Crystallization (Comment) | Organism |
---|---|
in complex with 5'-methylthioadenosine and spermidine and with 5'-methylthioadenosine and spermine. Enzyme is a dimer of two identical subunits. Each monomer has three domains, a C-terminal domain, which contains the active site and is similar in structure to spermidine synthase, a central domain made up of four beta-strands, and an N-terminal domain with remarkable structural similarity to S-adenosylmethionine decarboxylase | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
D201A | 40000fold decrease in ratio kcat/Km value | Homo sapiens |
D201N | 40000fold decrease in ratio kcat/Km value | Homo sapiens |
D276N | 250000fold decrease in ratio kcat/Km value | Homo sapiens |
E353Q | 1000fold decrease in ratio kcat/Km value | Homo sapiens |
additional information | deletion of the N-terminal domain leads to a complete loss of spermine synthase activity | Homo sapiens |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | ratio of kcat/Km value of wild-type is 40000 for substrate spermidine, and 71000000 for S-adenosyl-L-methioninamine, respectively | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P52788 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
S-adenosyl-L-methioninamine + spermidine | - |
Homo sapiens | 5'-methylthioadenosine + spermine | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0015 | - |
spermidine | mutant D201A, pH 7.5, 37°C | Homo sapiens | |
0.0015 | - |
spermidine | mutant D201N, pH 7.5, 37°C | Homo sapiens | |
0.0022 | - |
spermidine | mutant D276N, pH 7.5, 37°C | Homo sapiens | |
0.64 | - |
spermidine | mutant E353Q, pH 7.5, 37°C | Homo sapiens | |
32 | - |
spermidine | wild-type, pH 7.5, 37°C | Homo sapiens |