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] catalyses the following chemical reaction
[eIF5A-precursor]-lysine + spermidine
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{\displaystyle \rightleftharpoons }
(1a) spermidine + NAD+
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{\displaystyle \rightleftharpoons }
(1b) dehydrospermidine + [enzyme]-lysine
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{\displaystyle \rightleftharpoons }
(1c) N-(4-aminobutylidene)-[enzyme]-lysine + [eIF5A-precursor]-lysine
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{\displaystyle \rightleftharpoons }
(1d) N-(4-aminobutylidene)-[eIF5A-precursor]-lysine + NADH + H+
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{\displaystyle \rightleftharpoons }
+ The eukaryotic initiation factor eIF5A contains a hypusine residue that is essential for activity.
References
^ 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 . ^ 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 . ^ 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 . ^ 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 . ^ 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 . ^ 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 . ^ 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 . ^ 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 . ^ 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
Activity Regulation Classification Kinetics Types
