“Saccharopine dehydrogenase (NADP+, L-glutamate-forming)”的意思、由来-开放百科全书

词条

Saccharopine dehydrogenase (NADP+, L-glutamate-forming)

释义

Structural studies
References

{{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 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 {{PDB link|1E5L}}, {{PDB link|1E5Q}}, and {{PDB link|2AXQ}}.

References

{{cite journal |vauthors=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 = 3430–4 | pmid = 4380448 | issue = 14 }}

3 : EC 1.5.1|NADPH-dependent enzymes|Enzymes of known structure

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