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Literature summary for 1.1.1.198 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
Search for more literature for 1.1.1.198

Cloned(Commentary)

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

KM Value [mM]

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

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
27600
-
-
 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+
-
 r
additional information Pseudomonas sp. GC-MS analysis of borneol degradation metabolites ?
-
 ?

Organism

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

Purification (Commentary)

Purification (Comment) Organism
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.

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

Subunits

Subunits Comment Organism
monomer 1 * 30000-40000, SDS-PAGE, 1 * 27600, about, sequence calculation, x * 30000-40000, recombinant enzyme, SDS-PAGE Pseudomonas sp.
More enzyme three-dimensional structural molecular modeling and docking Pseudomonas sp.

Synonyms

Synonyms Comment Organism
BDH
-
 Pseudomonas sp.
THL1_4180
-
 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
0.75
-
 (+)-borneol recombinant enzyme, pH 8.5, 22°C Pseudomonas sp.

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
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.
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.
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

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

General Information

General Information Comment Organism
evolution BDH is a member of the NAD+-dependent dehydrogenases Pseudomonas sp.
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.
additional information enzyme three-dimensional structural modelling, and docking analysis, overview Pseudomonas sp.