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Literature summary for 4.2.1.127 extracted from

  • Brodkorb, D.; Gottschall, M.; Marmulla, R.; Lüddeke, F.; Harder, J.
    Linalool dehydratase-isomerase, a bifunctional enzyme in the anaerobic degradation of monoterpenes (2010), J. Biol. Chem., 285, 30436-30442.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.2.1.127

Activating Compound

Activating Compound Comment Organism Structure
dithiothreitol the aerobically purified enzyme is anaerobically activated in the presence of 2 mM dithiothreitol Castellaniella defragrans
additional information the enzyme requires dithiothreitol as a reducing agent and an oxygen free microenvironment (less than 1% (v/v)) for the dehydration of linalool Castellaniella defragrans

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Castellaniella defragrans

Inhibitors

Inhibitors Comment Organism Structure
KCl high salt concentrations (NaCl, KCl, or MgCl2 at a concentration of 220 mM) inhibit the enzyme activity completely Castellaniella defragrans
MgCl2 high salt concentrations (NaCl, KCl, or MgCl2 at a concentration of 220 mM) inhibit the enzyme activity completely Castellaniella defragrans
additional information not inhibited by 10% (v/v) DMSO. EDTA (5 mM) does not affect the enzyme activity Castellaniella defragrans
NaCl high salt concentrations (NaCl, KCl, or MgCl2 at a concentration of 220 mM) inhibit the enzyme activity completely Castellaniella defragrans
O2 the enzyme requires dithiothreitol as a reducing agent and an oxygen free microenvironment (less than 1% (v/v)) for the dehydration of linalool Castellaniella defragrans
pyridoxal 5'-phosphate 1 mM; 35% inhibition Castellaniella defragrans
S-adenosyl-L-methionine 40 mM, 80% inhibition Castellaniella defragrans
Ti(III)citrate 1 mM, complete inhibition Castellaniella defragrans
Urea 20% activity remains at 3 M urea, and no activity is detected in 6 M urea Castellaniella defragrans

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.75
-
 linalool pH 9.0, 35°C Castellaniella defragrans

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
40000
-
 4 * 40000, SDS-PAGE Castellaniella defragrans
160000
-
 gel filtration Castellaniella defragrans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
myrcene + H2O Castellaniella defragrans degradation of myrcene linalool
-
 r
myrcene + H2O Castellaniella defragrans 65Phen degradation of myrcene linalool
-
 r

Organism

Organism UniProt Comment Textmining
Castellaniella defragrans E1XUJ2
-
-
Castellaniella defragrans 65Phen E1XUJ2
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification precursor protein with a signal peptide for a periplasmatic location Castellaniella defragrans

Purification (Commentary)

Purification (Comment) Organism
-
 Castellaniella defragrans

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.55
-
 pH 9.0, 35°C Castellaniella defragrans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
linalool dehydration of linalool to myrcene in the absence of molecular oxygen. The aerobically purified enzyme is anaerobically activated in the presence of 2 mM dithiothreitol. The enzyme catalyzes in vitro the reaction in both directions depending on the thermodynamic driving forces Castellaniella defragrans myrcene + H2O myrcene is the only product detected r
linalool dehydration of linalool to myrcene in the absence of molecular oxygen. The aerobically purified enzyme is anaerobically activated in the presence of 2 mM dithiothreitol. The enzyme catalyzes in vitro the reaction in both directions depending on the thermodynamic driving forces Castellaniella defragrans 65Phen myrcene + H2O myrcene is the only product detected r
additional information neither the monoterpenes alpha- and beta-ocimene nor the monoterpenoids citronellol and nerol are transformed Castellaniella defragrans ?
-
 ?
additional information neither the monoterpenes alpha- and beta-ocimene nor the monoterpenoids citronellol and nerol are transformed Castellaniella defragrans 65Phen ?
-
 ?
myrcene + H2O degradation of myrcene Castellaniella defragrans linalool
-
 r
myrcene + H2O degradation of myrcene Castellaniella defragrans 65Phen linalool
-
 r

Subunits

Subunits Comment Organism
tetramer 4 * 40000, SDS-PAGE Castellaniella defragrans

Synonyms

Synonyms Comment Organism
linalool dehydratase-isomerase bifunctional enzyme that catalyzes the reversible dehydration and isomerization of linalool (3,7-dimethyl-1,6-octadien-3-ol) Castellaniella defragrans

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
35
-
-
 Castellaniella defragrans

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
28 40 28°C: about 60% of maximal activity, 40°C: about 80% of maximal activity Castellaniella defragrans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
 Tris-HCl buffer, sharp decrease in linalool dehydratase activity beyond pH 9.0 Castellaniella defragrans

Cofactor

Cofactor Comment Organism Structure
additional information contains no prosthetic group Castellaniella defragrans