Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required, enzyme binding structure, overview | Thermus thermophilus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
adenine + 5-phospho-alpha-D-ribose 1-diphosphate | Thermus thermophilus | - |
AMP + diphosphate | - |
r | |
adenine + 5-phospho-alpha-D-ribose 1-diphosphate | Thermus thermophilus DSM 7039 | - |
AMP + diphosphate | - |
r | |
adenine + 5-phospho-alpha-D-ribose 1-diphosphate | Thermus thermophilus ATCC BAA-163 | - |
AMP + diphosphate | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermus thermophilus | Q72I82 | - |
- |
Thermus thermophilus ATCC BAA-163 | Q72I82 | - |
- |
Thermus thermophilus DSM 7039 | Q72I82 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
adenine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Thermus thermophilus | AMP + diphosphate | - |
r | |
adenine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Thermus thermophilus DSM 7039 | AMP + diphosphate | - |
r | |
adenine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Thermus thermophilus ATCC BAA-163 | AMP + diphosphate | - |
r | |
additional information | APRT from Thermus thermophilus is known to have broad specificity in relation to adenine analogues, while it shows no significant catalytic activity if stereoisomers of PRPP are used as a substrate, narrow PRPP analogue specificity. One of the key factors determining the substrate specificity of an enzyme is its structure and the conformation of its active site in particular. Enzyme ligand interaction analysis | Thermus thermophilus | ? | - |
- |
|
additional information | APRT from Thermus thermophilus is known to have broad specificity in relation to adenine analogues, while it shows no significant catalytic activity if stereoisomers of PRPP are used as a substrate, narrow PRPP analogue specificity. One of the key factors determining the substrate specificity of an enzyme is its structure and the conformation of its active site in particular. Enzyme ligand interaction analysis | Thermus thermophilus DSM 7039 | ? | - |
- |
|
additional information | APRT from Thermus thermophilus is known to have broad specificity in relation to adenine analogues, while it shows no significant catalytic activity if stereoisomers of PRPP are used as a substrate, narrow PRPP analogue specificity. One of the key factors determining the substrate specificity of an enzyme is its structure and the conformation of its active site in particular. Enzyme ligand interaction analysis | Thermus thermophilus ATCC BAA-163 | ? | - |
- |
Synonyms | Comment | Organism |
---|---|---|
APRT | - |
Thermus thermophilus |
TT_C1250 | - |
Thermus thermophilus |
General Information | Comment | Organism |
---|---|---|
evolution | adenine phosphoribosyltransferase (APRT) from the thermophilic eubacteria Thermus thermophilus belongs to the type I phosphorybosyltransferase protein family on the basis of its structure and catalytic activity | Thermus thermophilus |
metabolism | APRT from Thermus thermophilus is a member of purine nucleotide processing methabolical pathways and can be used as a key component of an nucleotide synthesis enzymatic cascade that uses only pentose carbohydrates, nitrogenous bases and ATP as substrates | Thermus thermophilus |
additional information | modeling of the model of the enzyme, substrate and magnesium cation co-factor complex and structure-function relationship analysis, X-ray crystallographic and NMR structure analysis, overview. In silico modeling of protein-ligand interaction by molecular docking via simulations of molecular dynamic, modeling of the APRT-PRPP-Mg2+ enzyme complex, homology modeling using the APRT structure from Homo sapiens (PDB code 1ZN7) | Thermus thermophilus |