CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.30 | Roll |
|
2.30.140 | Spermidine Synthase; Chain: A, domain 2 |
|
2.30.140.10 | Spermidine synthase, tetramerisation domain |
Domain Context
CATH Clusters
| Superfamily | Spermidine synthase, tetramerisation domain |
| Functional Family | Polyamine aminopropyltransferase |
Enzyme Information
| 2.5.1.79 |
Thermospermine synthase.
based on mapping to UniProt P09158
S-adenosyl 3-(methylthio)propylamine + spermidine = S-methyl- 5'-thioadenosine + thermospermine + H(+).
-!- This enzyme is required for correct xylem specification through regulation of the lifetime of the xylem elements.
|
| 2.5.1.16 |
Spermidine synthase.
based on mapping to UniProt P09158
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.
|
| 2.5.1.22 |
Spermine synthase.
based on mapping to UniProt P09158
S-adenosyl 3-(methylthio)propylamine + spermidine = S-methyl- 5'-thioadenosine + spermine.
-!- The enzyme from mammalia is highly specific for spermidine, cf. EC 2.5.1.16 and EC 2.5.1.23.
|
| 2.5.1.- |
Transferring alkyl or aryl groups, other than methyl groups.
based on mapping to UniProt P09158
|
UniProtKB Entries (1)
| P09158 |
SPEE_ECOLI
Escherichia coli K-12
Polyamine aminopropyltransferase
|
PDB Structure
| PDB | 3O4F |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
The crystal structure of Escherichia coli spermidine synthase SpeE reveals a unique substrate-binding pocket
J.Struct.Biol.
|
