A Escherichia coli strain for producing 5-aminolevulinic which has double pdxY genes is provided. A method of producing 5-aminolevulinic acid is provided, the method comprises providing the above Escherichia coli; and inoculating the above Escherichia coli into liquid modified M9 medium containing carbon source, IPTG, glycine, succinic acid and pyridoxal to cultivate the above Escherichia coli thereby producing 5-amino-levulinic. By the above Escherichia coli and the method of producing 5-aminolevulinic acid, the strain with high growth rate and 5-aminolevulinic productivity and the mothed of quickly producing 5-aminolevulinic acid with high 5-aminolevulinic productivity are provided.

The present disclosure provides methods for preparing β-substituted tryptophan compounds. The methods include: combining i) an unsubstituted indole or a substituted indole, ii) a β-substituted serine, and iii) a tryptophan synthase β-subunit (i.e., a TrpB); and maintaining the resulting mixture under conditions sufficient to form the β-substituted tryptophan. The TrpB contains at least one amino acid mutation which promotes formation of an amino-acrylate intermediate. New TrpB variants and new β-substituted tryptophan analogs are also described.

Described herein is a method for preparing an amino salt compound, the method including: i) providing a carbonyl compound; ii) reacting the carbonyl compound provided according to (i) in the presence of a transaminase with ii-a) at least one primary amine; and ii-b) at least one carboxylic acid; thereby obtaining a mixture including an at least partially crystallized amino salt compound including a cation and a carboxylate anion based on the at least one carboxylic acid added according to (ii-b). Also described herein is an amino salt compound obtained or obtainable by the method and to the amino salt compound, and a composition including a) an amine of general formula (IIa); and b) at least one carboxylic acid of general formula (III).

Disclosed are transaminase (TA) enzymes and nucleic acids encoding them. In some cases, the transaminase enzymes are non-natural, engineered transaminases. Also disclosed are biosynthetic methods and engineered microorganisms that enhance or improve the biosynthesis of 6-aminocaproate, hexamethylenediamine, caproic acid, caprolactone, or caprolactam. The engineered microorganisms include exogenous TA and in some cases engineered TA.

Provided herein is a method for producing a protein hydrolysate using a polypeptide having endopeptidase activity and a polypeptide having carboxypeptidase activity and the use of these enzymes for hydrolysing a protein substrate. Also provided are polypeptides having carboxypeptidase activity and polynucleotides encoding the polypeptides, nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using the polypeptides.

This document describes biochemical pathways for producing pimelic acid, 7-hydroxyheptanoic acid, 7-aminoheptanoic acid, heptamethylenediamine or 1,7-heptanediol by forming two terminal functional groups, comprised of carboxyl, amine or hydroxyl group, in a C7 aliphatic backbone substrate. These pathways, metabolic engineering and cultivation strategies described herein rely on the CoA-dependent elongation enzymes or analog enzymes associated with the carbon storage pathways from polyhydroxyalkanoate accumulating bacteria.

This invention relates to methods of producing a rare amino acid- or non-natural amino acid-containing protein in a cell free protein synthesis system and kits for use in and for accomplishing same. Specifically, the methods comprise the steps of expressing at least one orthogonal suppressor tRNA (o-tRNA)/aminoacyl-tRNA synthetase (aaRS) pair or derivatives thereof specific for incorporation of a rare amino acid- or non-natural amino acid in an E. coli organism; preparing a lysate of said E. coli organism expressing said orthogonal suppressor tRNA (o-tRNA)/aminoacyl-tRNA synthetase (aaRS) pair; and contacting said lysate with a template DNA containing a mutant gene in which at least one amino acid codon at a given site of the protein-encoding gene has been mutated into an amber or ochre mutation and further providing a cognate rare amino acid or non-natural amino acid and other factors necessary for protein synthesis; wherein protein synthesis occurs following said contact to produce a protein containing said at least one rare amino acid or said non-natural amino acid. Kits for use are described, as well.

The present invention relates to a mutant microorganism having the ability to produce 5-aminolevulinic acid, and more particularly, to a mutant microorganism having the ability to produce 5-aminolevulinic acid wherein a glutamyl-tRNA reductase-encoding gene is introduced in a glutamic acid-producing microorganism, and to a method for producing 5-aminolevulinic acid using the same. According to the present invention, 5-aminolevulinic acid that is useful in the medical or agricultural field can be produced in a significantly higher yield than that of conventional production methods.

The invention relates to methods for enriching monomer content in a cycloalkane oxidation process mixed organic waste stream. In particular, the methods involve combining a biocatalyst with a mixed organic waste stream from a cycloalkane oxidation process, and enzymatically converting dimeric and/or oligomeric components of said waste stream into monomeric components. The methods may enrich the content of diacids, adipic acid, and/or other α,ω-difunctional C6 alkanes in the mixed organic waste stream. Additionally, the treated mixed organic waste streams may have improved burning efficiency.

This document describes biochemical pathways for producing 2-aminopimelate from 2,6-diaminopimelate, and methods for converting 2-aminopimelate to one or more of adipic acid, adipate semialdehyde, caprolactam, 6-aminohexanoic acid, 6-hexanoic acid, hexamethylenediamine, or 1,6-hexanediol by decarboxylating 2-aminopimelate into a six carbon chain aliphatic backbone and enzymatically forming one or two terminal functional groups, comprised of carboxyl, amine or hydroxyl group, in the backbone.