Methods and compositions relating to the engineering of an improved protein with methionine-γ-lyase enzyme activity are described. For example, in certain aspects there may be disclosed a modified cystathionine-γ-lyase (CGL) comprising one or more amino acid substitutions and capable of degrading methionine. Furthermore, certain aspects of the invention provide compositions and methods for the treatment of cancer with methionine depletion using the disclosed proteins or nucleic acids.

Methods for evolving cells or strains towards improved methyltransferase activity, particularly SAM-dependent methyltransferase activity, as well as to cells and strains useful in such methods and methods of using the evolved cells in the production of methylated products.

Methods for evolving cells or strains towards improved methyltransferase activity, particularly SAM-dependent methyltransferase activity, as well as to cells and strains useful in such methods and methods of using the evolved cells in the production of methylated products.

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.

Novel semiconductor nanoparticles and methods of biosynthesizing the same are provided by biosynthetic processes using cell-free supernatants and isolated enzymes.

A method of treating or preventing methamphetamine related endothelial dysfunction in a patient comprising administering to the patient an effective dose of a pharmacologic composition; the composition comprising a therapeutic, the therapeutic including a hydrogen sulfide (H.sub.2S) donor, or a salt, solvate, ester, amide, clathrate, stereoisomer, enantiomer, prodrug or analogs thereof. The H.sub.2S donor may be one of sodium sulfide, diallyl trisulfide, dially disulfide, acillin, sugammadex, sulfanilamide, disulfram, sulfonamide, sulfinates, sulfoxides, persulfides, polysulfides, and sulfones. The H.sub.2S donor may be sugammadex. The H.sub.2S donor may be administered in a dosage of between 0.5 mg/kg and 10.0 mg/kg.

Methods and compositions related to the engineering of a protein with L-cyst(e)ine degrading enzyme activity are described. For example, in certain aspects there may be disclosed a modified cystathionine-γ-lyase comprising one or more amino acid substitutions and capable of degrading L-cyst(e)ine. Furthermore, certain aspects of the invention provide compositions and methods for the treatment of cancer with L-cyst(e)ine using the disclosed proteins or nucleic acids.

Methods and compositions relating to the engineering of an improved protein with homocyst(e)inase enzyme activity are described. For example, there are disclosed modified cystathionine-γ-lyase (CGL) enzymes comprising one or more amino acid substitutions and capable of degrading homocyst(e)ine. Furthermore, provided are compositions and methods for the treatment of homocystinuria or hyperhomocysteinemia with homocyst(e)ine depletion using the disclosed enzymes or nucleic acids.

Methods and compositions related to the engineering of a protein with L-cyst(e)ine degrading enzyme activity are described. For example, disclosed are modified cystathionine-γ-lyases comprising one or more amino acid substitutions and capable of degrading L-cyst(e)ine. Furthermore, compositions and methods are provided for the treatment of cystinuria using the disclosed modified enzymes or nucleic acids encoding said enzymes.

The presently disclosed invention relates to a method of diagnosing Multiple Sclerosis (MS) in a patient comprising obtaining a sample from the patient, determining a level of one or more H2S generating enzymes in the sample from the patient, and diagnosing the patient with MS when the level of the one or more H2S generating enzymes is one of at least 15% higher or lower than a control level for the one or more H2S generating enzymes, and at least 10% higher or lower than a control level for the one or more H2S generating enzymes.