The present disclosure provides engineered ketoreductase enzymes having improved properties as compared to a naturally occurring wild-type ketoreductase enzyme. Also provided are polynucleotides encoding the engineered ketoreductase enzymes, host cells capable of expressing the engineered ketoreductase enzymes, and methods of using the engineered ketoreductase enzymes to synthesize chiral compounds.

The present invention relates to a cytochrome P450 enzyme comprising the amino acid sequence set forth in SEQ ID NO: 3, or a variant thereof having an amino acid sequence having at least 95% identity thereto and having CYP450 activity. The cytochrome P450 enzyme provided herein was isolated from Streptomyces eurythermus NRRL 2539 and has a wide substrate range and high activity, and may be used to oxidate organic compounds.

Recombinant Sorangium cellulosum for producing de-epoxidized epothilone B by fermentation, insertional inactivation of an epoK gene in an epothilone biosynthetic gene cluster in the recombinant bacteria, and a method for producing de-epoxidized epothilone B using the recombinant bacteria.

The present invention provides a carbonyl reductase having the activity of reducing a carbonyl group-containing compound to convert the compound into an optically active compound, and a production method of an optically active compound using the enzyme. Specifically, a carbonyl reductase having one or more mutations in which the 54th aspartic acid, the 157th methionine, the 170th alanine, the 211th isoleucine, the 214th methionine, and the 249th methionine are each substituted by other specific amino acid in the amino acid sequence shown in SEQ ID NO: 1 or a homologue of the amino acid sequence, and a production method of an optically active compound using the same are provided.

The present disclosure provides engineered ketoreductase enzymes having improved properties as compared to a naturally occurring wild-type ketoreductase enzyme. Also provided are polynucleotides encoding the engineered ketoreductase enzymes, host cells capable of expressing the engineered ketoreductase enzymes, and methods of using the engineered ketoreductase enzymes to synthesize chiral compounds.

The present invention relates to a cytochrome P450 enzyme comprising the amino acid sequence set forth in SEQ ID NO: 3, or a variant thereof having an amino acid sequence having at least 95% identity thereto and having CYP450 activity. The cytochrome P450 enzyme provided herein was isolated from Streptomyces eurythermus NRRL 2539 and has a wide substrate range and high activity, and may be used to oxidate organic compounds.

The present disclosure relates to a genetically modified host cell having improved production of thiamine, wherein the host cell expresses one or more heterologous ThiO enzymes converting glycine into dehydroglycine (DHG) in the host cell and/or one or more heterologous ThiI enzymes catalyzing the transfer of sulfur from IscS to the sulfur carrier protein ThiS in the host cell, whereby the production of the thiamine in the genetically modified host cell is improved compared to an unmodified parent host cell.

Microorganisms and bioprocesses are provided that convert gaseous C1 containing substrates, such as syngas, producer gas, and renewable H.sub.2 combined with CO.sub.2, into nutritional and other useful bioproducts.

Provided is a new CueO mutant with improved activity compared with wild-type CueO. The protein according to one or more embodiments of the present invention contains an amino acid sequence [1] or [2] and has laccase activity: [1] an amino acid sequence containing at least a region of positions 29-516 in SEQ ID NO: 14 with mutations (a) and (b): (a) a substitution of D360 with an amino acid other than D; and (b) one or more selected from a substitution of G304 with an amino acid other than G, a substitution of D373 with an amino acid other than D, and a substitution of Q374 with an amino acid other than Q; or [2] an amino acid sequence 90% or more identical to the sequence [1], and having residues corresponding to positions 360, 304, 373, and 374 of SEQ ID NO: 14 identical to those of the sequence [1].