The present invention provides engineered proline hydroxylase polypeptides for the production of hydroxylated compounds, polynucleotides encoding the engineered proline hydroxylases, host cells capable of expressing the engineered proline hydroxylases, and methods of using the engineered proline hydroxylases to prepare compounds useful in the production of active pharmaceutical agents.

The present disclosure provides engineered proline hydroxylase polypeptides for the production of hydroxylated compounds, polynucleotides encoding the engineered proline hydroxylases, host cells capable of expressing the engineered proline hydroxylases, and methods of using the engineered proline hydroxylases to prepare compounds useful in the production of active pharmaceutical agents.

The present disclosure provides engineered proline hydroxylase polypeptides for the production of hydroxylated compounds, polynucleotides encoding the engineered proline hydroxylases, host cells capable of expressing the engineered proline hydroxylases, and methods of using the engineered proline hydroxylases to prepare compounds useful in the production of active pharmaceutical agents.

The present invention provides engineered proline hydroxylase polypeptides for the production of hydroxylated compounds, polynucleotides encoding the engineered proline hydroxylases, host cells capable of expressing the engineered proline hydroxylases, and methods of using the engineered proline hydroxylases to prepare compounds useful in the production of active pharmaceutical agents.

Disclosed herein include methods and compositions for making proteins in peroxisomes as well as methods of making cells for producing proteins in peroxisomes. Also disclosed herein are cells for producing a protein in a peroxisome, and methods for producing a protein in a eukaryotic cell containing a peroxisome as described herein.

The present invention provides engineered proline hydroxylase polypeptides for the production of hydroxylated compounds, polynucleotides encoding the engineered proline hydroxylases, host cells capable of expressing the engineered proline hydroxylases, and methods of using the engineered proline hydroxylases to prepare compounds useful in the production of active pharmaceutical agents.

The disclosure herein provides a monomeric prolyl 4-hydroxylase. A microorganism including a monomeric prolyl 4-hydroxylase is provided. The disclosure provides a microorganism including a monomeric prolyl 4-hydroxylase; and another protein to be hydroxylated. A method for providing skincare benefits including applying the fusion protein of the present disclosure on skin is also taught.

The present invention relates to a pharmaceutical composition for preventing and treating cancer or inflammatory disease, containing an NDRG3 expression or activity inhibitor as an active ingredient. Furthermore, the present invention relates to an NDRG3 protein-specific antibody and a use thereof. Specifically, the antibody to the NDRG3 protein is prepared, and the antibody is used to verify that NDRG3 mediated by lactate generated from a hypoxia reaction promotes cell proliferation, angiogenesis, and cytokine expression through the lactate-NDRG3-c-Raf-ERK signaling pathway, and thus the antibody binding to the epitope of the NDRG3 or a fragment of the antibody can be favorably used in the research of cancer or inflammation occurrence mechanism, the development of novel genes involved in the mechanism, and the development of therapeutic agents and new pharmaceuticals.

A method of producing collagen in a plant and plants producing collagen are provided. The method is effected by expressing in the plant at least one type of a collagen alpha chain in a manner enabling accumulation of the collagen alpha chain in a subcellular compartment devoid of endogenous P4H activity, thereby producing the collagen in the plant.

Light-generating fusion proteins having a ligand binding site and a light-generating polypeptide moiety and their use as diagnostics, in drug screening and discovery, and as therapeutics, are disclosed. The light-generating fusion protein has a feature where the bioluminescence of the polypeptide moiety changes upon binding of a ligand at the ligand binding site. The ligand may be, for example, an enzyme present in an environment only under certain conditions, e.g., ubiquitin ligase in a hypoxic state, such that the light-generating fusion protein is “turned on” only under such conditions.