Isochorismate hydroxymutase from a cell-suspension culture of Galium mollugo L. |
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Authors: | C Ledüc I Birgel R Müller E Leistner |
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Institution: | Institut für Pharmazeutische Biologie, Rheinische Friedrich-Wilhelms-Universit?t Bonn, Nu?allee 6, D-53115 Bonn, Germany, DE
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Abstract: | Isochorismate hydroxymutase (i.e. isochorismate synthase, EC 5.4.99.6) was purified from an anthraquinone-producing cell-suspension
culture of Galium mollugo L. Although attempts to stabilize the labile enzyme met with little success, a substantial increase in enzyme activity was
observed in the presence of glycine betaine (500 mM). Column chromatography on solid supports other than diethylaminoethyl
(DEAE)-Sephacel, Phenylsepharose Cl-4B or Cibacron Blue 3G-A did not give active enzyme preparations. In spite of these drawbacks
the enzyme was purified 573-fold. Enzyme activity depended strictly on the presence of Mg2+. Kinetic data for chorismate in the forward reaction (K
m = 807 μM, V
max = 6.2 pkat · mg−1) and for isochorismate in the reverse reaction (K
m = 675 μM, V
max = 5.9 pkat · mg−1) were determined.
Received: 18 November 1996 / Accepted: 28 December 1996 |
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Keywords: | : Anthraquinone biosynthesis Galium Isochorismate hydroxymutase Rubiaceae |
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