Literature summary for 2.5.1.46 extracted from

Wator, E.; Wilk, P.; Grudnik, P.
Half way to hypusine-structural basis for substrate recognition by human deoxyhypusine synthase (2020), Biomolecules, 10, 522 .

Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Homo sapiens

Crystallization (Comment)

Organism

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

Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
additional information	during purification and crystallization, residue C177 is is covalently modified to a 2-mercaptoethanol adduct	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P49366	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
additional information	no substrates: putrecine, lysine	Homo sapiens	?	-	-
[eIF5A-precursor]-lysine + spermidine	overall reaction	Homo sapiens	[eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine	-	?
[eIF5A-precursor]-lysine + spermine	-	Homo sapiens	?	-	?

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Release 2023.1 (January 2023)