Deoxyhypusine synthase

Deoxyhypusine synthase (EC 2.5.1.46, spermidine:eIF5A-lysine 4-aminobutyltransferase (propane-1,3-diamine-forming)) is an enzyme with systematic name (eIF5A-precursor)-lysine:spermidine 4-aminobutyltransferase (propane-1,3-diamine-forming).[1][2][3][4][5][6][7][8][9] This enzyme catalyses the following chemical reaction

[eIF5A-precursor]-lysine + spermidine [eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine (overall reaction)
(1a) spermidine + NAD+ dehydrospermidine + NADH
(1b) dehydrospermidine + [enzyme]-lysine N-(4-aminobutylidene)-[enzyme]-lysine + propane-1,3-diamine
(1c) N-(4-aminobutylidene)-[enzyme]-lysine + [eIF5A-precursor]-lysine N-(4-aminobutylidene)-[eIF5A-precursor]-lysine + [enzyme]-lysine
(1d) N-(4-aminobutylidene)-[eIF5A-precursor]-lysine + NADH + H+ [eIF5A-precursor]-deoxyhypusine + NAD+
Deoxyhypusine synthase
Identifiers
EC number2.5.1.46
CAS number127069-31-2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

The eukaryotic initiation factor eIF5A contains a hypusine residue that is essential for activity.

References
  1. Yoshioka H, Ramirez F (April 1990). "Pro-alpha 1(XI) collagen. Structure of the amino-terminal propeptide and expression of the gene in tumor cell lines". The Journal of Biological Chemistry. 265 (11): 6423–6. PMID 1690726.
  2. Wolff EC, Folk JE, Park MH (June 1997). "Enzyme-substrate intermediate formation at lysine 329 of human deoxyhypusine synthase". The Journal of Biological Chemistry. 272 (25): 15865–71. doi:10.1074/jbc.272.25.15865. PMID 9188485.
  3. Chen KY, Liu AY (1997). "Biochemistry and function of hypusine formation on eukaryotic initiation factor 5A". Biological Signals. 6 (3): 105–9. doi:10.1159/000109115. PMID 9285092.
  4. Ober D, Hartmann T (November 1999). "Deoxyhypusine synthase from tobacco. cDNA isolation, characterization, and bacterial expression of an enzyme with extended substrate specificity". The Journal of Biological Chemistry. 274 (45): 32040–7. doi:10.1074/jbc.274.45.32040. PMID 10542236.
  5. Ober D, Hartmann T (December 1999). "Homospermidine synthase, the first pathway-specific enzyme of pyrrolizidine alkaloid biosynthesis, evolved from deoxyhypusine synthase". Proceedings of the National Academy of Sciences of the United States of America. 96 (26): 14777–82. Bibcode:1999PNAS...9614777O. doi:10.1073/pnas.96.26.14777. PMC 24724. PMID 10611289.
  6. Wolff EC, Park MH (January 1999). "Identification of lysine350 of yeast deoxyhypusine synthase as the site of enzyme intermediate formation". Yeast. 15 (1): 43–50. doi:10.1002/(SICI)1097-0061(19990115)15:1<43::AID-YEA344>3.0.CO;2-K. PMID 10028184.
  7. Wolff EC, Wolff J, Park MH (March 2000). "Deoxyhypusine synthase generates and uses bound NADH in a transient hydride transfer mechanism". The Journal of Biological Chemistry. 275 (13): 9170–7. doi:10.1074/jbc.275.13.9170. PMID 10734052.
  8. Joe YA, Wolff EC, Park MH (September 1995). "Cloning and expression of human deoxyhypusine synthase cDNA. Structure-function studies with the recombinant enzyme and mutant proteins". The Journal of Biological Chemistry. 270 (38): 22386–92. doi:10.1074/jbc.270.38.22386. PMID 7673224.
  9. Tao Y, Chen KY (October 1995). "Molecular cloning and functional expression of Neurospora deoxyhypusine synthase cDNA and identification of yeast deoxyhypusine synthase cDNA". The Journal of Biological Chemistry. 270 (41): 23984–7. doi:10.1074/jbc.270.41.23984. PMID 7592594.
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