(eIF5A-precursor)-lysine:spermidine 4-aminobutyltransferase (propane-1,3-diamine-forming)

Deoxyhypusine synthase
Identifiers
EC no.2.5.1.46
CAS no.127069-31-2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

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+

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. doi:10.1016/S0021-9258(19)39343-3. 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.

External links[]