scholarly journals Saccharopine, an Intermediate of the Aminoadipic Acid Pathway of Lysine Biosynthesis

1965 ◽  
Vol 240 (6) ◽  
pp. 2524-2530 ◽  
Author(s):  
J.S. Trupin ◽  
Harry P. Broquist
Keyword(s):  
Lysine Biosynthesis ◽  
Acid Pathway

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 Lysine catabolism: flow, metabolic role and regulation

2003 ◽  
Vol 15 (1) ◽  
pp. 9-18 ◽  
Author(s):  
Ricardo Francisco Fornazier ◽  
Ricardo Antunes Azevedo ◽  
Renato Rodrigues Ferreira ◽  
Vanderlei Aparecido Varisi
Keyword(s):  
Environmental Changes ◽  
Lysine Biosynthesis ◽  
Direct Result ◽  
Physiological Processes ◽  
Saccharopine Dehydrogenase ◽  
Metabolic Role ◽  
Lysine Concentration ◽  
Lysine Degradation ◽  
Acid Pathway ◽  
Lysine Catabolism

Lysine is an essential amino acid, synthesized in plants in the aspartic acid pathway. The lysine catabolism is performed by the action of two consecutive enzymes, lysine 2-oxoglutarate reductase (LOR) and saccharopine dehydrogenase (SDH). The steady state of lysine is controlled by both, synthesis and catabolism rates, with the final soluble lysine concentration in cereal seeds a direct result of these processes. In the last 40 years, the enzymes involved in lysine biosynthesis have been purified and characterized from some plant species such as carrot, maize, barley, rice, and coix. Recent reports have revealed that lysine degradation might be related to various physiological processes, for instance growth, development and response to environmental changes and stress. The understanding of the regulatory aspects of the lysine biosynthetic and catabolic pathways and manipulation of related enzymes is important for the production of high-lysine plants.

Lysine biosynthesis inMethanobacterium thermoautotrophicum is by the diaminopimelic acid pathway

1984 ◽  
Vol 10 (4) ◽  
pp. 195-198 ◽  
Author(s):  
Nouna Bakhiet ◽  
Fred W. Forney ◽  
Donald P. Stahly ◽  
Lacy Daniels
Keyword(s):  
Lysine Biosynthesis ◽  
Diaminopimelic Acid ◽  
Acid Pathway

Chlorobutanol, a Preservative of Desmopressin, Inhibits Human Platelet Aggregation and Release In Vitro

1990 ◽  
Vol 64 (03) ◽  
pp. 473-477 ◽  
Author(s):  
Shih-Luen Chen ◽  
Wu-Chang Yang ◽  
Tung-Po Huang ◽  
Shiang Wann ◽  
Che-ming Teng
Keyword(s):  
Arachidonic Acid ◽  
Platelet Aggregation ◽  
Atp Release ◽  
Free Calcium ◽  
Dependent Manner ◽  
Antiplatelet Effect ◽  
Human Platelet Aggregation ◽  
Acid Pathway ◽  
Arachidonic Acid Pathway

SummaryTherapeutic preparations of desmopressin for parenteral use contain the preservative chlorobutanol (5 mg/ml). We show here that chlorobutanol is a potent inhibitor of platelet aggregation and release. It exhibited a significant inhibitory activity toward several aggregation inducers in a concentration- and time-dependent manner. Thromboxane B2 formation, ATP release, and elevation of cytosolic free calcium caused by collagen, ADP, epinephrine, arachidonic acid and thrombin respectively were markedly inhibited by chlorobutanol. Chlorobutanol had no effect on elastase- treated platelets and its antiplatelet effect could be reversed. It is concluded that the antiplatelet effect of chlorobutanol is mainly due to its inhibition on the arachidonic acid pathway but it is unlikely to have a nonspecitic toxic effect. This antiplatelet effect of chlorobutanol suggests that desmopressin, when administered for improving hemostasis, should not contain chlorobutanol as a preservative.

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