Hypusine

Title: Hypusine
CAS Registry Number: 34994-11-1
CAS Name: N6-[(2R)-4-Amino-2-hydroxybutyl]-L-lysine
Additional Names: (2S,9R)-2,11-diamino-9-hydroxy-7-azaundecanoic acid; N6-(4-amino-2-hydroxybutyl)-2,6-diaminohexanoic acid
Molecular Formula: C10H23N3O3
Molecular Weight: 233.31
Percent Composition: C 51.48%, H 9.94%, N 18.01%, O 20.57%
Literature References: Naturally occurring L-amino acid formed by the post-translational modification of lysine. Name coined to indicate the condensation product of hydroxyputrescine with lysine. Isoln: T. Shiba et al., Biochim. Biophys. Acta 244, 523 (1971); from archaebacteria: H. Schümann, F. Klink, Syst. Appl. Microbiol. 11, 103 (1989). In eukaryotes occurs only at a single position in one protein, eukaryotic protein synthesis initiation factor 5A, (eIF-5A, formerly eIF-4D): M. H. Park et al., Proc. Natl. Acad. Sci. USA 78, 2869 (1981); H. L. Cooper et al., ibid. 80, 1854 (1983). Biosynthesis: M. H. Park et al., J. Biol. Chem. 257, 7217 (1982); M. H. Park et al., ibid. 259, 12123 (1984). Synthesis and stereochemistry: T. Shiba et al., Bull. Chem. Soc. Jpn. 55, 899 (1982). Total synthesis: C. M. Tice, B. Ganem, J. Org. Chem. 48, 5043, 5048 (1983); R. J. Bergeron et al., ibid. 58, 6804 (1993). Biological significance in eukaryotes: J. W. B. Hershey et al., Biochim. Biophys. Acta 1050, 160 (1990). HPLC determn in eukaryotic samples: S. Beninati et al., Anal. Biochem. 184, 16 (1990). Chromatographic determn in archaebacteria: D. Bartig, F. Klink, J. Chromatogr. 606, 43 (1992). Review of biological significance: M. H. Park et al., Trends Biochem. Sci. 18, 475-479 (1993).
Derivative Type: Dihydrochloride
CAS Registry Number: 82310-93-8
Molecular Formula: C10H23N3O3.2HCl
Molecular Weight: 306.23
Percent Composition: C 39.22%, H 8.23%, N 13.72%, O 15.67%, Cl 23.15%
Properties: White crystals, mp 239-241° (dec). [a]D23 +8.3° (c = 0.96 in 6M HCl).
Melting point: mp 239-241° (dec)
Optical Rotation: [a]D23 +8.3° (c = 0.96 in 6M HCl)
IACFT Ibafloxacin Ibandronic Acid Iberiotoxin Ibopamine

Hypusine
Stereo, partially condensed, skeletal formula of hypusine ((2S)-2-amino, -6-{[(2S)-2-hydroxybutyl]amino})
Identifiers
CAS number 34994-11-1 (2S)-2-Amino, -6-{[(2R)-2-hydroxybutyl]amino} YesY
PubChem 21878228, 15930878 (2S)-2-Amino, 10922432 (2S)-2-Amino, -6-{[(2R)-2-hydroxybutyl]amino}, 65396 (2S)-2-Amino, -6-{[(2S)-2-hydroxybutyl]amino}
ChemSpider 10624726 N, 16740599 (2S)-2-Amino YesY, 9097677 (2S)-2-Amino, -6-{[(2R)-2-hydroxybutyl]amino} YesY, 58862 (2S)-2-Amino, -6-{[(2S)-2-hydroxybutyl]amino} YesY
MeSH hypusine
ChEBI CHEBI:21858 N
Jmol-3D images Image 1
Image 2
Properties
Molecular formula C10H23N3O3
Molar mass 233.31 g mol−1
Related compounds
Related alkanoic acids
  • 4-(γ-Glutamylamino)butanoic acid
  • Saccharopine
Related compounds Palmitoylethanolamide
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Except where noted otherwise, data are given for materials in their standard state (at 25 °C (77 °F), 100 kPa)
Infobox references

Hypusine is an unusual amino acid found in all eukaryotes and in some archaea, but not in bacteria. The only known protein containing hypusine is eukaryotic translation initiation factor 5A (eIF5A) and a similar protein found in archaebacteria.[2] In humans, two isoforms of eIF-5A have been described: eIF5A-1 and eIF5A-2. They are encoded by two different genes EIF5A and EIF5A2. The protein is involved in protein biosynthesis and promotes the formation of the first peptide bond. The region surrounding the hypusine residue is highly conserved and is essential to the function of eIF5A.[3] Thus, hypusine and eIF-5A appear to be vital for the viability and proliferation of eukaryotic cells.

Hypusine is formed in eIF-5A by post-translational modification of one of the lysyl residues. There are two reactions and two enzymes involved:

  • 1. Deoxyhypusine synthase catalyzes the cleavage of the polyamine spermidine and transfer of its 4-aminobutyl moiety to the ε-amino group of one specific lysine residue of the eIF-5A precursor to form deoxyhypusine and 1,3-diaminopropane.
  • 2. Deoxyhypusine hydroxylase mediates the formation of hypusine by addition of a hydroxyl group to the deoxyhypusine residue.

An excess of hypusine was found in the urine of children and patients with familial hyperlysinemia.

Hypusine was first isolated from bovine brain by Japanese scientists Shiba et al. in 1971.[4] The name hypusine indicates that the molecule comprises moieties of hydroxyputrescine and lysine.