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InterPro: IPR002773 Deoxyhypusine synthase

Protein matchesHelp
UniProtKB
Matches:
508 proteins
AccessionHelp IPR002773 Deoxyhypus_synth
TypeHelp Family
SignaturesHelp
GO Term annotationHelp
Process GO:0008612 peptidyl-lysine modification to hypusine
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

Eukaryotic initiation factor 5A (eIF-5A), now considered to be an elongation factor (see IPR001884), contains an unusual amino acid, hypusine [N epsilon-(4-aminobutyl-2-hydroxy)lysine]. The first step in the post-translational formation of hypusine is catalysed by the enzyme deoxyhypusine synthase (DS) EC:2.5.1.46. The enzyme catalyses the following reaction:

Spermidine + [eIF-5A]-lysine = 1,3-diaminopropane + [eIF-5A]-deoxyhypusine

The modified version of eIF-5A, and DS, are required for eukaryotic cell proliferation [1]. The structure is known for this enzyme [1] in complex with its NAD+ cofactor.

Structural linksHelp
SCOP: c.31.1.1
CATH: 3.40.910.10
Database linksHelp
Enzyme: EC:2.5.1.46
PANDIT: PF01916
Blocks: IPB002773
Pfam Clan: CL0085.10

Taxonomic coverageHelp

Example proteinsHelp
P38791 Deoxyhypusine synthase

P49366 Deoxyhypusine synthase

Q3TXU5 Deoxyhypusine synthase

Q9VSF4 Probable deoxyhypusine synthase

Q9XXJ0 Probable deoxyhypusine synthase

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR002773 Deoxyhypusine synthase
SWISS-MODEL
PDB Chain
ModBase
CATH Domain
SCOP Domain

PublicationsHelp
1. Liao DI, Wolff EC, Park MH, Davies DR.
Crystal structure of the NAD complex of human deoxyhypusine synthase: an enzyme with a ball-and-chain mechanism for blocking the active site.
Structure 6 23-32 1998 [PubMed: 9493264]
http://dx.doi.org/10.1016/S0969-2126(98)00004-5

Additional ReadingHelp
Umland TC, Wolff EC, Park MH, Davies DR.
A new crystal structure of deoxyhypusine synthase reveals the configuration of the active enzyme and of an enzyme.NAD.inhibitor ternary complex.
J. Biol. Chem. 279 2004 28697-705 [PubMed: 15100216]
http://dx.doi.org/10.1074/jbc.M404095200
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InterPro 23.1