Die Gene der (1-Methylalkyl)succinat-Synthase im anaeroben n-Alkanabbau des Betaproteobakteriums Stamm HxN1
Date Issued
2012-03-16
Author(s)
Supervisors
Referees
Abstract
The betaproteobacterial strain HxN1 completely oxidizes the n-alkanes pentane to octane under denitrifying conditions. The activation of n-alkanes is catalyzed by the glycyl radical enzyme (1-methylalkyl)succinate synthase, whose encoding mas genes are organized in an operon in strain HxN1. In this study, a genetic system for strain HxN1 was developed. The deletion of masD, encoding the catalytic subunit of the enzyme, revealed the presence of a second identical mas operon in strain HxN1. The physiological characterization of the mutant confirmed in vivo the anaerobic activation of n-alkanes by (1-methylalkyl)succinate synthase. The phenotype was restored by complementation with the entire mas operon. Regarding regulation, the mas operon was induced by several hydrocarbons and expression was not inhibited in the presence of a carboxylic acid or a sugar as second carbon source. Furthermore, it was attempted to crystallize the (1-methylalkyl)succinate synthase of strain HxN1.
Subjects
mas genes
;
anaerobic degradation
;
n-alkanes
Institution
Type
Dissertation
Secondary publication
No
Language
German
File(s)![Thumbnail Image]()
Loading...
Name
00102600-1.pdf
Size
2.21 MB
Format
Adobe PDF
Checksum
(MD5):d599557944a565dc9311c97f3686f6c6