CATH Classification

Domain Context

CATH Clusters

Superfamily Spermidine synthase, tetramerisation domain
Functional Family SPE3p Spermidine synthase

Enzyme Information

2.5.1.16
Spermidine synthase.
based on mapping to UniProt P19623
S-adenosyl 3-(methylthio)propylamine + putrescine = 5'-S-methyl- 5'-thioadenosine + spermidine.
-!- The enzymes from the plant Glycine max and from mammalia are highly specific for putrescine as the amine acceptor. -!- The enzymes from the bacteria Escherichia coli and Thermotoga maritima prefer putrescine but are more tolerant toward other amine acceptors, such as spermidine and cadaverine. -!- Cf. EC 2.5.1.22 and EC 2.5.1.23.

UniProtKB Entries (1)

P19623
SPEE_HUMAN
Homo sapiens
Spermidine synthase

PDB Structure

PDB 3RW9
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Binding and inhibition of human spermidine synthase by decarboxylated S-adenosylhomocysteine.
Seckute, J., McCloskey, D.E., Thomas, H.J., Secrist, J.A., Pegg, A.E., Ealick, S.E.
Protein Sci.