Provided are a novel isoprene synthase derived from sweet potato and a method of preparing isoprene using the same, and more specifically, a novel isoprene synthase derived from sweet potato, a gene encoding the isoprene synthase, a host cell transformed with the gene, and a method of preparing isoprene using the same. The isoprene synthase of the present invention may have higher isoprene productivity as compared to isoprene synthases known in the related art to thereby be effectively used in isoprene biosynthesis and preparation of an isoprene polymer using the same.

The invention provides a polypeptide capable of using 4-hydroxy-3-methyl-but-2-enyl pyrophosphate (HMBPP) as a substrate to produce isoprene, a nucleic acid encoding the polypeptide, and a vector and a cell comprising the nucleic acid. In addition, the invention also provides a method for producing isoprene using the polypeptide, and a method for preparing the polypeptide.

An object of the present invention is to provide a series of techniques for producing 1,4-butanediol from methanol or the like. Provided is a recombinant cell prepared by introducing a gene encoding at least one enzyme selected from the group consisting of succinate semialdehyde dehydrogenase, succinyl-CoA synthase, CoA-dependent succinate semialdehyde dehydrogenase, 4-hydroxybutyrate dehydrogenase, 4-hydroxybutyryl-CoA transferase, 4-hydroxybutyryl-CoA reductase, 4-hydroxybutyraldehyde dehydrogenase, and alcohol dehydrogenase, into a host cell which is a methylotroph, wherein the gene is expressed in the host cell, and the recombinant cell is capable of producing 1,4-butanediol from at least one C1 compound selected from the group consisting of methane, methanol, methylamine, formic acid, formaldehyde, and formamide.

This application describes methods, including non-naturally occurring methods, for biosynthesizing 3-hydroxy-3-methylglutaryl-coA and intermediates thereof, as well as non-naturally occurring hosts for producing 3-hydroxy-3-methylglutaryl-coA. This application also describes methods, including non-naturally occurring methods, for biosynthesizing isoprene and intermediates thereof, as well as non-naturally occurring hosts for producing isoprene.

Systems, networks, methods, compositions and recombinant hosts for biosynthesizing hydrocarbons from a feedstock, such as gas, are provided.

Genetically engineered hosts and methods for their production and use in synthesizing hydrocarbons are provided.

Cells comprising a heterologous metabolic pathway are configured to produce a terpene product containing non-multiples of five carbon, particularly wherein the pathway comprises heterologous Lepidoptera insect juvenile hormone biosynthetic pathway enzymes of the insect's mevalonate pathway.

This application describes methods, including non-naturally occurring methods, for biosynthesizing 3-hydroxy-3-methylglutaryl-coA and intermediates thereof, as well as non-naturally occurring hosts for producing 3-hydroxy-3-methylglutaryl-coA. This application also describes methods, including non-naturally occurring methods, for biosynthesizing isoprene and intermediates thereof, as well as non-naturally occurring hosts for producing isoprene.

A recombinant cell having a function of synthesizing acetyl-CoA from methyltetrahydrofolate, carbon monoxide, and CoA, including: a gene that expresses an exogenous NAD(P)H consumption pathway, the gene being expressed in the recombinant cell, wherein expression in at least one of endogenous NAD(P)H consumption pathways of the recombinant cell is down-regulated, and the endogenous NAD(P)H consumption pathway is different from the exogenous NAD(P)H consumption pathway, and the recombinant cell produces an organic compound having 4 or more carbon atoms from at least one selected from the group consisting of carbon monoxide and carbon dioxide via the exogenous NAD(P)H consumption pathway.

The invention provides for methods for the production of mevalonate, isoprene, isoprenoid precursor molecules, and/or isoprenoids in cells via the heterologous expression of phosphoketolase enzymes.