The present disclosure relates to a putrescine-producing microorganism of the genus Corynebacterium, and a method of producing putrescine using the same.

Disclosed is an antibody which binds to a symmetrically dimethylated arginine analyte that can be used to detect a symmetrically dimethylated arginine analyte in a sample, such as in a homogeneous enzyme immunoassay method.

This invention relates to metabolically engineered microorganisms, such as bacterial and or fungal strains, and bioprocesses utilizing such strains. These strains enable the dynamic control of metabolic pathways, which can be used to optimize production. Dynamic control over metabolism is accomplished via a combination of methodologies including but not limited to transcriptional silencing and controlled enzyme proteolysis. These microbial strains are utilized in a multi-stage bioprocess encompassing at least two stages, the first stage in which microorganisms are grown and metabolism can be optimized for microbial growth and at least one other stage in which growth can be slowed or stopped, and dynamic changes can be made to metabolism to improve the production of desired product, such as a chemical or fuel.

Homogeneous immunoassays that allow for compensation of background signals inherent in samples and reagents. The use of homogeneous immunoassays for the detection of the presence or amount of symmetrical Dimethyl Arginine (SDMA) in biological samples. Reagents and kits for conducting the assays.

The invention concerns a genetically modified microorganism expressing a functional type I or II RuBisCO enzyme and a functional phosphoribulokinase (PRK), and in which the glycolysis pathway is at least partially inhibited, said microorganism being genetically modified so as to produce an exogenous molecule and/or to overproduce an endogenous molecule. According to the invention, the oxidative branch of the pentose phosphate pathway may also be at least partially inhibited. The invention also concerns the use of such a genetically modified microorganism for the production or overproduction of a molecule of interest and processes for the synthesis or bioconversion of molecules of interest.

Disclosed is an antibody which binds to a symmetrically dimethylated arginine analyte that can be used to detect a symmetrically dimethylated arginine analyte in a sample, such as in a homogeneous enzyme immunoassay method.

A method of quantifying ammonia, which method includes: performing a first reaction in which a test liquid containing ammonia is reacted with ATP and L-glutamic acid in the presence of glutamine synthetase to produce ADP; performing a second reaction in which the produced ADP is reacted with glucose in the presence of ADP-dependent hexokinase to produce glucose-6-phosphate; performing a third reaction in which the produced glucose-6-phosphate is reacted with an oxidized NAD compound in the presence of glucose-6-phosphate dehydrogenase to produce a reduced NAD compound; and quantifying the reduced NAD compound to quantify ammonia.

Disclosed are nucleotide sequences and corresponding amino acid sequences of Arxula adeninivorans genes that can be utilized to manipulate the lipid content and/or composition of a cell. Methods and compositions for utilizing this information are disclosed to increase the lipid content or modify the lipid composition of a cell by either increasing or decreasing the activity of certain genetic targets.

Disclosed is an antibody which binds to a symmetrically dimethylated arginine analyte that can be used to detect a symmetrically dimethylated arginine analyte in a sample, such as in a homogeneous enzyme immunoassay method.

Metabolites produced by a microorganism using more particularly oxaloacetate as substrate or co-substrate upstream in the biosynthesis pathway. There is indeed a need in the art for transformed, in particular recombinant, microorganisms having at least an increased ability to produce oxaloacetate, thus allowing an increased capacity to produce oxaloacetate-derived amino acids and amino acid derivatives, the oxaloacetate-derived amino acids and amino acid derivatives being termed oxaloacetate derivatives. The solution is the use of a genetically modified yeast including many modifications as described in the present text.