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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 2O06
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Structure and mechanism of spermidine synthases.
Wu, H., Min, J., Ikeguchi, Y., Zeng, H., Dong, A., Loppnau, P., Pegg, A.E., Plotnikov, A.N.
Biochemistry
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