A third glucose uptake bypass in Corynebacterium glutamicum ATCC 31833

Ikeda, Masato; Noguchi, Norio; Ohshita, Masakazu; Senoo, Akihiro; Mitsuhashi, Satoshi; Takeno, Sachio

doi:10.1007/s00253-014-6323-1

Cited by 13 publications

(6 citation statements)

References 36 publications

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“…The carbon source plays an important role in amino acid synthesis . In the present study, in order to free up more carbon for l ‐serine production, the central metabolic pathway of C. glutamicum was redesigned by engineering the glucose uptake systems and the upper glycolytic pathway, achieving l ‐serine yield of 0.30 g g −1 glucose, which was the highest yield in C. glutamicum using glucose as a sole carbon source.…”

Section: Discussionmentioning

confidence: 99%

“…However, lower l ‐serine production (21.17 g L −1 ) and yield (≈0.21 g g −1 glucose) were obtained when glucose was applied as a sole carbon source . Although C. glutamicum could grow in a wide variety of carbon sources, glucose stemmed from starch hydrolysates was the optimal carbon source for amino acid production . Therefore, improving the yield of l ‐serine from glucose in C. glutamicum was important for industrial production of l ‐serine.…”

Section: Introductionmentioning

confidence: 99%

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Rewiring the Central Metabolic Pathway for High‐Yield l‐Serine Production in Corynebacterium glutamicum by Using Glucose

Zhang

Lai

et al. 2019

Biotechnology Journal

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L-Serine is widely used in the pharmaceutical, food, and cosmetic industries. The direct fermentative production of L-serine from glucose in Corynebacterium glutamicum (C. glutamicum) has been achieved but the yield is generally low. In this study, the central metabolic pathway is rewired to direct higher accumulation of glycerate-3-phosphate (3-PG), the precursor for L-serine biosynthesis, thereby freeing up more carbon to enhance L-serine production and yield. To this end, the native phosphotransferase system (PTS) is inactivated by deleting the gene ptsH. Meanwhile, the PTS-independent glucose uptake pathway is activated via overexpression of iolT1, ppgk, and deletion of the transcriptional regulator gene iolR. Furthermore, metabolic changes between PTS and non-PTS strains are elucidated using gas chromatography-tandem mass spectrometry. Based on the metabonomic and enzyme activities analysis, the glycolysis pathway upstream of 3-PG is further enhanced by co-overexpressing pgi, pfkA, and gapA. The resulting strain with all of the modifications mentioned above leads to the L-serine yield of 0.30 g g −1 glucose (42.8% higher than that of the original strain), which is the highest yield in C. glutamicum by using glucose as the sole carbon source. These strategies can be expanded for the production of other value-added chemicals derived from the intermediates of glycolysis pathway in C. glutamicum.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Rewiring the Central Metabolic Pathway for High‐Yield l‐Serine Production in Corynebacterium glutamicum by Using Glucose

Zhang

Lai

et al. 2019

Biotechnology Journal

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“…Potential of alternative glucose permeases to substitute for the glucose PTS C. glutamicum not only takes up and phosphorylates glucose mainly via the high-affinity (Km of 14 μM) phosphotransferase system (PTS) but also can use inositol permeases IolT1 and IolT2, which have about hundred fold lower affinities for glucose and require subsequent phosphorylation by glucokinases (Lindner et al 2011;Ikeda et al 2015). The latter systems may be important at the high glucose concentrations employed in industrial fermentations.…”

Section: Resultsmentioning

confidence: 99%

Engineering Corynebacterium glutamicum for fast production of l-lysine and l-pipecolic acid

Pérez-García

Peters‐Wendisch

Wendisch

2016

Appl Microbiol Biotechnol

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The Gram-positive Corynebacterium glutamicum is widely used for fermentative production of amino acids. The world production of L-lysine has surpassed 2 million tons per year. Glucose uptake and phosphorylation by C. glutamicum mainly occur by the phosphotransferase system (PTS) and to lesser extent by inositol permeases and glucokinases. Heterologous expression of the genes for the high-affinity glucose permease from Streptomyces coelicolor and Bacillus subtilis glucokinase fully compensated for the absence of the PTS in Δhpr strains. Growth of PTS-positive strains with glucose was accelerated when the endogenous inositol permease IolT2 and glucokinase from B. subtilis were overproduced with balanced translation initiation rates using plasmid pEKEx3-IolTBest. When the genome-reduced C. glutamicum strain GRLys1 carrying additional in-frame deletions of sugR and ldhA to derepress glycolytic and PTS genes and to circumvent formation of L-lactate as by-product was transformed with this plasmid or with pVWEx1-IolTBest, 18 to 20 % higher volumetric productivities and 70 to 72 % higher specific productivities as compared to the parental strain resulted. The non-proteinogenic amino acid L-pipecolic acid (L-PA), a precursor of immunosuppressants, peptide antibiotics, or piperidine alkaloids, can be derived from L-lysine. To enable production of L-PA by the constructed L-lysine-producing strain, the L-lysine 6-dehydrogenase gene lysDH from Silicibacter pomeroyi and the endogenous pyrroline 5-carboxylate reductase gene proC were overexpressed as synthetic operon. This enabled C. glutamicum to produce L-PA with a yield of 0.09 ± 0.01 g g(-1) and a volumetric productivity of 0.04 ± 0.01 g L(-1) h(-1).To the best of our knowledge, this is the first fermentative process for the production of L-PA from glucose.

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“…Recently, the genome of C. glutamicum ATCC13869 was sequenced ; it shows 87.4% symmetrical identity to the genome of C. glutamicum ATCC13032 . Based on Blast search, the protein encoded by BBD29_RS14045 in C. glutamicum ATCC13869 is the homologue (99.48% similarity) of Pks13 encoded by the gene Cgl2871 in C. glutamicum ATCC13032.…”

Section: Resultsmentioning

confidence: 99%

Impact of mycolic acid deficiency on cells of Corynebacterium glutamicum ATCC13869

Gao

Wang

et al. 2017

Biotech and App Biochem

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Mycolic acid (MA) plays important role in Corynebacterium glutamicum, but the key enzymes in the biosynthetic pathway of MA in C. glutamicum ATCC13869 have not been characterized. Since the locus BBD29_RS14045 in C. glutamicum ATCC13869 shows high similarity to the gene Cgl2871, which encodes Pks13, the key enzyme for synthesizing MA in C. glutamicum ATCC13032, it was deleted, resulting in the mutant WG001. Compared with the wild-type ATCC13869, MA was not synthesized in WG001, but more phosphatidylglycerol and phosphatidylinositol containing longer unsaturated fatty acids were produced. WG001 cells also show hindered cell growth and defective cell separation when compared with ATCC13869 cells. Transcriptomic analysis shows that many genes relevant to the pathways of fatty acids, inositol, phospholipids, cell wall, and cell division were significantly regulated in WG001 cells when compared with ATCC13869 cells. This study demonstrates that the locus BBD29_RS14045 encodes a key enzyme that plays important role for synthesizing MA in C. glutamicum ATCC13869.

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A third glucose uptake bypass in Corynebacterium glutamicum ATCC 31833

Cited by 13 publications

References 36 publications

Rewiring the Central Metabolic Pathway for High‐Yield l‐Serine Production in Corynebacterium glutamicum by Using Glucose

Rewiring the Central Metabolic Pathway for High‐Yield l‐Serine Production in Corynebacterium glutamicum by Using Glucose

Engineering Corynebacterium glutamicum for fast production of l-lysine and l-pipecolic acid

Impact of mycolic acid deficiency on cells of Corynebacterium glutamicum ATCC13869

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