scholarly journals Nutritional‐rich and stress‐tolerant crops by saccharopine pathway manipulation

2012 ◽  
Vol 1 (2) ◽  
pp. 141-147 ◽  
Author(s):  
Paulo Arruda ◽  
Izabella Pena Neshich
Keyword(s):  
Saccharopine Pathway

scholarly journals Regulation of oxidative degradation of l-lysine in rat liver mitochondria

1994 ◽  
Vol 300 (3) ◽  
pp. 887-891 ◽  
Author(s):  
P W Scislowski ◽  
A R Foster ◽  
M F Fuller
Keyword(s):  
Rat Liver ◽  
Oxidative Degradation ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Complex Mechanism ◽  
Saccharopine Dehydrogenase ◽  
Saccharopine Pathway

The generation of 14CO2 from [1-14C]lysine by hepatic mitochondria through the saccharopine pathway is controlled by intramitochondrial concentrations of lysine, 2-oxoglutarate and NADPH. Mitochondria, isolated from rats pre-treated with glucagon, exhibited higher activities of L-lysine: 2-oxoglutarate reductase, saccharopine dehydrogenase and 2-aminoadipate aminotransferase. The flux through this pathway is stimulated in liver mitochondria after glucagon treatment. Multiple regulation of lysine oxidation in liver mitochondria confirms a complex mechanism of ‘mitochondrial activation’ by glucagon.

scholarly journals Mouse lysine catabolism to aminoadipate occurs primarily through the saccharopine pathway; implications for pyridoxine dependent epilepsy (PDE)

2017 ◽  
Vol 1863 (1) ◽  
pp. 121-128 ◽  
Author(s):  
Izabella Agostinho Pena ◽  
Lygia Azevedo Marques ◽  
Ângelo B.A. Laranjeira ◽  
José A. Yunes ◽  
Marcos N. Eberlin ◽  
...  
Keyword(s):  
Lysine Catabolism ◽  
Saccharopine Pathway

scholarly journals Lysine degradation through the saccharopine pathway in mammals: involvement of both bifunctional and monofunctional lysine-degrading enzymes in mouse

1999 ◽  
Vol 344 (2) ◽  
pp. 555 ◽  
Author(s):  
Fabio PAPES ◽  
Edson L. KEMPER ◽  
Germano CORD-NETO ◽  
Francesco LANGONE ◽  
Paulo ARRUDA
Keyword(s):  
Degrading Enzymes ◽  
Lysine Degradation ◽  
Saccharopine Pathway

scholarly journals Lysine degradation through the saccharopine pathway in bacteria: LKR and SDH in bacteria and its relationship to the plant and animal enzymes

FEBS Letters ◽  
2012 ◽  
Vol 586 (6) ◽  
pp. 905-911 ◽  
Author(s):  
Guilherme Coutinho de Mello Serrano ◽  
Thaís Rezende e Silva Figueira ◽  
Eduardo Kiyota ◽  
Natalia Zanata ◽  
Paulo Arruda
Keyword(s):  
Lysine Degradation ◽  
Saccharopine Pathway

The saccharopine pathway in seed development and stress response of maize

2015 ◽  
Vol 38 (11) ◽  
pp. 2450-2461 ◽  
Author(s):  
Eduardo Kiyota ◽  
Izabella Agostinho Pena ◽  
Paulo Arruda
Keyword(s):  
Stress Response ◽  
Seed Development ◽  
Saccharopine Pathway

scholarly journals Lysine degradation through the saccharopine pathway in mammals: involvement of both bifunctional and monofunctional lysine-degrading enzymes in mouse

1999 ◽  
Vol 344 (2) ◽  
pp. 555-563 ◽  
Author(s):  
Fabio PAPES ◽  
Edson L. KEMPER ◽  
Germano CORD-NETO ◽  
Francesco LANGONE ◽  
Paulo ARRUDA
Keyword(s):  
Mitochondrial Protein ◽  
Bifunctional Enzyme ◽  
Saccharopine Dehydrogenase ◽  
Isolation And Characterization ◽  
Short Transcript ◽  
Liver And Kidney ◽  
Lysine Degradation ◽  
First Time ◽  
Saccharopine Pathway

Lysine-oxoglutarate reductase and saccharopine dehydrogenase are enzymic activities that catalyse the first two steps of lysine degradation through the saccharopine pathway in upper eukaryotes. This paper describes the isolation and characterization of a cDNA clone encoding a bifunctional enzyme bearing domains corresponding to these two enzymic activities. We partly purified those activities from mouse liver and showed for the first time that both a bifunctional lysine-oxoglutarate reductase/saccharopine dehydrogenase and a monofunctional saccharopine dehydrogenase are likely to be present in this organ. Northern analyses indicate the existence of two mRNA species in liver and kidney. The longest molecule, 3.4 kb in size, corresponds to the isolated cDNA and encodes the bifunctional enzyme. The 2.4 kb short transcript probably codes for the monofunctional dehydrogenase. Sequence analyses show that the bifunctional enzyme is likely to be a mitochondrial protein. Furthermore, enzymic and expression analyses suggest that lysine-oxoglutarate reductase/saccharopine dehydrogenase levels increase in livers of mice under starvation. Lysine-injected mice also show an increase in lysine-oxoglutarate reductase and saccharopine dehydrogenase levels.

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