A microorganism is transformed to be capable of producing guanidinoacetic acid (GAA). A method can be used for the fermentative production of GAA using such a microorganism. A corresponding method can be used for the fermentative production of creatine.

Pharmaceuticals for treating patient with excessive lactate production and related acidemia are disclosed. Pharmaceuticals include glutamate, aspartate, BCAA, pyruvate, malate, oxaloacetate, α-ketoglutarate, AST, ALT, PLP, MDH and GPDH, Lodoxamite and Oxamate. The mechanism is that invented pharmaceuticals inhibit LDH and enhance malate/aspartate shuttle activity.

This disclosure relates to strategies for in vivo production of certain carbon-based products, for example, aminated aliphatic compounds having a carbon chain length of C5-C19.

A microorganism is transformed to be capable of producing guanidinoacetic acid (GAA). A method can be used for the fermentative production of GAA using such a microorganism. A corresponding method can be used for the fermentative production of creatine.

The present invention relates to a method for producing a medium chain diamine and, more specifically, to a method for producing a medium chain diamine from an alcohol or alkane derived from a fatty acid, by culturing a recombinant microorganism from which a fatty aldehyde dehydrogenase gene in a ω-oxidative metabolic pathway and a β-oxidative metabolic pathway related gene have been deleted, and also into which a ω-transaminase gene has been introduced. The recombinant microorganism disclosed in the present invention can prevent the additional oxidation and β-oxidation metabolism of fatty aldehyde and can produce a medium chain diamine with a high yield by introducing an amine group to the terminus thereof.

Disclosed herein are genetically engineered hematopoietic cells, which express one or more Krebs cycle modulating polypeptides, and optionally a chimeric receptor polypeptide (e.g., an antibody-coupled T cell receptor (ACTR) polypeptide or a chimeric antigen receptor (CAR) polypeptide) capable of binding to a target antigen of interest. Also disclosed herein are uses of the engineered hematopoietic cells for inhibiting cells expressing a target antigen in a subject in need thereof.

Provided herein are compositions, systems, and methods for assessing and monitory disease stage and phases, predicting likelihood of disease progression, and predicting and monitoring responses to disease therapies (e.g., in HBV infection).

This document describes biochemical pathways for biosynthesizing a 3-oxo-7-hydroxyheptanoyl-CoA intermediate using a -ketothiolase, and enzymatically converting 3-oxo-7-hydroxyheptanoyl-CoA to 7-hydroxyheptanoic acid. 7-hydroxyheptanoic acid can be further enzymatically converted to pimelic acid, 7-aminoheptanoic acid, heptamethylenediamine or 1,7-heptanediol. This document also describes recombinant hosts producing 7-hydroxyheptanoic acid as well as pimelic acid, 7-aminoheptanoic acid, heptamethylenediamine and 1,7-heptanediol.

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.

This document describes biochemical pathways for biosynthesizing a 3-oxo-7-hydroxyheptanoyl-CoA intermediate using a -ketothiolase, and enzymatically converting 3-oxo-7-hydroxyheptanoyl-CoA to 7-hydroxyheptanoic acid. 7-hydroxyheptanoic acid can be further enzymatically converted to pimelic acid, 7-aminoheptanoic acid, heptamethylenediamine or 1,7-heptanediol. This document also describes recombinant hosts producing 7-hydroxyheptanoic acid as well as pimelic acid, 7-aminoheptanoic acid, heptamethylenediamine and 1,7-heptanediol.