Lan, Jie (1997) Escherichia coli mutants unable to use a combination of L-serine, glycine and L-leucine as carbon source. Masters thesis, Concordia University.
Previously, medium containing a combination of L-serine, glycine and L-leucine (SGL medium) has been used to study the characteristics, including the activation system, of L-serine deaminase (L-SD), an interesting enzyme from Escherichia coli that is first synthesized in an inactive form. In this thesis, I isolated two new E. coli SGL- mutants through $\lambda$placMu insertion. All these mutants MEW20b and MEWb1 are quite likely involved in the activation of L-SD enzyme. Applying inverse PCR technique, I identified the mutated gene in these two mutant strains to be nuoM and torA respectively. A formerly isolated SGL- mutant MEW84 was also identified as a $\lambda$placMu insertion in the glpC gene. Further experiments proved that mutations in these three genes actually were responsible for the SGL- phenotype of the mutant strains. A comparison of the functions of the three mutated genes suggests that electron donation may be part of the process necessary to activate L-SD. Physiological studies were carried out to investigate further these three mutants.
|Divisions:||Concordia University > Faculty of Arts and Science > Biology|
|Item Type:||Thesis (Masters)|
|Pagination:||xiii, 117 leaves : ill. ; 29 cm.|
|Degree Name:||Theses (M.Sc.)|
|Program:||Dept. of Biology|
|Thesis Supervisor(s):||Newman, E. B|
|Deposited By:||Concordia University Libraries|
|Deposited On:||27 Aug 2009 17:12|
|Last Modified:||04 Nov 2016 17:58|
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