Hydrophobic enzymes in hydrocarbon degradation
| Autor: | J. C. van Ravenswaay Claasen, A. C. van der Linden |
|---|---|
| Rok vydání: | 1971 |
| Předmět: |
Chromatography
Gas Stereochemistry Carboxylic Acids Alcohol oxidoreductase Primary alcohol Biochemistry Mixed Function Oxygenases Hydrophobic effect Hydroxylation chemistry.chemical_compound Isomerism Cyclohexanes Alkanes Benzene Derivatives Enzyme inducer Coloring Agents Alcohol dehydrogenase chemistry.chemical_classification Binding Sites biology Ethanol Chemistry Organic Chemistry Substrate (chemistry) Stereoisomerism Cell Biology Hydrocarbons Culture Media Models Structural Oxygen Alcohol Oxidoreductases Enzyme Indophenol Alcohols Enzyme Induction Pseudomonas aeruginosa biology.protein Cytochromes Chlorine Oxidation-Reduction NADP Ethers |
| Zdroj: | Lipids. 6(7) |
| ISSN: | 0024-4201 |
| Popis: | Pseudomonas aeruginosa (strain 473) constitutively contains an NADP-linked alcohol dehydrogenase. This enzyme is believed to function only in assimilative processes, because growth on primary alcohols, α,ω-diols orn-alkanes induces another alcohol dehydrogenase which is not linked to a pyridine nucleotide. The inducible enzyme reduces bovine cytochromec and various dyes, but not oxygen. At least two variants of the dissimilative NAD(P)-independent enzyme can be induced by choosing the substrate used for growth. The main difference between the two variants is their different capacity to oxidize ethanol. A noteworthy property of the inducible enzyme is its hydrophobic character. Some of its consequences in paraffin dissimilation are discussed. The paraffin hydroxylase system of the heptane-grownPseudomonas was found to hydroxylate various types of hydrocarbons and thus shows a low substrate specificity. On the other hand, remarkable specificities were also encountered; in some cases only thetrans configuration of a substrate was hydroxylated. With respect to the site of hydroxylation, the enzyme system was quite specific, even to the extent that, in appropriate cases, the hydroxyl group was introduced in thetrans-position only. The results obtained with the enzymatic hydroxylations, including some of the specificities encountered, can be explained by assuming that substrate molecules capable of attaining a planar conformation are bound by hydrophobic forces to the enzyme surface. |
| Databáze: | OpenAIRE |
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