Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

2.5.1.46: deoxyhypusine synthase

This is an abbreviated version!
For detailed information about deoxyhypusine synthase, go to the full flat file.

Word Map on EC 2.5.1.46

Reaction

dehydrospermidine
+
[enzyme]-lysine
=
N-(4-aminobutylidene)-[enzyme]-lysine
+
propane-1,3-diamine

Synonyms

CpDHS, deoxyhypusine synthase, deoxyhypusine synthase (Caulobacter crescentus gene CC0359), deoxyhypusine synthase (Halobacterium strain NRC-1 gene dhs), deoxyhypusine synthase (human clone 30649 gene DHPS subunit reduced), deoxyhypusine synthase (Nicotiana tabacum gene DHS1), deoxyhypusine synthase (Senecio vernalis gene DHS1), deoxyhypusinesynthase, DHPS, DHS, DHS1, DHS2, DHS20, DHS34, DHSc, DHSp, DHYS, Dys1, Dys1p, EC 1.1.1.249, HVO 2297, PF3D7_1412600, speY, synthase, deoxyhypusine, TbDHSc, TbDHSp

ECTree

     2 Transferases
         2.5 Transferring alkyl or aryl groups, other than methyl groups
             2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
                2.5.1.46 deoxyhypusine synthase

Crystallization

Crystallization on EC 2.5.1.46 - deoxyhypusine synthase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
at 2.2 A a new form II crystal of the deoxyhypusine synthase:NAD holoenzyme is grown at low ionic strength and pH 8.0, near the optimal pH for enzymatic activity
in complex with inhibitors 6-bromo-N-(1H-indol-4-yl)-1-benzothiophene-2-carboxamide and N''-guanyl-1,7-diaminoheptane. Presence of 6-bromo-N-(1H-indol-4-yl)-1-benzothiophene-2-carboxamide induces a dramatic conformational change in DHPS
structures of the apoprotein, as well as ligand-bound states at 1.41 to 1.69 A resolution. Polyamines namely spermine and putrescine bind DHS in a similar manner as spermidine. Spermine may to some extent serve as an alternative DHS substrate. No conformational changes occur in the DHS structure upon spermidine binding. A conserved ball-and-chain motif is indispensable to assembling a functional DHS tetramer
vapor diffusion in hanging drops, crystal structure of the enzyme-NAD complex at 2.2 A resolution
-
heterotetramer, to 3.5 A resolution. The activity is dependent on heterotetramer formation between paralogs DHSc and DHSp. The X-ray structure of DHS shows a single functional shared active site formed at the DHSc/DHSp heterodimer interface. Deficiencies in one subunit are complemented by the other