scholarly journals Involvement of meso-.ALPHA.,.EPSILON.-diaminopimelate D-dehydrogenase in lysine biosynthesis in Corynebacterium glutamicum.

1984 ◽  
Vol 48 (10) ◽  
pp. 2557-2560 ◽  
Author(s):  
Shuichi ISHINO ◽  
Kazuo YAMAGUCHI ◽  
Kunikatsu SHIRAHATA ◽  
Kazumi ARAKI
Keyword(s):  
Corynebacterium Glutamicum ◽  
Lysine Biosynthesis

Production of Cadaverine in Recombinant Corynebacterium Glutamicum Overexpressing Lysine Decarboxylase (ldcC) and Response Regulator dr1558

2021 ◽  
Author(s):  
Soong-bin Kang ◽  
Jong-il choi
Keyword(s):  
Corynebacterium Glutamicum ◽  
Phosphoenolpyruvate Carboxykinase ◽  
Deinococcus Radiodurans ◽  
Response Regulator ◽  
Fold Increase ◽  
Lysine Biosynthesis ◽  
Lysine Decarboxylase ◽  
Fed Batch ◽  
Fed Batch Fermentation ◽  
Polymerase Chain

Abstract In this study, the response regulator DR1558 from Deinococcus radiodurans was overexpressed in recombinant Corynebacterium glutamicum with lysine decarboxylase (ldcC). The recombinant C. glutamicum strain overexpressing dr1558 and ldcC produced 5.9 g/L of cadaverine by flask cultivation, whereas the control strain overexpressing only ldcC produced 4.5 g/L of cadaverine. To investigate the mechanism underlying the effect of DR1558, the expression levels of genes related to central metabolism and lysine-biosynthesis were analyzed by quantitative-real time polymerase chain reaction. The results showed that phosphoenolpyruvate carboxykinase (pck) was downregulated, and pyruvate kinase (pyk) and other lysine biosynthesis genes were upregulated. Furthermore, in fed-batch fermentation, C. glutamicum coexpressing dr1558 produced 25.14 g/L of cadaverine, a 1.25-fold increase in concentration relative to the control. These results suggested that the heterologous expression of dr1558 may improve the production of biorefinery products by recombinant C. glutamicum.

scholarly journals Regulation of Enzymes of Lysine Biosynthesis in Corynebacterium glutamicum

Microbiology ◽  
1988 ◽  
Vol 134 (12) ◽  
pp. 3221-3229 ◽  
Author(s):  
J. CREMER ◽  
C. TREPTOW ◽  
L. EGGELING ◽  
H. SAHM
Keyword(s):  
Corynebacterium Glutamicum ◽  
Lysine Biosynthesis

scholarly journals Reconstruction of the Diaminopimelic Acid Pathway to Promote L-lysine Production in Corynebacterium Glutamicum

2021 ◽  
Author(s):  
Ning Liu ◽  
Ting-Ting Zhang ◽  
Zhi-Ming Rao ◽  
Wei-Guo Zhang ◽  
Jian-Zhong Xu
Keyword(s):  
Corynebacterium Glutamicum ◽  
Regulatory Protein ◽  
Lysine Biosynthesis ◽  
Diaminopimelic Acid ◽  
Specific Rate ◽  
Original Strain ◽  
Lysine Production ◽  
Final Strain ◽  
Acid Pathway ◽  
Maximum Specific Rate

Abstract Background: The dehydrogenase pathway and the succinylase pathway are involved in the synthesis of L-lysine in Corynebacterium glutamicum. Despite the low contribution rate to L-lysine production, the dehydrogenase pathway is favorable for its simple steps and great potentials to increase the production of L-lysine. Results: The aim of this work is to enhance the carbon flux in dehydrogenase pathway to promote L-lysine production. Firstly, the effect of ammonium (NH4+) concentration on L-lysine biosynthesis was investigated, and the results indicated that the biosynthesis of L-lysine can be promoted in high NH4+ environment. In order to reduce the requirement of NH4+, the nitrogen source regulatory protein AmtR was knocked out, resulting in an 8.5% increase in L-lysine production (i.e., 52.3±4.31 g/L). Subsequently, the dehydrogenase pathway was upregulated by blocking or weakening tetrahydrodipicolinate succinylase (DapD)-coding gene dapD and overexpressing the ddh gene to further enhance L-lysine biosynthesis. The final strain XQ-5-W4 could produce 189±8.7 g/L L-lysine with the maximum specific rate (qLys,max.) of 0.35±0.05 g/(g·h) in a 5-L jar fermenter. Conclusions: The L-lysine titer and qLys,max achieved in this study is about 25.2% and 59.1% higher than that of the original strain without enhancement of dehydrogenase pathway, respectively. The results indicated that the dehydrogenase pathway could serve as a breakthrough point to reconstruct the diaminopimelic acid (DAP) pathway and promote L-lysine production.

scholarly journals Reconstruction of the Diaminopimelic Acid Pathway to Promote L-lysine Production in Corynebacterium glutamicum

2021 ◽  
Vol 22 (16) ◽  
pp. 9065
Author(s):  
Ning Liu ◽  
Ting-Ting Zhang ◽  
Zhi-Ming Rao ◽  
Wei-Guo Zhang ◽  
Jian-Zhong Xu
Keyword(s):  
Corynebacterium Glutamicum ◽  
Regulatory Protein ◽  
Lysine Biosynthesis ◽  
Diaminopimelic Acid ◽  
Specific Rate ◽  
Original Strain ◽  
Lysine Production ◽  
Final Strain ◽  
Acid Pathway ◽  
Maximum Specific Rate

The dehydrogenase pathway and the succinylase pathway are involved in the synthesis of L-lysine in Corynebacterium glutamicum. Despite the low contribution rate to L-lysine production, the dehydrogenase pathway is favorable for its simple steps and potential to increase the production of L-lysine. The effect of ammonium (NH4+) concentration on L-lysine biosynthesis was investigated, and the results indicated that the biosynthesis of L-lysine can be promoted in a high NH4+ environment. In order to reduce the requirement of NH4+, the nitrogen source regulatory protein AmtR was knocked out, resulting in an 8.5% increase in L-lysine production (i.e., 52.3 ± 4.31 g/L). Subsequently, the dehydrogenase pathway was upregulated by blocking or weakening the tetrahydrodipicolinate succinylase (DapD)-coding gene dapD and overexpressing the ddh gene to further enhance L-lysine biosynthesis. The final strain XQ-5-W4 could produce 189 ± 8.7 g/L L-lysine with the maximum specific rate (qLys,max.) of 0.35 ± 0.05 g/(g·h) in a 5-L jar fermenter. The L-lysine titer and qLys,max achieved in this study is about 25.2% and 59.1% higher than that of the original strain without enhancement of dehydrogenase pathway, respectively. The results indicated that the dehydrogenase pathway could serve as a breakthrough point to reconstruct the diaminopimelic acid (DAP) pathway and promote L-lysine production.

scholarly journals Fermentative Production of l-2-Hydroxyglutarate by Engineered Corynebacterium glutamicum via Pathway Extension of l-Lysine Biosynthesis

2021 ◽  
Vol 8 ◽  
Author(s):  
Carina Prell ◽  
Arthur Burgardt ◽  
Florian Meyer ◽  
Volker F. Wendisch
Keyword(s):  
Corynebacterium Glutamicum ◽  
Strain Engineering ◽  
Lysine Biosynthesis ◽  
Oxidation Reactions ◽  
Native Promoter ◽  
Fermentative Production ◽  
A Genome ◽  
Media Adaptation ◽  
Major Bottleneck ◽  
Pharmaceutical Industries

l-2-hydroxyglutarate (l-2HG) is a trifunctional building block and highly attractive for the chemical and pharmaceutical industries. The natural l-lysine biosynthesis pathway of the amino acid producer Corynebacterium glutamicum was extended for the fermentative production of l-2HG. Since l-2HG is not native to the metabolism of C. glutamicum metabolic engineering of a genome-streamlined l-lysine overproducing strain was required to enable the conversion of l-lysine to l-2HG in a six-step synthetic pathway. To this end, l-lysine decarboxylase was cascaded with two transamination reactions, two NAD(P)-dependent oxidation reactions and the terminal 2-oxoglutarate-dependent glutarate hydroxylase. Of three sources for glutarate hydroxylase the metalloenzyme CsiD from Pseudomonas putida supported l-2HG production to the highest titers. Genetic experiments suggested a role of succinate exporter SucE for export of l-2HG and improving expression of its gene by chromosomal exchange of its native promoter improved l-2HG production. The availability of Fe2+ as cofactor of CsiD was identified as a major bottleneck in the conversion of glutarate to l-2HG. As consequence of strain engineering and media adaptation product titers of 34 ± 0 mM were obtained in a microcultivation system. The glucose-based process was stable in 2 L bioreactor cultivations and a l-2HG titer of 3.5 g L−1 was obtained at the higher of two tested aeration levels. Production of l-2HG from a sidestream of the starch industry as renewable substrate was demonstrated. To the best of our knowledge, this study is the first description of fermentative production of l-2HG, a monomeric precursor used in electrochromic polyamides, to cross-link polyamides or to increase their biodegradability.

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