ Levilactobacillus brevis 6239 reduction of the aldehyde is the preferred reaction propane-1,3-diol + NAD+
-
 r
1.1.1.202 propane-1,3-diol + NAD+ Levilactobacillus brevis
-
 3-hydroxypropanal + NADH + H+
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.202 Levilactobacillus brevis A0A0C1Q6R1
-
-
1.1.1.202 Levilactobacillus brevis 6239 A0A0C1Q6R1
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.202 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]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.1.202 32.6
-
 purified recombinant His-tagged enzyme, substrate propane-1,3-diol, pH 9.5, 25°C Levilactobacillus brevis
1.1.1.202 52.7
-
 purified recombinant His-tagged enzyme, substrate 3-hydroxypropanal, pH 7.5, 37°C Levilactobacillus brevis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.202 1,4-butanediol + NAD+
-
 Levilactobacillus brevis 4-hydroxybutanal + NADH + H+
-
 r
1.1.1.202 1-butanol + NAD+
-
 Levilactobacillus brevis 1-butanal + NADH + H+
-
 r
1.1.1.202 1-propanol + NAD+
-
 Levilactobacillus brevis 1-propanal + NADH + H+
-
 r
1.1.1.202 3-hydroxypropanal + NADH + H+ reduction of the aldehyde is the preferred reaction Levilactobacillus brevis propane-1,3-diol + NAD+
-
 r
1.1.1.202 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
1.1.1.202 3-hydroxypropanal + NADH + H+ reduction of the aldehyde is the preferred reaction Levilactobacillus brevis 6239 propane-1,3-diol + NAD+
-
 r
1.1.1.202 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
1.1.1.202 acetone + NADH + H+
-
 Levilactobacillus brevis ? + NAD+
-
 r
1.1.1.202 dihydroxyacetone + NADH + H+
-
 Levilactobacillus brevis ? + NAD+
-
 r
1.1.1.202 ethanol + NAD+
-
 Levilactobacillus brevis acetaldehyde + NADH + H+
-
 r
1.1.1.202 ethanol + NAD+
-
 Levilactobacillus brevis 6239 acetaldehyde + NADH + H+
-
 r
1.1.1.202 glyceraldehyde + NADH + H+
-
 Levilactobacillus brevis ? + NAD+
-
 r
1.1.1.202 glycerol + NAD+
-
 Levilactobacillus brevis dihydroxyacetone + NADH + H+
-
 r
1.1.1.202 glycerol + NAD+
-
 Levilactobacillus brevis 6239 dihydroxyacetone + NADH + H+
-
 r
1.1.1.202 hydroxyacetone + NADH + H+
-
 Levilactobacillus brevis ? + NAD+
-
 r
1.1.1.202 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 ?
-
 ?
1.1.1.202 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 ?
-
 ?
1.1.1.202 propane-1,2-diol + NAD+
-
 Levilactobacillus brevis 2-hydroxypropanal + NADH + H+
-
 r
1.1.1.202 propane-1,3-diol + NAD+
-
 Levilactobacillus brevis 3-hydroxypropanal + NADH + H+
-
 r

Subunits

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

Synonyms

EC Number Synonyms Comment Organism
1.1.1.202 DhaT
-
 Levilactobacillus brevis
1.1.1.202 PDOR
-
 Levilactobacillus brevis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.202 25
-
 alcohol oxidation Levilactobacillus brevis
1.1.1.202 37
-
 aldehyde reduction Levilactobacillus brevis

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.1.1.202 15 40 activity range, aldehyde reduction, profile overview Levilactobacillus brevis
1.1.1.202 25 45 activity range, alcohol oxidation, profile overview Levilactobacillus brevis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.1.202 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
1.1.1.202 37
-
 60% of enzyme relative activity remain after a 2h incubation at 37°C Levilactobacillus brevis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.202 7.5
-
 aldehyde reduction Levilactobacillus brevis
1.1.1.202 9.5
-
 alcohol oxidation Levilactobacillus brevis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.1.1.202 6 10 activity range, aldehyde reduction, profile overview Levilactobacillus brevis
1.1.1.202 8 10.5 activity range, alcohol oxidation, profile overview Levilactobacillus brevis

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.1.1.202 additional information
-
 PDOR is more stable in acid buffer than in alkaline condition Levilactobacillus brevis
1.1.1.202 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

EC Number Cofactor Comment Organism Structure
1.1.1.202 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
1.1.1.202 NADH
-
 Levilactobacillus brevis

General Information

EC Number General Information Comment Organism
1.1.1.202 evolution the enzyme belongs to the type III alcohol dehydrogenases Levilactobacillus brevis
1.1.1.202 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