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Literature summary extracted from

  • Tsang, H.L.; Huang, J.L.; Lin, Y.H.; Huang, K.F.; Lu, P.L.; Lin, G.H.; Khine, A.A.; Hu, A.; Chen, H.P.
    Borneol dehydrogenase from Pseudomonas sp. strain TCU-HL1 catalyzes the oxidation of (+)-borneol and its isomers to camphor (2016), Appl. Environ. Microbiol., 82, 6378-6385.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.198 gene bdh, DNA and amino acid sequence determination and analysis, recombinnat expression in inclusion bodies in Escherichia coli strain BL21 Pseudomonas sp.
1.1.1.227 gene bdh, DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli in inclusion bodies Pseudomonas sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.198 0.2
-
(+)-borneol recombinant enzyme, pH 8.5, 22°C Pseudomonas sp.
1.1.1.227 0.16
-
(-)-borneol recombinant enzyme, pH 8.5, 22°C Pseudomonas sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.198 27600
-
-
Pseudomonas sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.198 (+)-borneol + NAD+ Pseudomonas sp.
-
(+)-camphor + NADH + H+
-
r
1.1.1.198 additional information Pseudomonas sp. GC-MS analysis of borneol degradation metabolites ?
-
?
1.1.1.227 (-)-borneol + NAD+ Pseudomonas sp.
-
(-)-camphor + NADH + H+
-
?
1.1.1.227 additional information Pseudomonas sp. GC-MS analysis of borneol degradation metabolites ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.198 Pseudomonas sp. A0A1B3EB36 a borneol-degrading strain, isolated from soil samples collected in Hualien County, Taiwan
-
1.1.1.227 Pseudomonas sp.
-
isolated from soil samples collected in Hualien County, Taiwan
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.198 recombinant enzyme refolded from inclusion bodies after expression in Escherichia coli strain BL21 by anion exchange chromatography and dialysis for refolding, native enzyme from strain TCU-HL1 by hydrophobic interaction and anion exchange chromatography Pseudomonas sp.
1.1.1.227 native enzyme from strain TCU-HL1 by hydrophobic interaction and anion exchange chromatography, recombinant refolded enzyme from Escherichia coli Pseudomonas sp.

Renatured (Commentary)

EC Number Renatured (Comment) Organism
1.1.1.198 recombinant enzyme from Escherichia coli inclusion bodies, solubilized in 25 ml of 0.1 M potassium phosphate buffer, pH 7.0, containing 6 M urea, 10 mM DTT, and 1 mM EDTA, for 2 h at room temperature stirred. Refolding by dissolution in 8 M urea and dialysis against 10 mM potassium phosphate buffer in the presence of 10% glycerol results in an inactive enzyme Pseudomonas sp.
1.1.1.227 recombinant enzyme from Escherichia coli inclusion bodies, solubilized in 25 ml of 0.1 M potassium phosphate buffer, pH 7.0, containing 6 M urea, 10 mM DTT, and 1 mM EDTA, for 2 h at room temperature stirred. Refolding by dissolution in 8 M urea and dialysis against 10 mM potassium phosphate buffer in the presence of 10% glycerol results in an inactive enzyme Pseudomonas sp.

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.1.1.198 additional information strain TCU-HL1 is able to use borneol as the sole carbon source Pseudomonas sp.
-
1.1.1.227 additional information strain TCU-HL1 is able to use borneol as the sole carbon source Pseudomonas sp.
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.198 (+)-borneol + NAD+
-
Pseudomonas sp. (+)-camphor + NADH + H+
-
r
1.1.1.198 (+)-borneol + NAD+ stereospecific reaction Pseudomonas sp. (+)-camphor + NADH + H+
-
?
1.1.1.198 (+)-borneol + NADP+
-
Pseudomonas sp. (+)-camphor + NADPH + H+
-
r
1.1.1.198 additional information GC-MS analysis of borneol degradation metabolites Pseudomonas sp. ?
-
?
1.1.1.198 additional information the enzyme is also active with (-)-borneol, reaction of EC 1.1.1.227 Pseudomonas sp. ?
-
?
1.1.1.227 (-)-borneol + NAD+
-
Pseudomonas sp. (-)-camphor + NADH + H+
-
?
1.1.1.227 (-)-borneol + NAD+ stereospecific reaction Pseudomonas sp. (-)-camphor + NADH + H+
-
?
1.1.1.227 additional information GC-MS analysis of borneol degradation metabolites Pseudomonas sp. ?
-
?
1.1.1.227 additional information the enzyme is also active with (+)-borneol, reaction of EC 1.1.1.198 Pseudomonas sp. ?
-
?

Subunits

EC Number Subunits Comment Organism
1.1.1.198 monomer 1 * 30000-40000, SDS-PAGE, 1 * 27600, about, sequence calculation, x * 30000-40000, recombinant enzyme, SDS-PAGE Pseudomonas sp.
1.1.1.198 More enzyme three-dimensional structural molecular modeling and docking Pseudomonas sp.
1.1.1.227 ? x * 30000-40000, recombinant enzyme, SDS-PAGE Pseudomonas sp.
1.1.1.227 More molecular modeling and docking of the three-dimensional structure of Pseudomonas sp. TCU-HL1 BDH Pseudomonas sp.

Synonyms

EC Number Synonyms Comment Organism
1.1.1.198 BDH
-
Pseudomonas sp.
1.1.1.198 THL1_4180
-
Pseudomonas sp.
1.1.1.227 BDH
-
Pseudomonas sp.
1.1.1.227 borneol dehydrogenase
-
Pseudomonas sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.198 22
-
assay at room temperature Pseudomonas sp.
1.1.1.227 22
-
assay at room temperature Pseudomonas sp.

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.198 0.75
-
(+)-borneol recombinant enzyme, pH 8.5, 22°C Pseudomonas sp.
1.1.1.227 0.53
-
(-)-borneol recombinant enzyme, pH 8.5, 22°C Pseudomonas sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.198 8.5
-
assay at Pseudomonas sp.
1.1.1.227 8.5
-
-
Pseudomonas sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.198 additional information an N-terminal conserved Gly13-X-X-X-Gly17-X-Gly19 sequence motif is present in the NAD(H)-binding region Pseudomonas sp.
1.1.1.198 NAD+ strong preference for NAD+ over NADP+ is observed. When cofactor NAD+ is replaced by NADP+, the catalytic rate of refolded BDH is reduced to below 5% compared to NAD+. NAD+ docking into the active site of the BDH homology model for binding domain and mode analysis Pseudomonas sp.
1.1.1.198 NADP+ strong preference for NAD+ over NADP+ is observed. When cofactor NAD+ is replaced by NADP+, the catalytic rate of refolded BDH is reduced to below 5% compared to NAD+ Pseudomonas sp.
1.1.1.227 NAD+ strong preference for NAD+ over NADP+ is observed. When cofactor NAD+ is replaced by NADP+, the catalytic rate of refolded BDH is reduced to below 5% compared to NAD+ Pseudomonas sp.
1.1.1.227 NADP+ strong preference for NAD+ over NADP+ is observed. When cofactor NAD+ is replaced by NADP+, the catalytic rate of refolded BDH is reduced to below 5% compared to NAD+ Pseudomonas sp.

pI Value

EC Number Organism Comment pI Value Maximum pI Value
1.1.1.198 Pseudomonas sp. sequence calculation
-
5.66

General Information

EC Number General Information Comment Organism
1.1.1.198 evolution BDH is a member of the NAD+-dependent dehydrogenases Pseudomonas sp.
1.1.1.198 metabolism the enzyme from the soil microorganism is involved in degradation of borneol through a camphor degradation pathway, pathway overview. Borneol is converted into camphor by BDH in borneol-degrading strain, Pseudomonas sp. strain TCU-HL1 and is further decomposed through a camphor degradation pathway Pseudomonas sp.
1.1.1.198 additional information enzyme three-dimensional structural modelling, and docking analysis, overview Pseudomonas sp.
1.1.1.227 metabolism borneol is converted into camphor by BDH in borneol-degrading strain, Pseudomonas sp. strain TCU-HL1 and is further decomposed through a camphor degradation pathway Pseudomonas sp.
1.1.1.227 additional information molecular modeling and docking of the three-dimensional structure of Pseudomonas sp. TCU-HL1 BDH Pseudomonas sp.