According to the present invention, theanine can efficiently be produced without exogenously adding ethylamine and without accumulation or leftover of ethylamine as a byproduct, by using a microorganism having enhanced activity to produce ethylamine with acetaldehyde and alanine as substrates and having enhanced activity of γ-glutamylmethylamide synthetase or glutaminase.

The present invention relates generally to glutaminase inhibitors of Formula I, Formula II, or Formula III, as well as pharmaceutical compounds containing them and methods of their use.

Disclosed herein are methods of increasing nitrogen fixation in a non-leguminous plant. The methods can comprise exposing the plant to a plurality of bacteria. Each member of the plurality comprises one or more genetic variations introduced into one or more genes or non-coding polynucleotides of the bacteria's nitrogen fixation or assimilation genetic regulatory network, such that the bacteria are capable of fixing atmospheric nitrogen in the presence of exogenous nitrogen. The bacteria are not intergeneric microorganisms. Additionally, the bacteria, in planta, produce 1% or more of the fixed nitrogen in the plant.

The present invention relates to a combination therapy for the treatment of cancer, particularly to combinations of oligo(2-(2-ethoxy)ethoxy ethyl guanidinium chloride), poly(hexamethylendiamine guanidiniumchloride), polyetheramines, triethyleneglycol diamine, enzymes, PGPR, amino acids, antioxidants like humic acids and some natural products like phytotherapeutic plant extracts. The combination therapy of the present invention shows enhanced anti-cancerous therapeutic effects compared to the effect of each of the components administered alone. In some embodiments, the combination therapy provide for a synergistic anti-cancer effect. A liposomal drug composition comprising; A dimeric or polymeric guanidine derivative or polyetheramines, triethyleneglycol diamine, enzymes, PGPR, amino acids, antioxidants like humic acids and some natural products like phytotherapeutic plant extracts a pharmaceutically acceptable salt thereof as drug substance, and a lipid modified by polyethylene glycole (PEG).

The present invention relates to a labeled glutaminase (GLS) protein comprising a GLS protein and a fluorescent reporter group attached to the GLS protein, wherein the fluorescent reporter group is attached to the GLS protein within the glutaminase domain pfam04960 of GLS. The present invention also relates to isolated glutaminase protein mutants. Also disclosed is a method of screening for compounds that allosterically bind to a glutaminase protein. The present invention also relates to a method of identifying compounds that inhibit or stabilize tetramer formation of glutaminase protein. The present invention further relates to a screening kit for compounds that inhibit or stabilize tetramer formation.

The purpose of the present invention is to provide a processing technique with which it is possible to enhance the aroma of a plant protein food/beverage product ingredient and/or of a plant protein food/beverage product. By using a method for manufacturing a processed article of a plant protein food/beverage product ingredient and/or of a plant protein food/beverage product, the method including a step for treating a plant protein food/beverage product ingredient and/or a plant protein food/beverage product with a protein deamidation enzyme and a -amylase, it is possible to enhance the raw-ingredient-derived aroma of the resultant processed article of the plant protein food/beverage product ingredient and/or of the plant protein food/beverage product.

Disclosed herein are methods of increasing nitrogen fixation in a non-leguminous plant. The methods can comprise exposing the plant to a plurality of bacteria. Each member of the plurality comprises one or more genetic variations introduced into one or more genes or non-coding polynucleotides of the bacteria's nitrogen fixation or assimilation genetic regulatory network, such that the bacteria are capable of fixing atmospheric nitrogen in the presence of exogenous nitrogen. The bacteria are not intergeneric microorganisms. Additionally, the bacteria, in planta, produce 1% or more of the fixed nitrogen in the plant.

The present technology relates to kidney-type glutaminase (GLS) proteins that have a phenylalanine to tryptophan substitution at the position corresponding to residue 322 of human glutaminase C (GAC), and methods of using such proteins to screen for compounds that bind to the activation loop of GLS and/or modulate glutaminase activity of GLS.

The present invention provides enzymes that have been optimized by implementation of Protein Repair One Stop Shop (PROSS), an algorithm that generates protein design(s) for enhanced stability without changing either enzymatic properties or enzyme active site conformation of the respective enzyme. The protein design(s) generated by PROSS introduce mutations to the amino acid sequence of a wild-type protein, resulting in a mutated amino acid sequence that encodes a variant of the wild-type enzyme, i.e., an enzyme variant, which has an enhanced stability, core packing, surface polarity and backbone rigidity, a higher functional expression, and/or a combination thereof, compared to the stability core packing, surface polarity and backbone rigidity, functional expression and/or a combination thereof, of the wild-type enzyme.

The present invention relates generally to glutaminase inhibitors of Formula I, Formula II, or Formula III, as well as pharmaceutical compounds containing them and methods of their use.