View source for Saccharopine dehydrogenase (NADP+, L-lysine-forming)

{{infobox enzyme
| Name       = saccharopine dehydrogenase (NADP+, L-lysine-forming)
| EC_number  = 1.5.1.8
| CAS_number = 9031-19-0
| GO_code    = 0047130
| image      =
| width      = 
| caption    =  
}}
In [[enzymology]], a '''saccharopine dehydrogenase (NADP+, L-lysine-forming)''' ({{EC number|1.5.1.8}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]

:N<sub>6</sub>-(L-1,3-dicarboxypropyl)-L-lysine + NADP<sup>+</sup> + H<sub>2</sub>O <math>\rightleftharpoons</math> L-lysine + 2-oxoglutarate + NADPH + H<sup>+</sup>

The 3 [[substrate (biochemistry)|substrates]] of this enzyme are [[N6-(L-1,3-dicarboxypropyl)-L-lysine]], [[nicotinamide adenine dinucleotide phosphate|NADP<sup>+</sup>]], and [[water|H<sub>2</sub>O]], whereas its 4 [[product (chemistry)|products]] are [[L-lysine]], [[2-oxoglutarate]], [[nicotinamide adenine dinucleotide phosphate|NADPH]], and [[hydrogen ion|H<sup>+</sup>]].

This enzyme belongs to the family of [[oxidoreductase]]s, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor.  The [[List of enzymes|systematic name]] of this enzyme class is '''N6-(L-1,3-dicarboxypropyl)-L-lysine:NADP+ oxidoreductase (L-lysine-forming)'''. Other names in common use include '''lysine-2-oxoglutarate reductase''', '''lysine-ketoglutarate reductase''', '''L-lysine-alpha-ketoglutarate reductase''', '''lysine:alpha-ketoglutarate:TPNH oxidoreductase''', '''(epsilon-N-[gultaryl-2]-L-lysine forming)''', '''saccharopine (nicotinamide adenine dinucleotide phosphate,''', '''lysine-forming) dehydrogenase''', '''6-N-(L-1,3-dicarboxypropyl)-L-lysine:NADP+ oxidoreductase''', and '''(L-lysine-forming)'''.  This enzyme participates in [[lysine biosynthesis]] and [[lysine degradation]].

==References==
{{reflist|1}}
* {{cite journal | vauthors = Hutzler J, Dancis J | date = 1968 | title = Conversion of lysine to saccharopine by human tissues | journal = Biochim. Biophys. Acta  | volume = 158 | pages = 62&ndash;9  | pmid = 4385118 | issue = 1 | doi=10.1016/0304-4165(68)90072-x}}
* {{cite journal | vauthors = Markovitz PJ, Chuang DT, Cox RP | date = 1984 | title = Familial hyperlysinemias. Purification and characterization of the bifunctional aminoadipic semialdehyde synthase with lysine-ketoglutarate reductase and saccharopine dehydrogenase activities | journal = J. Biol. Chem.  | volume = 259 | pages = 11643&ndash;6  | pmid = 6434529 | issue = 19 }}

{{CH-NH oxidoreductases}}
{{Enzymes}}
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[[Category:EC 1.5.1]]
[[Category:NADPH-dependent enzymes]]
[[Category:Enzymes of unknown structure]]


{{1.5-enzyme-stub}}