Literature summary for 2.5.1.46 extracted from

Park, J.; Dias, C.; Lee, S.; Valentini, S.; Sokabe, M.; Fraser, C.; Park, M.
Production of active recombinant eIF5A: Reconstitution in E. coli of eukaryotic hypusine modification of eIF5A by its coexpression with modifying enzymes (2011), Protein Eng. Des. Sel., 24, 301-309.

Search for more literature for 2.5.1.46

Cloned(Commentary)

Cloned (Comment)	Organism
DHS DNA and amino acid seuence determination and analysis, functional coexpression with human deoxyhypusine hydroxylase and human eukaryotic translation initiation factor 5A in Escherichia coli strain BL21(DE3)pLys that produces eIF5A(Hpu), overview	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
[eIF5A-precursor]-lysine + spermidine	Homo sapiens	-	[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
[eIF5A-precursor]-lysine + spermidine	-	Homo sapiens	[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine	-	?

Synonyms

Synonyms	Comment	Organism
DHS	-	Homo sapiens

General Information

General Information	Comment	Organism
metabolism	deoxyhypusine synthase catalyzes a step in hypusine sythesis, a unique mmoified lysine derivative of eukaryotic translation initiation factor 5A, eIF5A	Homo sapiens
physiological function	eukaryotic translation initiation factor 5A, eIF5A, is a small acidic protein and the only cellular protein that contains the unique modified lysine, hypusine [N1-(4-amino-2-hydroxybutyl)lysine]. Hypusine is formed by the post-translational modification of one specific lysine residue of the eIF5A precursor, eIF5A(Lys), in two consecutive enzymatic steps. The first enzyme, deoxyhypusine synthase, DHS, catalyzes the transfer of the aminobutyl moiety from the polyamine spermidine to form an intermediate, deoxyhypusine [N1-(4-aminobutyl)lysine] residue, which is subsequently hydroxylated by deoxyhypusine hydroxylase	Homo sapiens

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Release 2023.1 (January 2023)