"Saccharopine Dehydrogenases" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
Amine oxidoreductases that use either NAD+ (EC 184.108.40.206) or NADP+ (EC 220.127.116.11) as an acceptor to form L-LYSINE or NAD+ (EC 18.104.22.168) or NADP+ (EC 22.214.171.124) as an acceptor to form L-GLUTAMATE. Deficiency of this enzyme causes HYPERLYSINEMIAS.
- Saccharopine Dehydrogenases
- Dehydrogenases, Saccharopine
- Lysine-Ketoglutarate Reductase
- Lysine Ketoglutarate Reductase
- Reductase, Lysine-Ketoglutarate
Below are MeSH descriptors whose meaning is more general than "Saccharopine Dehydrogenases".
Below are MeSH descriptors whose meaning is more specific than "Saccharopine Dehydrogenases".
This graph shows the total number of publications written about "Saccharopine Dehydrogenases" by people in this website by year, and whether "Saccharopine Dehydrogenases" was a major or minor topic of these publications.
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Below are the most recent publications written about "Saccharopine Dehydrogenases" by people in Profiles.
Probing the chemical mechanism of saccharopine reductase from Saccharomyces cerevisiae using site-directed mutagenesis. Arch Biochem Biophys. 2015 Oct 15; 584:98-106.
Supporting role of lysine 13 and glutamate 16 in the acid-base mechanism of saccharopine dehydrogenase from Saccharomyces cerevisiae. Arch Biochem Biophys. 2012 Jun 01; 522(1):57-61.
Evidence in support of lysine 77 and histidine 96 as acid-base catalytic residues in saccharopine dehydrogenase from Saccharomyces cerevisiae. Biochemistry. 2012 Jan 31; 51(4):857-66.
The oxidation state of active site thiols determines activity of saccharopine dehydrogenase at low pH. Arch Biochem Biophys. 2011 Sep 15; 513(2):71-80.
Contribution of K99 and D319 to substrate binding and catalysis in the saccharopine dehydrogenase reaction. Arch Biochem Biophys. 2011 Oct; 514(1-2):8-15.
Glutamates 78 and 122 in the active site of saccharopine dehydrogenase contribute to reactant binding and modulate the basicity of the acid-base catalysts. J Biol Chem. 2010 Jul 02; 285(27):20756-68.
Chemical mechanism of saccharopine reductase from Saccharomyces cerevisiae. Biochemistry. 2009 Jun 30; 48(25):5899-907.
Overall kinetic mechanism of saccharopine dehydrogenase (L-glutamate forming) from Saccharomyces cerevisiae. Biochemistry. 2008 May 13; 47(19):5417-23.
Crystal structures of ligand-bound saccharopine dehydrogenase from Saccharomyces cerevisiae. Biochemistry. 2007 Nov 06; 46(44):12512-21.
Determinants of substrate specificity for saccharopine dehydrogenase from Saccharomyces cerevisiae. Biochemistry. 2007 Jun 26; 46(25):7625-36.