Provided herein are non-naturally occurring microbial organisms having biosynthetic pathways for production of target products and one or more genetic modifications that reduce a byproduct of the biosynthetic pathway. Compositions of target products from such cells and methods of using such cells are provided.

The present disclosure provides recombinant bacterial cells that have been engineered with genetic circuitry which allow the recombinant bacterial cells to sense a patient's internal environment and respond by turning an engineered metabolic pathway on or off. When turned on, the recombinant bacterial cells complete all of the steps in a metabolic pathway to achieve a therapeutic effect in a host subject. These recombinant bacterial cells are designed to drive therapeutic effects throughout the body of a host from a point of origin of the microbiome. Specifically, the present disclosure provides recombinant bacterial cells that comprise an amino acid catabolism enzyme for the treatment of diseases and disorders associated with amino acid metabolism, including cancer, in a subject. The disclosure further provides pharmaceutical compositions and methods of treating disorders associated with amino acid metabolism, such as cancer.

Isolated oxidases, isolated polynucleotides encoding the oxidases, and methods of using the oxidases to produce -oxocarboxylic acid compounds or L--amino acid compounds are described.

A polynucleotide encoding an amino acid sequence represented by SEQ ID NO: 1 or 3; a protein having an amino acid sequence represented by SEQ ID NO: 1 or 3; and a method for producing an L--amino acid compound are provided. The method includes a step (1) of reacting the protein described herein with an -hydroxycarboxylic acid compound to obtain a corresponding -oxocarboxylic acid compound; and a step of reacting a protein having the ability to aminate an -oxocarboxylic acid compound and convert the same into a corresponding L--amino acid compound with the -oxocarboxylic acid compound obtained in step (1) to obtain a corresponding L--amino acid compound.

Methods and systems for the production of alcohols are described. A two stage process is utilized, where fermentation in a first stage produces an intermediate product, such as an amino acid or organic acid, from a carbon containing feedstock. A second stage produces alcohol by fermentation of this intermediate product.

The application provides an enzyme immobilization carrier and a preparation method thereof, an immobilized enzyme and a preparation method thereof. The above enzyme immobilization carrier is obtained by an amino modification or a cyanuric chloride modification of super-crosslinked polyvinyl alcohol. The use of the enzyme immobilization carrier provided by the application may effectively improve the stability and reusability of the immobilized enzyme. Moreover, due to the use of the form of enzyme covalent linkage, compared with an embedding method, the preparation method is no need for chemical reagent immersion and the like, it is beneficial to maintain the own activity of the enzyme, and promote the immobilized enzyme to have the better activity while the stability and reusability are kept.

The present disclosure relates to the use of an amino acid dehydrogenase in combination with a cofactor regenerating system comprising a ketoreductase. In particular embodiments, the process can be used to prepare L-tert-leucine using a leucine dehydrogenase.

Methods and systems for the production of alcohols are described. A two stage process is utilized, where fermentation in a first stage produces an intermediate product, such as an amino acid or organic acid, from a carbon containing feedstock. A second stage produces alcohol by fermentation of this intermediate product.

Disclosed herein is a process for preparing enantioenriched (S)-2-aminonon-8-enoic acid by amination of 2-oxonon-8-enoic acid in the presence of an enzyme and an ammonia source.

Disclosed are, among other things, variant polypeptides, nucleic acids encoding the polypeptides, production of the variant polypeptides, and use of the variant polypeptides in various applications, such as screening and synthetic methods. For example, the variant polypeptides, or enzymatically-active fragments thereof, are useful for converting aliphatic keto acids to aliphatic alpha amino acids.