Deoxyhypusine synthase

Deoxyhypusine synthase
Identifiers
EC number	2.5.1.46
CAS number	127069-31-2
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Search PMC articles PubMed articles NCBI proteins

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 $\rightleftharpoons$ [eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine (overall reaction)

(1a) spermidine + NAD⁺ $\rightleftharpoons$ dehydrospermidine + NADH

(1b) dehydrospermidine + [enzyme]-lysine $\rightleftharpoons$ N-(4-aminobutylidene)-[enzyme]-lysine + propane-1,3-diamine

(1c) N-(4-aminobutylidene)-[enzyme]-lysine + [eIF5A-precursor]-lysine $\rightleftharpoons$ N-(4-aminobutylidene)-[eIF5A-precursor]-lysine + [enzyme]-lysine

(1d) N-(4-aminobutylidene)-[eIF5A-precursor]-lysine + NADH + H+ $\rightleftharpoons$ [eIF5A-precursor]-deoxyhypusine + NAD⁺

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

References

1. Wolff, E.C.; Park, M.H.; Folk, J.E. (1990). "Cleavage of spermidine as the first step in deoxyhypusine synthesis. The role of NAD⁺". J. Biol. Chem. 265 (11): 4793–4799. PMID 1690726.
2. Wolff, E.C.; Folk, J.E.; Park, M.H. (1997). "Enzyme-substrate intermediate formation at lysine 329 of human deoxyhypusine synthase". J. Biol. Chem. 272 (25): 15865–15871. doi:10.1074/jbc.272.25.15865. PMID 9188485.
3. Chen, K.Y.; Liu, A.Y.C. (1997). "Biochemistry and function of hypusine formation on eukaryotic initiation factor 5A". Biol. Signals. 6 (3): 105–109. doi:10.1159/000109115. PMID 9285092.
4. Ober, D.; Hartmann, T. (1999). "Deoxyhypusine synthase from tobacco. cDNA isolation, characterization, and bacterial expression of an enzyme with extended substrate specificity". J. Biol. Chem. 274 (45): 32040–32047. doi:10.1074/jbc.274.45.32040. PMID 10542236.
5. Ober, D.; Hartmann, T. (1999). "Homospermidine synthase, the first pathway-specific enzyme of pyrrolizidine alkaloid biosynthesis, evolved from deoxyhypusine synthase". Proc. Natl. Acad. Sci. USA. 96 (26): 14777–14782. Bibcode:1999PNAS...9614777O. doi:10.1073/pnas.96.26.14777. PMC 24724. PMID 10611289.
6. Wolff, E.C.; Park, M.H. (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, E.C.; Wolff, J.; Park, M.H. (2000). "Deoxyhypusine synthase generates and uses bound NADH in a transient hydride transfer mechanism". J. Biol. Chem. 275 (13): 9170–9177. doi:10.1074/jbc.275.13.9170. PMID 10734052.
8. Joe, Y.A.; Wolff, E.C.; Park, M.H. (1995). "Cloning and expression of human deoxyhypusine synthase cDNA: structure-function studies with the recombinant enzyme and mutant proteins". J. Biol. Chem. 270 (38): 22386–22392. doi:10.1074/jbc.270.38.22386. PMID 7673224.
9. Tao, Y.; Chen, K.Y. (1995). "Molecular cloning and functional expression of Neurospora deoxyhypusine synthase cDNA and identification of yeast deoxyhypusine synthase cDNA". J. Biol. Chem. 270 (41): 23984–23987. doi:10.1074/jbc.270.41.23984. PMID 7592594.

External links

• Deoxyhypusine synthase at the US National Library of Medicine Medical Subject Headings (MeSH)