C12Y401/01086

Recombinant microorganism producing 1,3-diaminopropane and method for producing 1,3-diaminopropane using the same

The present disclosure relates to a recombinant microorganism producing 1,3-diaminopropane, and a method for producing 1,3-diaminopropane using the same, and specifically, to a recombinant microorganism producing 1,3-diaminopropane into which genes encoding an enzyme involved in a metabolic pathway of 1,3-diaminopropane, dat and ddc, are introduced, and a method for producing 1,3-diaminopropane using the same. When the recombinant microorganism producing the 1,3-diaminopropane according to the present disclosure is used, 1,3-diaminopropane may be mass-produced to be industrially useful in various fields such as pharmaceutical products, agricultural products, fibers for clothing, etc.

RECOMBINANT MICROORGANISM PRODUCING 1,3-DIAMINOPROPANE AND METHOD FOR PRODUCING 1,3-DIAMINOPROPANE USING THE SAME
20170114345 · 2017-04-27 ·

The present disclosure relates to a recombinant microorganism producing 1,3-diaminopropane, and a method for producing 1,3-diaminopropane using the same, and specifically, to a recombinant microorganism producing 1,3-diaminopropane into which genes encoding an enzyme involved in a metabolic pathway of 1,3-diaminopropane, dat and ddc, are introduced, and a method for producing 1,3-diaminopropane using the same.

When the recombinant microorganism producing the 1,3-diaminopropane according to the present disclosure is used, 1,3-diaminopropane may be mass-produced to be industrially useful in various fields such as pharmaceutical products, agricultural products, fibers for clothing, etc.

Multi-Mechanistic Channeling Within a Biocatalytic Cascade for the Production of 1,3-Diaminopropane

Described herein is a one-pot, four-enzyme cascade of enzymes, three bound to quantum dots with one enzyme free in solution, for the conversion in vitro of fumarate to 1,3-diaminopropane. The cascade operates via two distinctly different enzymatic channeling mechanisms which simultaneously function to increase the overall rate. The first three enzymes of the pathway (AspB->LysC->Asd) were able to engage in channeling in a nanoparticle displayed format, but addition of the last two enzymes to this pathway in this format (AspB->LysC->Asd->Dat->Ddc) did not result in complete channeling through the entire pathway to the final diaminopropane product. Surprisingly, replacement of the last two enzymes (Dat->Ddc) with a naturally occurring fused Dat-Ddc hybrid (Daba) provided for full channeling in this system (AspB->LysC->Asd->Daba).