U.S. flag

An official website of the United States government

Format
Items per page
Sort by

Send to:

Choose Destination

Links from Protein

Items: 7

1.
new record, indexing in progress
Family Accession:
2.

deoxyhypusine synthase family protein

Eukaryotic initiation factor 5A (eIF-5A) 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:1.1.1.249. The modified version of eIF-5A, and DS, are required for eukaryotic cell proliferation [1]. [1]. 9493264. Crystal structure of the NAD complex of human deoxyhypusine. synthase: an enzyme with a ball-and-chain mechanism for blocking. the active site.. Liao DI, Wolff EC, Park MH, Davies DR;. Structure 1998;6:23-32. (from Pfam)

GO Terms:
Biological Process:
peptidyl-lysine modification to peptidyl-hypusine (GO:0008612)
Date:
2024-08-14
Family Accession:
NF014027.5
Method:
HMM
3.
new record, indexing in progress
Family Accession:
4.
new record, indexing in progress
Family Accession:
5.

deoxyhypusine synthase family protein

deoxyhypusine synthase family protein similar to deoxyhypusine synthase-like protein

Date:
2017-03-02
Family Accession:
10012102
Method:
Sparcle
6.

deoxyhypusine synthase

Transforms a conserved lysine residue of initiation factor 5A into deoxyhypusine

Date:
2020-10-26
Family Accession:
NF003052.0
Method:
HMM
7.

deoxyhypusine synthase

Deoxyhypusine synthase (DHS), as understood from eukaryotes, catalyzes the transfer of a 4-aminobutyl moiety from spermidine to a lysine residue of translation factor eIF5A. The deoxyhypusine modification is subsequently to hypusine by deoxyhypusine hydroxylase (DOHH). In the archaea, DOHH per se is not found, and aIF5A modification varies, deoxyhypusine in Haloferax volcanii, but hypusine in Sulfolobus solfataricus. The donor molecule for the initial modification of the aIF5A lysine appears to vary as well in the archaea, and in Haloferax volcanii appears not to be spermidine. Further characterization of functionally distinct subsets of DHS family aIF5A modification enzymes will be required.

GO Terms:
Biological Process:
peptidyl-lysine modification to peptidyl-hypusine (GO:0008612)
Date:
2022-07-07
Family Accession:
TIGR00321.1
Method:
HMM
Format
Items per page
Sort by

Send to:

Choose Destination

Supplemental Content

Find related data

Recent activity

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

See more...
Support Center