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Literature summary for 4.2.3.77 extracted from

  • Exnowitz, F.; Meyer, B.; Hackl, T.
    NMR for direct determination of K(m) and V(max) of enzyme reactions based on the Lambert W function-analysis of progress curves (2012), Biochim. Biophys. Acta, 1824, 443-449.
    View publication on PubMed
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Application

Application Comment Organism
analysis use of NMR spectroscopy as a tool to analyze the kinetics of enzyme reactions using progress curves. The protocol presented is also a simple and direct approach for the measurement of enzyme kinetics in the presence of synthetic inhibitors. The conversion of farnesyl diphosphate into (+)-germacrene D by the enzyme germacrene D synthase involves an amphiphilic substrate forming micelles and a water insoluble product. Using proper controls, the conversion can well be analyzed by the progress curve approach using the Lambert W function Solidago canadensis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.379
-
 (2E,6E)-farnesyl diphosphate pH 7.8, 12°C Solidago canadensis

Organism

Organism UniProt Comment Textmining
Solidago canadensis Q70EZ6
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(2E,6E)-farnesyl diphosphate
-
 Solidago canadensis (+)-germacrene D + diphosphate
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.04
-
 (2E,6E)-farnesyl diphosphate pH 7.8, 12°C Solidago canadensis