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Spermidine dehydrogenase

From Wikipedia, the free encyclopedia

In enzymology, a spermidine dehydrogenase (EC 1.5.99.6) is an enzyme that catalyzes the chemical reaction

spermidine + acceptor + H2O propane-1,3-diamine + 4-aminobutanal + reduced acceptor

The 3 substrates of this enzyme are spermidine, acceptor, and H2O, whereas its 3 products are propane-1,3-diamine, 4-aminobutanal, and reduced acceptor.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donor with other acceptors. The systematic name of this enzyme class is spermidine:acceptor oxidoreductase. This enzyme is also called spermidine:(acceptor) oxidoreductase. This enzyme participates in urea cycle and metabolism of amino groups and beta-alanine metabolism. It has 2 cofactors: FAD, and Heme.

References

  • Tabor CW, Kellogg PD (1970). "Identification of flavin adenine dinucleotide and heme in a homogeneous spermidine dehydrogenase from Serratia marcescens". J. Biol. Chem. 245 (20): 5424–33. PMID 4918845.
  • Tabor H; Tabor CW (1972). "Biosynthesis and metabolism of 1,4-diaminobutane, spermidine, spermine, and related amines. IIE2a Speridine dehydrogenase". Adv. Enzymol. Relat. Areas Mol. Biol. 36: 225–226.


This page was last edited on 26 August 2023, at 15:51
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