The disclosure relates to host cells having altered NADPH availability, allowing for increased production of compounds produced using NADPH, and methods of use thereof. NADPH availability is altered by one or more of: expressing an altered GAPDH, expressing a variant glutamate dehydrogenase (gdh), aspartate semialdehyde dehydrogenase (asd), dihydropicolinate reductase (dapB), and meso-diaminopimelate dehydrogenase (ddh), expressing a novel nicotinamide nucleotide transhydrogenase, expressing a novel threonine aldolase, and expressing or modulating the expression of a pyruvate carboxylase in the host cells.

The present disclosure relates to a variant polypeptide having attenuated dihydrodipicolinate reductase activity and a method of producing L-threonine using the same.

The present disclosure relates to a modified polypeptide, in which the activity of meso-diaminopimelate is weakened, and a method for producing L-threonine using the same.

The present invention relates to the provision of an enzymatic method for the preparation of 2,6-bis(hydroxymethyl) pyridine (Formula I) using as substrate 2,6-Dimethlypyridine (2,6-lutidene) and the multicomponent xylene monooxygenase comprising XylM and XylA from Pseudomonas putida (Arthrobacter siderocapsulatus). The enzymatic method of the present invention is advantageous over conventional synthetic preparations, providing access to the title compound with a one-step enzymatic procedure.

The present invention relates to a recombinant microorganism for producing formic acid, which has a formate dehydrogenase 1 alpha subunit (FDH1α)-encoding endogenous gene deleted therefrom and an FDH1-encoding exogenous gene introduced thereinto, and a method for production of formic acid by using the microorganism.

The present disclosure concerns recombinant yeast host cells having a first genetic modification for increasing formate production, when compared to a corresponding native yeast host cell as well as a source of formate dehydrogenase activity. The source of formate can be an internal source of formate dehydrogenase activity and/or the recombinant yeast host call can be supplemented by an external source of formate dehydrogenase activity.

The disclosure discloses construction and application of an engineered strain of E. coli for producing malic acid by fixing CO.sub.2, and belongs to the field of fermentation. The engineered strain is obtained by performing genetic engineering transformation on Escherichia coli MG1655; the genetic engineering transformation includes knocking out a fumarate reductase gene, a fumarase gene, a lactate dehydrogenase gene and an alcohol dehydrogenase gene and freely overexpressing a formate dehydrogenase, an acetyl coenzyme A synthetase, an acylated acetaldehyde dehydrogenase, a formaldehyde lyase, a dihydroxyacetone kinase, a malic enzyme and a phosphite oxidoreductase to obtain a strain GH0407. The strain is used for producing malic acid by fermentation, anaerobic fermentation is performed for 72 hours with CO.sub.2 and glucose as a co-substrate, the production of malic acid reaches 39 g/L, the yield is 1.53 mol/mol, and accumulation of malic acid in the original strain is not achieved.

Many biotechnologically relevant organisms cannot utilize cheap and abundant one carbon feedstocks, e.g. CO.sub.2, CO, formaldehyde, methanol, and methane, for growth and instead prefer complex feedstocks such as sugars. Disclosed herein is a system that enables organisms to consume one carbon molecules for growth and maintenance via a formyl-CoA elongation pathway. Utilization of one carbon feedstocks can replace the use of sugar as the primary means of cultivating organisms in biotechnological applications. This has the potential to be more cost effective and avoid the controversial use of food as feedstocks. Intermediates of the formyl-CoA elongation pathway may be also be converted to desired chemical products.

Disclosed is an NADH-dependent amino acid dehydrogenase and an application thereof in increasing lysine yield. The amino acid dehydrogenases are aspartate dehydrogenase derived from Pseudomonas aeruginos, aspartate semialdehyde dehydrogenase derived from Tistrella mobilis, dihydropyridine dicarboxylic acid reductase derived from Mycobacterium tuberculosis, and diaminopimelate dehydrogenase derived from Tepidanaerobacter acetatoxydans. The amino acid sequences thereof are as shown in SEQ ID NOs: 1, 3, 5, and 7, respectively. NADH or both NADH and NADPH can be used as co-factors of the amino acid dehydrogenase to synthesize lysine, thereby reducing the demand for NADPH in the cell, and significantly increasing the production of lysine or pentanediamine.

The present invention relates to an L-lysine-producing microorganism of the genus Corynebacterium and a method for producing L-lysine using the same.