An enzyme for reducing cystine to cysteine is a fusion protein that includes the protein activities of thioredoxin (protein i) having KEGG database number EC 1.8.4.8 or EC 1.8.4.10 and thioredoxin reductase (protein ii) having KEGG database number EC 1.8.1.9. The thioredoxin (protein i) is the protein activity of thioredoxin 1 from E. coli and the thioredoxin reductase (protein ii) is the protein activity of the thioredoxin reductase from E. coli. The activity of the fusion protein is at least 100% of the activity of a mixture of the same but unfused individual proteins i and ii. The fusion protein has the enzyme activity to reduce cystine to cysteine. The coding sequences (cds) responsible for the activity of protein i and ii has been fused.

In order to produce chondroitin sulfate in an animal-free manner, engineered E. coli host cells were modified so as to reduce expression of an endogenous gene for fructosyltransferase (kfoE); reduce expression of an endogenous gene for 3′-phosphoadenosine-5′-phosphosulfate reductase (cysH); and express one or more exogenous sulfotransferases. Expression of proteins forming ATP-binding cassette transporters were also reduced to limit export of glycosaminoglycans from the cells. The recombinant microorganisms are able produce all three components identified for chondroitin sulfate production—chondroitin, sulfate donor, and sulfotransferase. These modified E. coli are capable of complete, essentially one-step biosynthesis of chondroitin sulfate at a variety of sulfation levels from simple microbial media components and glucose. This is a major advantage over current production methods that depend on the natural distribution of chondroitin sulfate types in the animal tissue.

The present disclosure describes the engineering of microbial cells for fermentative production of cystathionine and provides novel engineered microbial cells and cultures, as well as related cystathionine production methods. An engineered microbial cell that expresses a heterologous cystathionine beta-synthase or a heterologous cystathionine gamma-synthase, wherein the engineered microbial cell produces cystathionine.

The present disclosure describes the engineering of microbial cells for fermentative production of L-homocysteine and provides novel engineered microbial cells and cultures, as well as related L-homocysteine production methods.

The incidence of high blood pressure is strikingly high with advancing age, and is an independent prognostic factor for the onset or progression of a variety of cardiovascular disorders (CVD). There is a critical need for a curative therapy against age-related hypertension. Overexpression of human thioredoxin (Trx) a redox protein in mice prevented age-related hypertension. Chronic injection of recombinant human Trx (rhTrx) for 3-consecutive days reversed hypertension in aged wildtype mice that lasted for at least 20 days. Arteries of wildtype mice so injected or mice with Trx overexpression exhibited decreased arterial stiffness, greater endothelium-dependent relaxations, increased nitric oxide (NO) production and decreased superoxide anion (O.sub.2..sup.) generation compared to appropriate controls. Collectively, a translational role of rhTrx in reversing age-related hypertension with long lasting efficacy is disclosed. Compositions and methods the treatment of cardiovascular disorders (CVD), primarily hypertension, comprise a therapeutically effective amount of thioredoxin-1 (Trx1 polypeptide, a pharmaceutically active Trx1 peptide fragment, or a functional derivative of Trx1 polypeptide or peptide, in a pharmaceutical carrier to ameliorate one or more symptom of the CVD.