The present disclosure relates to methods of using transaminase polypeptides in the synthesis of chiral amines from prochiral ketones.

A method for enzymatic preparation of fludarabine phosphate, comprising reaction of fludarabine with a high-energy phosphate compound under the action of deoxyribonucleic acid kinase. According to said method, acetate kinase and acetyl phosphate free acid or acetyl phosphate are also added. The technical problems present in the existing processes are successfully addressed by employing the enzymatic process to prepare the fludarabine phosphate. The usage of the high-energy phosphate compound is reduced by means of adding acetate kinase to recycle and regenerate a small amount of the high-energy phosphate compound, thereby reducing the generation of by-products having similar structures to the fludarabine phosphate, enhancing the operation convenience of purification steps in the industrial production of the fludarabine phosphate. The process is environment friendly, the reaction conditions are moderate, the cost is low, and the yield and the purity of the product obtained are high.

The present invention relates to a process for treating an oil comprising a chlorophyll substrate, the process comprising contacting the oil with a polypeptide having decolorase activity or a composition comprising the polypeptide, wherein the polypeptide is selected from the group consisting of: a. a polypeptide which has at least 80% identity to amino acids 1 to 318 of SEQ ID NO: 1; and, b. a polypeptide encoded by a nucleic acid sequence that has at least 80% identity to the nucleic acid sequence of SEQ ID NO: 2.

Provided is a folate producing strain and the preparation and application thereof, in particular, the expression level of the endogenous folC gene in the engineered strain of the present invention is decreased, and the exogenous folC gene is introduced, and the production capacity of the folate, the precursor, or the intermediate thereof in the engineered strain is significantly improved compared to the starting strain.

The use of a cytochrome P-450 enzyme comprising SEQ ID NO: 3, or a variant enzyme having at least 70% identity thereto and having CYP-450 activity, for the hydroxylation of an organic compound.

The present invention provides for a method of converting a depolymerized lignin aromatic compound into a bioproduct, comprising: (a) providing a composition comprising a depolymerized lignin aromatic compound, optionally a depolymerized cellulose, and optionally a depolymerized hemicellulose, and (b) introducing a genetically modified microorganism to the composition, wherein the genetically modified microorganism is capable of converting the depolymerized lignin aromatic compound into a bioproduct; such that the depolymerized lignin aromatic compound is converted into a bioproduct.

Provided herein are biocatalysts and systems thereof for pterin-dependent enzymes and pathways and methods of making and using the same.

This document describes biochemical pathways for producing pimeloyl-CoA using a polypeptide having the enzymatic activity of a hydroperoxide lyase to form non-3-enal and 9-oxononanoate from 9-hydroxyperoxyoctadec-10,12-dienoate. Non-3-enal and 9-oxononanoate can be enzymatically converted to pimeloyl-CoA or a salt thereof using one or more polypeptides having the activity of a dehydrogenase, a CoA ligase, an isomerase, a reductase, a thioesterase, a monooxygenase, a hydratase, and/or a thiolase. Pimeloyl-CoA can be enzymatically converted to pimelic acid, 7-aminoheptanoic acid, 7-hydroxyheptanoic acid, heptamethylenediamine, or 1,7-heptanediol, or corresponding salts thereof. This document also describes recombinant microorganisms producing pimeloyl-CoA, as well as pimelic acid, 7-aminoheptanoic acid, 7-hydroxyheptanoic acid, heptamethylenediamine, and 1,7-heptanediol, or corresponding salts thereof.

The present disclosure relates to polypeptides having transaminase activity, polynucleotides encoding the polypeptides, and methods of using the polypeptides.

The present disclosure provides engineered transaminase polypeptides useful for the synthesis of chiral amine compounds under industrially relevant conditions. The disclosure also provides polynucleotides encoding the engineered transaminase polypeptides, host cells capable of expressing the engineered transaminases, and methods of using the engineered transaminases for the production of chiral amine compounds.