The disclosure relates to modification of a heat resistant cytoplasmic heat stable 6-phosphogluconate dehydrogenase (6PGDH) enzyme by fusing the cytoplasmic 6PGDH enzyme in frame to a plastid-targeting sequence. This modification allows the import of the cytoplasmic 6PGDH enzyme into plastids of a plant cell. Polynucleotides encoding and expressing the modified cytoplasmic 6PGDH enzymes are provided. The disclosure further provides transgenic plants and seeds containing the disclosed polynucleotides and expressing the modified cytoplasmic 6PGDH enzymes during development. The invention further relates to methods for developing a transgenic plant that has increased heat resistance and yield during heat stress.

The present disclosure relates to compositions and methods for producing stereoisomerically pure aminocyclopropanes.

The present invention relates to mutated filamentous fungal host cell producing a secreted polypeptide of interest, wherein a native putative steroid dehydrogenase is modified, truncated, partly or fully inactivated, present at reduced level or eliminated compared to a non-mutated parent cell, and wherein said native putative steroid dehydrogenase comprises at least one conserved amino acid motif selected from: YGAR and/or VPHS[W/Y]F and/or QC[A/V/S]RRL and/or LKKYTLP and/or CPHYT, and methods of producing a secreted polypeptide of interest in said cells as well as methods of producing said cells.

A non-naturally occurring microbial organism includes a microbial organism having a 1,3-butanediol (1,3-BDO) pathway having at least one exogenous nucleic acid encoding a 1,3-BDO pathway enzyme expressed in a sufficient amount to produce 1,3-BDO. The pathway includes an enzyme selected from a 2-amino-4-ketopentanoate (AKP) thiolase, an AKP dehydrogenase, a 2-amino-4-hydroxypentanoate aminotransferase, a 2-amino-4-hydroxypentanoate oxidoreductase (deaminating), a 2-oxo-4-hydroxypentanoate decarboxylase, a 3-hydroxybutyraldehyde reductase, an AKP aminotransferase, an AKP oxidoreductase (deaminating), a 2,4-dioxopentanoate decarboxylase, a 3-oxobutyraldehyde reductase (ketone reducing), a 3-oxobutyraldehyde reductase (aldehyde reducing), a 4-hydroxy-2-butanone reductase, an AKP decarboxylase, a 4-aminobutan-2-one aminotransferase, a 4-aminobutan-2-one oxidoreductase (deaminating), a 4-aminobutan-2-one ammonia-lyase, a butenone hydratase, an AKP ammonia-lyase, an acetylacrylate decarboxylase, an acetoacetyl-CoA reductase (CoA-dependent, aldehyde forming), an acetoacetyl-CoA reductase (CoA-dependent, alcohol forming), an acetoacetyl-CoA reductase (ketone reducing), a 3-hydroxybutyryl-CoA reductase (aldehyde forming), a 3-hydroxybutyryl-CoA reductase (alcohol forming), a 4-hydroxybutyryl-CoA dehydratase, and a crotonase. A method for producing 1,3-BDO, includes culturing such microbial organisms under conditions and for a sufficient period of time to produce 1,3-BDO.

The present invention relates to a process for producing a beer tittering agent via enzyme catalyzed bioconversion of hop-derived isoalpha acids to dihydro-(rho)-isoalpha acids and to the novel enzyme catalysts which may be employed in such a process.

The present invention provides, a novel method for producing a compound represented by formula (I) and a novel method for producing a compound represented by formula (B) or a salt thereof, which are intermediates in the production of formula (I).

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.

Methods for increasing carbon-based chemical product yield in an organism by perturbing redox balance in an organism as well as nonnaturally occurring organisms with perturbed redox balance and methods for their use in producing carbon-based chemical products are provided.

Provided is a ketoreductase mutant and applications thereof. Compared with an amino acid sequence shown in SEQ ID NO: 1, the amino acid sequence of the ketoreductase mutant includes at least one of the following mutation sites: L198P, S96W/I/L/V, M194L or L1526, herein “/” means “or.” The ketoreductase mutant provides high selectivity and high activity with respect to a substrate ketone, and the application of the mutant in a catalytic reduction reaction of a ketone substrate may increase the production efficiency of a chiral alcohol compound corresponding thereto.

Pantoic acid is obtained by fermenting substrate 2-hydroxy-3,3-dimethyl-4-aldehydobutyric acid by using bacteria or yeast. A microorganism is selected from bacteria or fungi. The microorganism is selected from wild or genetically engineered Escherichia coli, Bacillus, Corynebacterium, yeast or Streptomyces. Pantothenic acid is obtained by chemically reacting the pantoic acid obtained by the method described above with β-alanine. Panthenol is obtained by chemically reacting the pantoic acid obtained by the method described above with β-alaninol.