C12Y401/01019

Method of producing an active-form mutant enzyme

A method for expressing, as a soluble protein or an active-form mutant enzyme, an enzyme that cannot be expressed as a soluble protein or an active-form enzyme in a heterologous expression system or that is obtained in a minute amount even when an active-form enzyme is expressed, the method including a technique for selecting an effective mutation site and a mutated amino acid. A new active-form mutant enzyme is also disclosed. The method involves: specifying an insoluble protein or an inactive-form enzyme; specifying a hydrophilic amino acid in a hydrophobic domain and/or a hydrophobic amino acid in a hydrophilic domain of an -helix structure portion of the insoluble protein or the inactive-form enzyme and preparing a gene that codes for an amino acid sequence in which a substitution is made to the hydrophilic amino acid in the hydrophobic domain and/or the hydrophobic amino acid in the hydrophilic domain.

Tropane Alkaloid Transporters and Methods of Making Tropane Alkaloids Using the Same
20240191267 · 2024-06-13 ·

Provided herein, among other things, is an engineered non-plant cell that produces a tropane alkaloid product, a precursor of a tropane alkaloid product, or a derivative of a tropane alkaloid product by means of a complement of biosynthetic enzymes and a complement of transporter proteins. A method for producing a tropane alkaloid, a precursor of a tropane alkaloid product, or a derivative of a tropane alkaloid product that makes use of the cell is also described.

Active-Form Mutant Enzyme Production Method, New Active-Form Mutant Enzyme, and Solubilized Mutant Protein Production Method

A method for expressing, as a soluble protein or an active-form mutant enzyme, an enzyme that cannot be expressed as a soluble protein or an active-form enzyme in a heterologous expression system or that is obtained in a minute amount even when an active-form enzyme is expressed, the method including a technique for selecting an effective mutation site and a mutated amino acid. A new active-form mutant enzyme is also disclosed. The method involves: specifying an insoluble protein or an inactive-form enzyme; specifying a hydrophilic amino acid in a hydrophobic domain and/or a hydrophobic amino acid in a hydrophilic domain of an -helix structure portion of the insoluble protein or the inactive-form enzyme and preparing a gene that codes for an amino acid sequence in which a substitution is made to the hydrophilic amino acid in the hydrophobic domain and/or the hydrophobic amino acid in the hydrophilic domain.

Antibodies to argininosuccinate synthase and related methods
09938355 · 2018-04-10 · ·

Antibodies, and antigen-binding fragments, which specifically bind to argininosuccinate synthase, and related compositions, kits, and methods of use, which are useful as companion diagnostics to identify suitable subjects for arginine deprivation or depletion therapies such as ADI-PEG 20 and other arginine deiminase (ADI) polypeptide-based therapies.

MODULATING ALKALOID PROFILES IN NICOTIANA TABACUM

A non-naturally occurring or transgenic Nicotiana tabacum plant cell encompassing a heterologous polynucleotide that encodes arginine decarboxylase (ADC) and a method for producing such a cell are provided. Transgenic Nicotiana tabacum plants, plant parts, and plant tissues including these cells and plant materials and biomass produced by these cells and plants cells forming such a plant are provided. Materials produced by this plant, including plant leaves, flowers, seeds, extracts, and other plant biomass obtained from this plant including materials that have altered alkaloid levels are disclosed. Also provided are smoking articles including various tobacco products containing these materials.

Gene Products of Bacillus Licheniformis Which Form Odorous Substances and Improved Biotechnological Production Methods Based Thereon

The present invention relates to 25 hitherto undescribed genes of B. licheniformis and gene products derived thereform and all sufficiently homologous nucleic acids and proteins thereof. They occur in five different metabolic pathways for the formation of odorous substances. The metabolic pathways in question are for the synthesis of: 1) isovalerian acid (as part of the catabolism of leucine), 2) 2-methylbutyric acid and/or isobutyric acid (as part of the catabolism of valine and/or isoleucine), 3) butanol and/or butyric acid (as part of the metabolism of butyric acid), 4) propyl acid (as part of the metabolism of propionate) and/or 5) cadaverine and/or putrescine (as parts of the catabolism of lysine and/or arginine). The identification of these genes allows biotechnological production methods to be developed that are improved to the extent that, to assist these nucleic acids, the formation of the odorous substances synthesised via these metabolic pathways can be reduced by deactivating the corresponding genes in the micro-organism used for the biotechnological production. In addition, these gene products are thus available for preparing reactions or for methods according to their respective biochemical properties.

Tropane alkaloid (TA) producing non-plant host cells, and methods of making and using the same

Provided herein, among other things, is an engineered non-plant cell that produces a tropane alkaloid product, a precursor of a tropane alkaloid product, or a derivative of a tropane alkaloid product. A method for producing a tropane alkaloid, a precursor of a tropane alkaloid product, or a derivative of a tropane alkaloid product that makes use of the cell is also described.

Methods and kits for identifying subjects responsive to arginine deprivation therapy

Disclosed herein are methods and kits for identifying responsiveness or non-responsiveness of a cancer subject to arginine deprivation therapy. The method includes determining the presence of a G/G genotype of rs13338697 of the target nucleic acid in a biological sample derived from the subject by use of a polymerase chain reaction (PCR)-based method, in which the presence of the G/G genotype of rs13338697 of the target nucleic acid is an indication that the subject is responsive to the arginine deprivation therapy.