L-Threonine Fermentation. Part I

The fermentation of L-threonine, L-serine, L-cysteine and acrylic acid by a gram-negative coccus.

Optimization of fermentation conditions for the biosynthesis of L-threonine by Escherichia coli.

In this study, the fed-batch fermentation technique was applied to improve the yield of L-threonine produced by Escherichia coli TRFC. Various fermentation substrates and conditions were investigated to identify the optimal carbon source, its concentration and C/N ratio in the production of L-threonine. Sucrose was found to be the optimal initial carbon source and its optimal concentration was ...

Rat liver L-threonine dehydrogenase.

L-threonine dehydrogenase (E.C.1.1.1.103) catalyzes the NAD+-dependent transformation of Lthreonine to 2-amino 3-0x0-butyric acid, which spontaneously loses CO2 with the final production of aminoacetone ( 1) The enzyme is present in several microorganisms as well as in the liver of vertebrates (2-6). We studied some properties of the rat liver enzyme, showing that the activity was strongly inhi...

L-threonine in the treatment of spasticity.

Preclinical data indicate that the administration of the amino acid L-threonine increases glycine levels in rat spinal cord. In order to investigate glycinergic mechanisms in spasticity, and other signs of the upper motor syndrome, we gave 4.5 and 6.0 g/day of L-threonine to 18 patients with familial spastic paraparesis (FSP) according to a double-blind, crossover protocol. The response to trea...

Biodegradative L-threonine deaminase of Salmonella typhimurium.

The threonine deaminase formed under anaerobic conditions by Salmonella typhimurium is induced by l-serine and l-threonine, is catabolite repressible, requires cyclic adenosine 3',5'-monophosphate for its synthesis and adenylic acid for optimal activity, and is immunologically different from biosynthetic threonine deaminase.