L-erythro-3,5-diaminohexanoate dehydrogenase

In enzymology, a L-erythro-3,5-diaminohexanoate dehydrogenase (EC number|1.4.1.11) is an enzyme that catalyzes the chemical reaction

:L-erythro-3,5-diaminohexanoate + H₂O + NAD⁺ $ightleftharpoons$ (S)-5-amino-3-oxohexanoate + NH₃ + NADH + H⁺

The 3 substrates of this enzyme are L-erythro-3,5-diaminohexanoate, H₂O, and NAD⁺, whereas its 4 products are (S)-5-amino-3-oxohexanoate, NH₃, NADH, and H⁺.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-erythro-3,5-diaminohexanoate:NAD+ oxidoreductase (deaminating). This enzyme is also called L-3,5-diaminohexanoate dehydrogenase. This enzyme participates in lysine degradation.

References

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External links

::"The CAS registry number for this enzyme class is CAS registry|37377-90-5."

Gene Ontology (GO) codes