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Literature summary for 2.5.1.16 extracted from

  • Sekula, B.; Dauter, Z.
    Spermidine synthase (SPDS) undergoes concerted structural rearrangements upon ligand binding - a case study of the two SPDS isoforms from Arabidopsis thaliana (2019), Front. Plant Sci., 10, 555 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.5.1.16

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Arabidopsis thaliana

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting drop method. Crystallographic date show in detail the structural rearrangements of the enzyme that are required to stabilize ligands within the active site Arabidopsis thaliana

Inhibitors

Inhibitors Comment Organism Structure
Cyclohexylamine competitive inhibitor. The inhibitor occupies the polyamine binding site of the enzyme where it binds at the bottom of the active site with the amine group placed analogously to the substrate; competitive inhibitor. The inhibitor occupies the polyamine binding site of the enzyme where it is binds at the bottom of the active site with the amine group placed analogously to the substrate Arabidopsis thaliana

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana O48661
-
-
Arabidopsis thaliana Q9ZUB3
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Arabidopsis thaliana

Subunits

Subunits Comment Organism
dimer
-
 Arabidopsis thaliana

Synonyms

Synonyms Comment Organism
AtSPDS1
-
 Arabidopsis thaliana
AtSPDS2
-
 Arabidopsis thaliana
SPDS
-
 Arabidopsis thaliana

General Information

General Information Comment Organism
metabolism the enzyme catalyzes the production of the linear triamine, spermidine, from putrescine Arabidopsis thaliana