The present disclosure relates to an ATP phosphoribosyltransferase (HisG) protein and a method for producing histidine using the same.

The present disclosure relates to a microorganism having increased glycine productivity and a method for producing a fermented composition using the microorganism, and more specifically, to a microorganism of the genus Corynebacterium having increased glycine productivity due to the introduction of a mutation in HisG, a method for preparing a fermented composition comprising glycine and glutamic acid using the microorganism of the genus Corynebacterium, and the fermented composition.

The present disclosure relates to a novel promoter and a method for producing L-amino acids using the promoter, and more specifically, to a novel polynucleotide having promoter activity, a vector and a microorganism of the genus Corynebacterium comprising the polynucleotide, a method for producing L-amino acids and a fermented composition using the microorganism, and a fermented composition.

The present invention relates to an E. coli hisG-derived ATP-phosphoribosyltransferase variant having a reduced feedback inhibition by histidine and a strain expressing the same. The variant may maintain its activity even at a high histidine concentration, thus increasing histidine production.

The present invention relates to an E. coli hisG-derived ATP-phosphoribosyltransferase variant having a reduced feedback inhibition by histidine and a strain expressing the same. The variant may maintain its activity even at a high histidine concentration, thus increasing histidine production.

The present invention relates to an E. coli hisG-derived ATP-phosphoribosyltransferase variant having a reduced feedback inhibition by histidine and a strain expressing the same. The variant may maintain its activity even at a high histidine concentration, thus increasing histidine production.

The present invention relates to an E. coli hisG-derived ATP-phosphoribosyltransferase variant having a reduced feedback inhibition by histidine and a strain expressing the same. The variant may maintain its activity even at a high histidine concentration, thus increasing histidine production.

The present disclosure describes the engineering of microbial cells for fermentative production of histamine and provides novel engineered microbial cells and cultures, as well as related histamine production methods.

Isolated mogroside and mogrol biosynthetic pathway enzyme polypeptides useful in mogroside biosynthesis are provided. Mogroside biosynthetic pathway enzymes of the invention include squalene epoxidase (SE), epoxy hydratase (EH), cytochrome p450 (Cyp), cucurbitadienol synthase (CDS) and udp-glucosyl-transferase (UGT), Also provided are methods of producing a mogroside using the isolated mogroside and mogrol biosynthetic enzyme polypeptides, the methods comprising contacting a mogrol and/or a glycosylated mogrol (mogroside) with at least one UDP glucose glucosyl transferase (UGT) enzyme polypeptide of the invention catalyzing glucosylation of the mogrol and/or the glucosylated mogrol to produce a mogroside with an additional glucosyl moietie(s), thereby producing the mogroside. Alternatively or additionally provided is a method of synthesizing a mogrol, the method comprising contacting a mogrol precursor substrate with one or more mogrol biosynthetic pathway enzyme polypeptides as described herein catalyzing mogrol synthesis from the mogrol precursor substrate, thereby synthesizing the mogrol.

Provided is a recombinant microorganism for producing carnosine, histidine and beta-alanine and a method for producing carnosine, histidine and beta-alanine by using same and, more particularly, to: a recombinant microorganism for high production of carnosine, histidine and beta-alanine produced through the redesign of metabolic pathways; a method for producing same; and a method for producing carnosine, histidine and beta-alanine by using same. According to the present invention, in a microorganism capable of producing histidine and beta-alanine, by enhancing the pentose phosphate pathways through the replacement of a pentose phosphate pathway-related operon gene with a highly expressing synthetic promoter and the replacement of a pgi gene with an initiation codon, and inducing enhancement of the production of histidine and beta-alanine through the overexpression of genes on histidine and beta-alanine metabolic pathways, respectively, it is possible to develop a recombinant microorganism for high production of histidine and beta-alanine.