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Literature summary extracted from

  • Wolff, E.C.; Wolff.J.; Park, M.H.
    Deoxyhypusine synthase generates and uses bound NADH in a transient hydride transfer mechanism (2000), J. Biol. Chem., 275, 9170-9177.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
2.5.1.46 K329R no activity Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.5.1.46 [eIF5A-precursor]-lysine + spermidine Homo sapiens
-
 [eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.46 Homo sapiens
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.46 [eIF5A-precursor]-lysine + spermidine
-
 Homo sapiens [eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
-
 ?
2.5.1.46 [eIF5A-precursor]-lysine + spermidine
-
 Homo sapiens [eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine i.e. [eIF5A-precursor]-N6-(4-aminobutyl)lysine ?

Cofactor

EC Number Cofactor Comment Organism Structure
2.5.1.46 NAD+ the NADH generated in the first step of the reaction remains enzyme-associated during the reaction and the hydride ion generated by the oxidation of spermidine is preserved for the reduction of the eIF5A-imine intermediate Homo sapiens
2.5.1.46 NADH
-
 Homo sapiens