The present disclosure is directed to the biosynthetic pathway for a nonribosomal peptide synthetase (NRPS) derived drug and analogs thereof. The invention provides polynucleotide sequences useful for heterologous expression in a convenient microbial host for the synthesis of the NRPS-derived drug, the polypeptides encoded by such polynucleotides, expression vectors comprising the polynucleotides, host cells comprising the polynucleotides or expression vectors, and kits comprising a host cell. Also provided is a method for the production of ET-743, the NRPS-derived drug.

The present invention generally relates to photocatalytic systems comprising graphene and associated methods. Some embodiments are directed to systems comprising one or more layers of graphene having a first surface and a second, opposed surface. A light-absorbing complex may be associated with the first surface of the one or more graphene layers, and an electron donor complex may be associated with the light-absorbing complex. A catalytic complex may be associated with the first surface or the second surface of the one or more graphene layers. For example, the catalytic complex may catalyze the formation of hydrogen gas, NADH, and/or NADPH.

The present invention relates to a composition for preparing retinoid, and more specifically, the composition comprises: a NADH or NADPH, a Beta-Carotene Oxygenase and a flavodoxin or a ferredoxin or a reductase of flavodoxin or ferredoxin; or a microorganism expressing them; or a culture or pulverized product of the microorganism, and thus can expand the supply metabolism of reducing electrons to enhance retinoid productivity through an increase in the activity of the cytochrome P450 system and provide a foundation for the low-cost production of raw materials, and thereby enhance the economic feasibility and efficiency of retinoid production.

The present invention is related to recombinant host cells comprising: (i) at least one deletion, mutation, and/or substitution in an endogenous gene encoding a polypeptide that converts pyruvate to acetaldehyde, acetyl-phosphate, or acetyl-CoA; and (ii) a heterologous polynucleotide encoding a polypeptide having phosphoketolase activity. The present invention is also related to recombinant host cells further comprising (iii) a heterologous polynucleotide encoding a polypeptide having phosphotransacetylase activity.

The present disclosure provides, among other features, an enzyme electrode in which an enzyme is immobilized via more appropriate bonds. An enzyme electrode according to the present disclosure includes an electrode and a modified protein having an amino acid sequence obtained by substituting at least one lysine residue in a protein that is a reductase or a dehydrogenase with a non-lysine amino acid residue, in which the modified protein is immobilized on a surface of the electrode.

Compositions, methods, and systems for modifying sterol metabolism in a subject is disclosed. In some embodiments, the subjects may be administered one or more mammalian cells modified to express at least one sterol degrading enzyme derived from a bacterium. In many embodiments, the cell is a macrophage or monocyte stably expressing three or more enzymes that aid in opening the ring of cholesterol. The disclosed compositions and methods may be useful in lowering cholesterol levels in a subject in need thereof. In some embodiments, the subject may have a genetic predisposition to atherosclerosis.

Disclosed herein are compositions, constructs, cassettes, vectors, cells, nucleic acids, peptides, proteins, protocols and methods for reducing cholesterol and lipid buildup in mammalian subjects, via gene and/or cell therapeutic treatments. In many embodiments, the disclosed compositions, cells, constructs, cassettes, vectors, nucleic acids, peptides, proteins, protocols and methods may help to reduce lipid levels in mammals. In one embodiment, the disclosed compositions, cells, constructs, cassettes, vectors, nucleic acids, peptides, proteins, protocols and methods are useful in reducing lipid build-up, especially cholesterol, in liver cells.