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

词条

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

释义

References

{{enzyme
| Name = saccharopine dehydrogenase (NADP+, L-lysine-forming)
| EC_number = 1.5.1.8
| CAS_number = 9031-19-0
| IUBMB_EC_number = 1/5/1/8
| 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 catalyzes the chemical reaction

N₆-(L-1,3-dicarboxypropyl)-L-lysine + NADP⁺ + H₂O L-lysine + 2-oxoglutarate + 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-lysine, 2-oxoglutarate, 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-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

{{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 = 62–9 | 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 = 11643–6 | pmid = 6434529 | issue = 19 }}

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

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