Provided herein are biocatalytic methods of producing terpene compounds by applying a novel type of phosphatase enzyme. The method allows the fully biochemical synthesis of terpene compounds, like for example copalol and labdendiol, and derivatives thereof, which serve as valuable intermediates for the production of perfumery ingredients, such as, for example, ambrox. Also provided are novel fully biochemical multistep processes for the production of such compounds as well as novel phosphatase enzymes and mutants and variants derived therefrom.

Recombinant microorganisms, plants, and plant cells are disclosed that have been engineered to have reduced levels or activity of one or more alcohol dehydrogenases or aldehyde reductases thereby increasing the production of benzylisoquinoline alkaloids and/or benzylisoquinoline alkaloid precursors.

Microorganisms are genetically engineered to produce 3-hydroxypropionate (3-HP). The microorganisms are carboxydotrophic acetogens. The microorganisms produce acetyl-coA using the Wood-Ljungdahl pathway for fixing CO/CO.sub.2. A β-alanine pyruvate aminotransferase from a microorganism that contains such an enzyme is introduced. Additionally, an acetyl-coA carboxylase may also be introduced. The production of 3-HP can be improved. This can be effected by improved promoters or higher copy number or enzymes that are catalytically more efficient.

Described herein are biological devices and methods for using the same to produce oxidized zinc. The biological devices include microbial cells transformed with a DNA construct containing genes for producing a zinc-related protein, an alkaline phosphatase, and an alcohol dehydrogenase. In some instances, the biological devices also include a gene for lipase. The oxidized zinc compositions produced herein have numerous applications.

Disclosed is an alcohol dehydrogenase mutant and application thereof in cofactor regeneration, and belongs to the technical fields of enzyme engineering and bioengineering. The alcohol dehydrogenase mutant is obtained by mutating valine at position 84 and/or tyrosine at position 127 in alcohol dehydrogenase having an original amino acid sequence as set forth in SEQ ID No. 1. The alcohol dehydrogenase mutant has high activity for a variety of alcohol co-substrates, and can catalyze these enzyme co-substrates for the regeneration of cofactor NADPH. Compared with the wild-type alcohol dehydrogenase KpADH, the alcohol dehydrogenase mutant has higher activity and catalytic efficiency, and for co-substrate 1,4-butanediol, its k.sub.cat value can be up to 75.9 min.sup.−1, its k.sub.cat/K.sub.m value can be up to 2009 min.sup.−1.Math.M.sup.−1, and its K.sub.m value can be as low as 11.3 mM. Therefore, the alcohol dehydrogenase mutant has a higher value in industrial application.

An engineered bacterium for producing ethanol from one or more carbohydrates is disclosed. The bacterium can be made by (a) inactivating within a Lactobacillus casei bacterium one or more endogenous genes encoding a lactate dehydrogenase; or (b) introducing into a Lactobacillus casei bacterium one or more exogenous genes encoding a pyruvate decarboxylase and one or more exogenous genes encoding an alcohol dehydrogenase II; or (c) performing both steps (a) and (b). The resulting engineered bacterium produces significantly more ethanol than the wild-type Lactobacillus casei bacterium, and can be used in producing ethanol from a substrate such as biomass that includes carbohydrates.

The present disclosure provides methods and compositions for producing artemisinic acid, dihydroartemisinic acid or artemisinin. In various aspects, the present disclosure provides enzymes, polynucleotides encoding said enzymes, and recombinant microbial host cells (or microbial host strains) for the production of artemisinic acid, dihydroartemisinic acid or artemisinin. The present disclosure further provides methods of making pharmaceutical products containing artemisinic acid, dihydroartemisinic acid or artemisinin.

The present invention provides for a polyketide synthase (PKS) capable of synthesizing a 3-hydroxycarboxylic acid or ketone. The present invention also provides for a host cell comprising the PKS and when cultured produces the 3-hydroxycarboxylic acid or ketone.

The present disclosure relates to biological processes and systems for the production of isopropanol and/or acetone utilizing modified alcohol dehydrogenases that exhibit increased activity with NADH as a cofactor. The disclosure further relates to polynucleotides and polypeptides of the modified alcohol dehydrogenases, and host cells containing the polynucleotides and expressing the polypeptides.

The present invention relates to a novel promoter for regulating ADH gene expression in an organic acid-resistant yeast, and a method of producing an organic acid by expressing an organic acid production-related gene using the same. When an organic acid production-related target gene is expressed in the organic acid-resistant yeast using the novel promoter according to the present invention, there is an advantage in that the yeast can produce the organic acid with high efficiency while having resistance to the organic acid without inhibiting the growth ability of the yeast.