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Literature summary for 3.1.7.3 extracted from

  • Croteau R.; Karp, F.
    Biosynthesis of monoterpenes: Hydrolysis of bornyl pyrophosphate, an essential step in camphor biosynthesis, and hydrolysis of geranyl pyrophosphate, the acyclic precursor of camphor, by enzymes from Sage (Salvia officinalis) (1979), Arch. Biochem. Biophys., 198, 523-532.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
diisopropylfluorophosphate IC50: 0.8 for 65 kDa BPP hydrolase Salvia officinalis
diphosphate IC50: 0.6 for 65 kDa BPP hydrolase, 2.5 for 20 kDa BPP hydrolase Salvia officinalis
F- IC50: 0.7 mM for 65 kDa BPP hydrolase, 15.5 mM for 20 kDa BPP hydrolase Salvia officinalis
Mn2+ IC50: 0.1 mM for 65 kDa BPP hydrolase, 15.0 mM for 20 kDa BPP hydrolase Salvia officinalis
phosphate IC50: 10.5 mM for 65 kDa BPP hydrolase, 4.3 for 20 kDa BPP hydrolase Salvia officinalis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.023
-
D-bornyl-diphosphate 65 kDa BPP hydrolase Salvia officinalis
0.12
-
D-bornyl-diphosphate 20 kDa BPP hydrolase Salvia officinalis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ slight stimulation at 10 mM Salvia officinalis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
20000
-
gel filtration, activity on bornyl-diphosphate and bornyl-monophosphate Salvia officinalis
65000
-
gel filtration Salvia officinalis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-bornyl-diphosphate + H2O Salvia officinalis camphor biosynthesis ?
-
?
geranyl-diphosphate + H2O Salvia officinalis acyclic precursor of camphor ?
-
?

Organism

Organism UniProt Comment Textmining
Salvia officinalis
-
sage
-

Purification (Commentary)

Purification (Comment) Organism
first step: gel filtration, second step: hydroxylapatite chromatography Salvia officinalis

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
Salvia officinalis
-

Storage Stability

Storage Stability Organism
0°C, 100 mM Tris-maleate pH 7.0, one week, 50% loss of activity for 20 kDa BPP hydrolase Salvia officinalis
0°C, 100 mM Tris-maleate pH 7.0, one week, less than 15% loss of activity for 65 kDa BPP hydrolase Salvia officinalis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-bornyl-diphosphate + H2O
-
Salvia officinalis D-borneol + diphosphate
-
?
D-bornyl-diphosphate + H2O camphor biosynthesis Salvia officinalis ?
-
?
D-bornyl-phosphate + H2O
-
Salvia officinalis D-borneol + phosphate
-
?
geranyl-diphosphate + H2O preference for geranyl-ester for 65 kDa BPP hydrolase Salvia officinalis geraniol + diphosphate
-
?
geranyl-diphosphate + H2O acyclic precursor of camphor Salvia officinalis ?
-
?
neryl-diphosphate + H2O
-
Salvia officinalis nerol + diphosphate
-
?

Synonyms

Synonyms Comment Organism
pyrophosphate hydrolase
-
Salvia officinalis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5
-
65 kDa BPP hydrolase Salvia officinalis
7.6
-
20 kDa BPP hydrolase Salvia officinalis

pH Range

pH Minimum pH Maximum Comment Organism
2.5 4.5 65 kDa BPP hydrolase, 33% of maximum activity above pH 4.5 and below pH 2.5 Salvia officinalis

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.1
-
IC50: 0.1 mM for 65 kDa BPP hydrolase, 15.0 mM for 20 kDa BPP hydrolase Salvia officinalis Mn2+
0.6
-
IC50: 0.6 mM for 65 kDa BPP hydrolase Salvia officinalis diphosphate
0.7
-
IC50: 0.7 mM for 65 kDa BPP hydrolase, 15.5 mM for 20 kDa BPP hydrolase Salvia officinalis F-
0.8
-
IC50: 0.8 mM for 65 kDa BPP hydrolase Salvia officinalis diisopropylfluorophosphate
2.5
-
IC50 2.5 mM for 20 kDa BPP hydrolase Salvia officinalis diphosphate
10.5
-
IC50: 10.5 mM for 65 kDa BPP hydrolase, 4.3 for 20 kDa BPP hydrolase Salvia officinalis phosphate