Isolierung und Rekonstitution des Alkan-Monooxygenase-Systems der HefeLodderomyces elongisporus

Schunck, Wolf‐Hagen; Riege, P.; Honeck, Horst; Müller, Hansgeorg

doi:10.1002/jobm.3630231007

Cited by 14 publications

References 23 publications

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Enzym‐Induktion in der Hefe Lodderomyces in Gegenwart von n‐Alkanen

Müller¹,

Mauersberger²,

Schunck³

et al. 1983

J of Basic Microbiology

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The utilization of n-alkanes is connected with extensive modifications of the yeast cell, especially of the cytochrome P-450-containing membrane. Beside the cytochrome P-450 the NADPH cytochrome P-450 reductasa, the cytochrome b6, long-chain alcohol and long-chain aldehyde dehydrogenases are induced. The activity of the alkane-hydroxylating enzyme system grows more than the concentration of its terminal oxidase. The induction of the cytochrome P-460 is inhibited by cyclcheximide. A low concentration of oxygen in the culture medium amplifies the induction both of the alkane-hydroxylating enzyme system and of catalase and cytochrome oxidase, which arelocalized in the peroxisomes and mitochondria, respectively. Von Prokaryoten wie von Eukaryoten ist der

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Enzym‐Induktion in der Hefe Lodderomyces in Gegenwart von n‐Alkanen

Müller¹,

Mauersberger²,

Schunck³

et al. 1983

J of Basic Microbiology

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Subcellular organization of alkane oxidation in the yeast Candida maltosa

Mauersberger¹,

Kärgel²,

Matyashova³

et al. 1987

J. Basic Microbiol.

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After spheroplast lysis and differential centrifugation the alkane monooxygenase system consisting of cytochrome P‐450 and the NADPH‐cytochrome P‐450 reductase of alkane‐grown Candida maltosa cells is enriched in the microsomal fraction. This membrane fraction is nearly free of intact mitochondria (cytochrome oxidase) and peroxisomes (catalase), but contains considerable amounts of plasma membrane fractures (azide insensitive, vanadate‐sensitive Mg2+‐ATPase) as demonstrated by biochemical an electron microscopic examinations. By means of sucrose density gradient centrifugation it was possible to separate the cytochrome P‐450 containing membranes ( = 1,11 g/cm3) from the plasma membranes ( = 1,18 g/cm3). Therefore the cytochrome P‐450 alkane monooxygenase system is most likely localized in the endoplasmic reticulum of the yeast cells. For the following enzymatic steps of terminal alkane oxidation to the corresponding fatty acid a quite different subcellular distribution was observed. The fatty alcohol oxidase and aldehyde dehydrogenase activities are mainly localized in the mitochondrial peroxisomal membrane fraction. During the oxidation of n‐alkanes by yeast cells the fatty alcohol should be regarded as an intracellular transport from between the cytochrome P‐450 containing endoplasmic reticulum and the sites of its further oxidation in peroxisomes and mitochondria.

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