scholarly journals Purification and Characterization of the Bifunctional Enzyme Lysine-Ketoglutarate Reductase-Saccharopine Dehydrogenase from Maize

1996 ◽  
Vol 110 (3) ◽  
pp. 765-771 ◽  
Author(s):  
M. Goncalves-Butruille ◽  
P. Szajner ◽  
E. Torigoi ◽  
A. Leite ◽  
P. Arruda
Keyword(s):  
Bifunctional Enzyme ◽  
Purification And Characterization ◽  
Saccharopine Dehydrogenase

scholarly journals Purification and Characterization of Bifunctional Lysine-Ketoglutarate Reductase/Saccharopine Dehydrogenase from Developing Soybean Seeds

2000 ◽  
Vol 123 (2) ◽  
pp. 655-664 ◽  
Author(s):  
Daphna Miron ◽  
Sari Ben-Yaacov ◽  
Dalit Reches ◽  
Avigail Schupper ◽  
Gad Galili
Keyword(s):  
Soybean Seeds ◽  
Purification And Characterization ◽  
Saccharopine Dehydrogenase

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.

Sign in / Sign up

Export Citation Format

Share Document