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 Q5SK28
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.
|
| 2.5.1.126 |
Norspermine synthase.
based on mapping to UniProt Q5SK28
S-adenosyl 3-(methylthio)propylamine + norspermidine = S-methyl- 5'-thioadenosine + norspermine.
-!- The enzyme, characterized from the thermophilic archaeon Pyrobaculum aerophilum, can also synthesize norspermidine from propane-1,3- diamine and thermospermine from spermidine (with lower activity). -!- The long-chain polyamines stabilize double-stranded DNA at high temperatures. -!- In contrast to EC 2.5.1.127, this enzyme does not accept norspermine as a substrate.
|
| 2.5.1.16 |
Spermidine synthase.
based on mapping to UniProt Q5SK28
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 Q5SK28
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.
|
| 2.5.1.104 |
N(1)-aminopropylagmatine synthase.
based on mapping to UniProt Q5SK28
S-adenosylmethioninamine + agmatine = S-methyl-5'-thioadenosine + N(1)- (3-aminopropyl)agmatine.
-!- The enzyme is involved in the biosynthesis of spermidine from agmatine in some archaea and bacteria. -!- The enzyme from the Gram-negative bacterium Thermus thermophilus accepts agmatine, spermidine and norspermidine with similar catalytic efficiency. -!- The enzymes from the archaea Pyrococcus furiosus and Thermococcus kodakarensis prefer agmatine, but can utilize cadaverine, putrescine and propane-1,3-diamine with much lower catalytic efficiency. -!- Cf. EC 2.5.1.16 and EC 2.5.1.23.
|
UniProtKB Entries (1)
| Q5SK28 |
SPEE_THET8
Thermus thermophilus HB8
Polyamine aminopropyltransferase
|
PDB Structure
| PDB | 3ANX |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystal structures and enzymatic properties of a triamine/agmatine aminopropyltransferase from Thermus thermophilus
J.Mol.Biol.
|
