Both glutamic acid decarboxylase (GAD) and myelin basic protein (MBP), which are cytoplasmic proteins, have been produced by the methods of the present invention.
GABA is a metabolite of plants and microorganisms that results from the decarboxylation of glutamic acid decarboxylase (GAD).
The present application deals with the use of glutamic acid decarboxylase (GAD) 65 for treating autoimmune diabetes.
In addition, we must note that excess L-glutamine is converted into GABA with the help of vitamin B6 and an enzyme called glutamic acid decarboxylase (GAD).
GABA (gamma-aminobutyric acid) is found in almost every region of brain, and is formed through the activity of the enzyme glutamic acid decarboxylase (GAD).
The plant is transformed with a recombinant nucleic acid encoding glutamic acid decarboxylase isolated from Orγza sativa.
Glutamic acid decarboxylase is an enzyme that is responsible for synthesizing an important inhibitory neurotransmitter in the body.
Additionally, a loss of glutamic acid decarboxylase 67 neurons in CA1 of the hippocampus is seen in aged canines over 10 years of age (Hwang et al., 2008b).
Specifically exemplified is the transformation of bacteria with genes, obtainable from Zymomonas mobilis, which encode pyruvate decarboxylase and alcohol dehydrogenase.
A polypeptide with pyruvate decarboxylase activity, derived from the pyruvate decarboxylase from Zymomonas mobilis by substitution of an amino acid in position 553.
The invention provides isolated nucleic acids molecules which encode pyruvate decarboxylase enzymes having improved decarboxylase activity, substrate affinity, thermostability, and activity at different pH.
The enzymes have alcohol acyl transferase, alcohol dehydrogenase, pyruvate decarboxylase, thiolase, aminotransferase and esterase activities, respectively.
Both organisms produce near theoretical ethanol yields without expressing pyruvate decarboxylase
This process is stimulated by vitamin B6 in its active form and the enzyme glutamate decarboxylase (GAD).
This process is catalyzed by the active form of vitamin B6 and the enzyme glutamate decarboxylase (GAD).
the Third analysis, which ensures maximum reliability of the diagnosis, is a test for antibodies to glutamic acid decarboxylase (antibodies to GAD).
The present invention relates to glutamate decarboxylase (GAD) gene sequence isolated from Oryza sativa (cv Rasi) and their corresponding encoded polypeptides that confer the traits of improved nitrogen use efficiency in plants.
Additionally, valerian has been shown to stimulate an enzyme called glutamate decarboxylase (GAD) which creates GABA from glutamate in the brain.
Ornithine decarboxylase participates on the metabolism of glutathione and amino acids.
It is considered that the medication acts on the hair follicle and helps to block the enzyme (ornithine decarboxylase) which is responsible hair growth cycle.
The invention relates to a process for obtaining a pyruvate decarboxylase by isolation from a producer organism.
It is the aim of the invention to obtain a pyruvate decarboxylase with improved synthesis capacity concerning the formation of (R)-(-)-phenylacetylcarbinole.
In addition, the pyruvate decarboxylase has a specific activity with regard to phenylacetylcarbinole formation of > 1 U/mg.
A novel operon and plasmids comprising genes which code for the alcohol dehydrogenase and pyruvate decarboxylase activities of Zymomonas mobilis are described.
The pyruvate decarboxylase is capable of forming (R)-(-)-phenylacetylcarbinole (I) in » 95 % enantiomer unit with a product ratio of (I) to 2-hydroxypropiophenone of » 95 %.
Oxalate decarboxylase crystals, including stabilized crystals, such as cross-linked crystals of oxalate decarboxylase, are disclosed.
The invention relates to a novel Glutamic Acid Decarboxylase (GAD).
A recombinant oxalate decarboxylase is produced by culturing the producing bacterium as described above and then harvesting the oxalate decarboxylase thus produced.
Various methods of employing the dicamba decarboxylase sequences are provided.
A host bacterium is transformed by this vector to give an oxalate decarboxylase-producing bacterium.
Various methods of employing the dicamba decarboxylase sequences are provided.
Further disclosed are: a hamster cysteine sulfinate decarboxylase, DNA encoding the hamster cysteine sulfinate decarboxylase, a recombinant vector, a transformed cell, and others.
Methods are also provided to identify additional dicamba decarboxylase variants.
Methods are also provided to identify additional dicamba decarboxylase variants.
The utility of this concept is demonstrated in the missing gene for lysine decarboxylase, and the resulting inhibitory activity of cadaverine (the diaminoalkyl reaction product of lysine decarboxylase) on the Shigella enterotoxins.
Inhibition of ornithine decarboxylase enzymes (ODCs)
Necessary enzymes deficiency, like cysteinsulfinic decarboxylase
an antibody specific for glutamic acid decarboxylase (GAD);
Pharmaceutical compositions comprising spray-dried oxalate decarboxylase crystals are disclosed.
The invention also relates to monoclonal antibodies which specifically bind the cytosolic NADP-dependent malate-decarboxylase and do not cross react with any other malate-decarboxylase isoenzymes.
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