The Pseudomonas oleovorans alkane hydroxylase gene
نویسندگان
چکیده
منابع مشابه
Carbon-source-dependent expression of the PalkB promoter from the Pseudomonas oleovorans alkane degradation pathway.
Pseudomonas oleovorans GPo1 can metabolize medium-chain-length alkanes by means of an enzymatic system whose induction is regulated by the AlkS protein. In the presence of alkanes, AlkS activates the expression of promoter PalkB, from which most of the genes of the pathway are transcribed. In addition, expression of the first enzyme of the pathway, alkane hydroxylase, is known to be influenced ...
متن کاملControlled and functional expression of the Pseudomonas oleovorans alkane utilizing system in Pseudomonas putida and Escherichia coli.
The OCT plasmid encodes enzymes for alkane hydroxylation and alkanol dehydrogenation. Structural components are encoded on the 7.5-kilobase pair alkBAC operon, whereas positive regulatory components are encoded by alkR. We have constructed plasmids containing fusions of cloned alkBAC and alkR DNA and used these fusion plasmids to study the functional expression of the alkBAC operon and the regu...
متن کاملInduction of alkane hydroxylase proteins by unoxidized alkane in Pseudomonas putida.
In vitro complementation assays have been used to demonstrate the induction of alkane hydroxylase proteins in mutants lacking the ability to convert n-alkanes to their primary alcohols. Purified heptane is an effective inducer in a mutant lacking detectable hydroxylase activity.
متن کاملFractionation of inducible alkane hydroxylase activity in Pseudomonas putida and characterization of hydroxylase-negative plasmid mutations.
The plasmid-determined inducible alkane hydroxylase of Pseudomonas putida resolved into particulate and soluble fractions. Spinach reductase and spinach ferredoxin could replace the soluble hydroxylase component. Two alkane hydroxylase mutants show in vitro complementation (S. Benson and J. Shapiro, J. Bacteriol., 123: 759-760, 1975): one, alk-7, lacks an active soluble component and the other,...
متن کاملCharacterization of the omega-hydroxylase of Pseudomonas oleovorans as a nonheme iron protein.
The w-hydroxylase of Pseudomonas oleovoruns, which catalyzes the hydroxylation of fatty acids and alkanes and the epoxidation of alkenes in the presence of a reduced pyridine nucleotide, a reductase, rubredoxin, and molecular oxygen, has been purified to electrophoretic homogeneity. Octane hydroxylation and octadiene epoxidation activities appear to remain at a constant ratio during the purific...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1989
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)83564-5