From Wikipedia, the free encyclopedia
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
⇌
{\displaystyle \rightleftharpoons }
[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine (overall reaction)
(1a) spermidine + NAD+
⇌
{\displaystyle \rightleftharpoons }
dehydrospermidine + NADH
(1b)
dehydrospermidine + [enzyme]-lysine
⇌
{\displaystyle \rightleftharpoons }
N-(4-aminobutylidene)-[enzyme]-lysine + propane-1,3-diamine
(1c) N-(4-aminobutylidene)-[enzyme]-lysine + [eIF5A-precursor]-lysine
⇌
{\displaystyle \rightleftharpoons }
N-(4-aminobutylidene)-[eIF5A-precursor]-lysine + [enzyme]-lysine
(1d) N-(4-aminobutylidene)-[eIF5A-precursor]-lysine + NADH + H+
⇌
{\displaystyle \rightleftharpoons }
[eIF5A-precursor]-deoxyhypusine + NAD+
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