• Corpus ID: 82010216

Development of metabolic pathways for the biosynthesis of hydroxyacids and lactones

  title={Development of metabolic pathways for the biosynthesis of hydroxyacids and lactones},
  author={Collin H. Martin},
Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Chemical Engineering, February 2010. 


Enzymatic Activation of Lysine 2,3-Aminomutase from Porphyromonas gingivalis
This is the first report to show that, in the absence of chemical reductants, lysine 2,3-aminomutase activity is dependent upon the presence of flavodoxin, ferredoxin, or Flavodoxin-NADP+ reductase.
Expanding metabolism for biosynthesis of nonnatural alcohols
The feasibility of an approach to build artificial metabolism beyond the natural metabolic network is demonstrated by optimizing the biosynthesis of the 6-carbon alcohol, (S)-3-methyl-1-pentanol, which is included in the metabolite family of living systems.
Acetone-butanol fermentation revisited.
Histoire-substrats-biochimie and physiologie, facteurs favorisant le passage de the production d'acides a la production de solvents a la phase of production de Solvents, andrology and physiology, et developpement du procede.
Preparation of Optically Active β-Amino Acids from Microbial Polyester Polyhydroxyalkanoates
An efficient method for the preparation of optically active ethyl β-aminobutyrate from the biopolymer, poly-(R)-(-)-3-hydroxybutyrate (PHB) obtained from bacterial cells has been established using
Thioesterase II of Escherichia coli Plays an Important Role in 3-Hydroxydecanoic Acid Production
The hypothesis that the physiological role of thioesterase II in E. coli is to prevent the abnormal accumulation of intracellular acyl-coenzyme A is supported.
Directed enzyme evolution.
Analysis of acyl CoA ester intermediates of the mevalonate pathway in Saccharomyces cerevisiae
The level of the metabolites changed depending on the growth phase/specific growth rate and the carbon source, in a way which indicated that the synthesis of acetoacetyl CoA and HMG CoA is subject to glucose repression.
Metabolic engineering of Escherichia coli for 1-butanol production.
Biochemical characterization of the 2-ketoacid reductases encoded by ycdW and yiaE genes in Escherichia coli.
The similarity with YiaE led us to test whether this protein was responsible for the remaining glyoxylate reductase activity, and purification of YcdW and YIAE proteins permitted their kinetic characterization and comparison.