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{{enzyme
| Name = saccharopine dehydrogenase (NADP+, L-glutamate-forming)
| EC_number = 1.5.1.10
| CAS_number = 9033-55-0
| IUBMB_EC_number = 1/5/1/10
| GO_code = 0004755
| image =
| width =
| caption =
}}
In [[enzymology]], a '''saccharopine dehydrogenase (NADP+, L-glutamate-forming)''' ({{EC number|1.5.1.10}}) 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-glutamate + L-2-aminoadipate 6-semialdehyde + NADPH + H<sup>+</sup>


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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-glutamate]], [[L-2-aminoadipate 6-semialdehyde]], [[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 systematic name of this enzyme class is '''N6-(L-1,3-dicarboxypropyl)-L-lysine:NADP+ oxidoreductase (L-glutamate-forming)'''. Other names in common use include '''saccharopine (nicotinamide adenine dinucleotide phosphate,''', '''glutamate-forming) dehydrogenase''', '''aminoadipic semialdehyde-glutamic reductase''', '''aminoadipate semialdehyde-glutamate reductase''', '''aminoadipic semialdehyde-glutamate reductase''', '''epsilon-N-(L-glutaryl-2)-L-lysine:NAD+(P) oxidoreductase''', '''(L-2-aminoadipate-semialdehyde forming)''', '''saccharopine reductase''', '''6-N-(L-1,3-dicarboxypropyl)-L-lysine:NADP+ oxidoreductase''', and '''(L-glutamate-forming)'''.  This enzyme participates in [[lysine biosynthesis]] and [[lysine degradation]]. 
 
==Structural studies==
 
As of late 2007, 3 [[tertiary structure|structures]] have been solved for this class of enzymes, with [[Protein Data Bank|PDB]] accession codes {{PDB link|1E5L}}, {{PDB link|1E5Q}}, and {{PDB link|2AXQ}}.
 
==References==
{{reflist|1}}
* {{cite journal | author = Jones EE, Broquist HP | date = 1966 | title = Saccharopine, an intermediate of the aminoadipic acid pathway of lysine biosynthesis. 3. Aminoadipic semialdehyde-glutamate reductase | journal = J. Biol. Chem. | volume = 241 | pages = 3430&ndash;4  | pmid = 4380448 | issue = 14 }}
 
{{1.5-enzyme-stub}}
 
[[Category:EC 1.5.1]]
[[Category:NADPH-dependent enzymes]]
[[Category:Enzymes of known structure]]

Revision as of 03:58, 2 March 2013

Template:Enzyme In enzymology, a saccharopine dehydrogenase (NADP+, L-glutamate-forming) (Air Transportation Experts Kull from Wingham, has many interests that include butterflies, property developers in singapore and digital photography. Is a travel freak and in recent past made buy a house in singapore journey to Paleochristian and Byzantine Monuments of Thessalonika.) is an enzyme that catalyzes the chemical reaction

N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O L-glutamate + L-2-aminoadipate 6-semialdehyde + NADPH + H+

The 3 substrates of this enzyme are N6-(L-1,3-dicarboxypropyl)-L-lysine, NADP+, and H2O, whereas its 4 products are L-glutamate, L-2-aminoadipate 6-semialdehyde, NADPH, and H+.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is N6-(L-1,3-dicarboxypropyl)-L-lysine:NADP+ oxidoreductase (L-glutamate-forming). Other names in common use include saccharopine (nicotinamide adenine dinucleotide phosphate,, glutamate-forming) dehydrogenase, aminoadipic semialdehyde-glutamic reductase, aminoadipate semialdehyde-glutamate reductase, aminoadipic semialdehyde-glutamate reductase, epsilon-N-(L-glutaryl-2)-L-lysine:NAD+(P) oxidoreductase, (L-2-aminoadipate-semialdehyde forming), saccharopine reductase, 6-N-(L-1,3-dicarboxypropyl)-L-lysine:NADP+ oxidoreductase, and (L-glutamate-forming). This enzyme participates in lysine biosynthesis and lysine degradation.

Structural studies

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes Template:PDB link, Template:PDB link, and Template:PDB link.

References

43 year old Petroleum Engineer Harry from Deep River, usually spends time with hobbies and interests like renting movies, property developers in singapore new condominium and vehicle racing. Constantly enjoys going to destinations like Camino Real de Tierra Adentro.

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