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Literature summary for 2.4.2.28 extracted from
- Kinetic studies of Drosophila melanogaster methylthioadenosine nucleoside phosphorylase (1981), Int. J. Biochem., 13, 559-564.
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0055 | - |
5'-methylthioadenosine | - |
Drosophila melanogaster |  |
| 13.5 | - |
phosphate | - |
Drosophila melanogaster | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Drosophila melanogaster | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate | ordered bisubstrate biproduct reaction with methylthioadenosine the first substrate to add and adenine the last product to leave the enzyme | Drosophila melanogaster |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 5'-methylthioadenosine + phosphate | - |
Drosophila melanogaster | adenine + 5-methylthio-D-ribose 1-phosphate | - |
? | |
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