EC Tree |
2. Transferases |
2.5 Transferring alkyl or aryl groups, other than methyl groups |
2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date) |
ID: | 2.5.1.16 | ||
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Description: | Spermidine synthase. | ||
Alternative Name: |
Putrescine aminopropyltransferase. Aminopropyltransferase. | ||
Prosite: | PDOC01033; | ||
PDB: |
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Cath: | 3.30.160.110; 2.30.140.10; 3.40.50.150; |
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Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.UniProtKB Enzyme Link: | UniProtKB 2.5.1.16 |
BRENDA Enzyme Link: | BRENDA 2.5.1.16 |
KEGG Enzyme Link: | KEGG2.5.1.16 |
BioCyc Enzyme Link: | BioCyc 2.5.1.16 |
ExPASy Enzyme Link: | ExPASy2.5.1.16 |
EC2PDB Enzyme Link: | EC2PDB 2.5.1.16 |
ExplorEnz Enzyme Link: | ExplorEnz 2.5.1.16 |
PRIAM enzyme-specific profiles Link: | PRIAM 2.5.1.16 |
IntEnz Enzyme Link: | IntEnz 2.5.1.16 |
MEDLINE Enzyme Link: | MEDLINE 2.5.1.16 |
RHEA:12721 | putrescine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) + S-methyl-5'-thioadenosine + spermidine |
RULE(radius=1) | [*:1]-[NH2;+0:2].[*:3]-[S+;H0:4](-[*:5])-[CH2;+0:6]-[*:7]>>[*:7]-[CH2;+0:6]-[NH;+0:2]-[*:1].[*:3]-[S;H0;+0:4]-[*:5] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
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Structure and mechanism of spermidine synthases. | Wu H, Min J, Ikeguchi Y, Zeng H, Dong A, Loppnau P, Pegg AE, Plotnikov AN | 2007 Jul 17 | 17585781 |
Crystal structure of Helicobacter pylori spermidine synthase: a Rossmann-like fold with a distinct active site. | Lu PK, Tsai JY, Chien HY, Huang H, Chu CH, Sun YJ | 2007 May 15 | 17357156 |
Structural and mechanistic insights into the action of Plasmodium falciparum spermidine synthase. | Burger PB, Birkholtz LM, Joubert F, Haider N, Walter RD, Louw AI | 2007 Feb 15 | 17196392 |