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Literature summary for 1.1.1.227 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)

Cloned (Comment) Organism
gene bdh, DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli in inclusion bodies Pseudomonas sp.

KM Value [mM]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Pseudomonas sp.
-
isolated from soil samples collected in Hualien County, Taiwan
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme from strain TCU-HL1 by hydrophobic interaction and anion exchange chromatography, recombinant refolded enzyme from Escherichia coli Pseudomonas sp.

Renatured (Commentary)

Renatured (Comment) Organism
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

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

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
? x * 30000-40000, recombinant enzyme, SDS-PAGE Pseudomonas sp.
More molecular modeling and docking of the three-dimensional structure of Pseudomonas sp. TCU-HL1 BDH Pseudomonas sp.

Synonyms

Synonyms Comment Organism
BDH
-
Pseudomonas sp.
borneol dehydrogenase
-
Pseudomonas sp.

Temperature Optimum [°C]

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

Turnover Number [1/s]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
-
Pseudomonas sp.

Cofactor

Cofactor Comment Organism Structure
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.
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.

General Information

General Information Comment Organism
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.
additional information molecular modeling and docking of the three-dimensional structure of Pseudomonas sp. TCU-HL1 BDH Pseudomonas sp.