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Literature summary extracted from

  • Zayats, E.A.; Timofeev, V.I.; Kostromina, M.A.; Esipov, R.S.
    An explanation for the narrow carbohydrate substrate specificity of adenine phosphoribosyltransferase from Thermus thermophilus from the model of the enzyme, substrate, and magnesium cation cofactor complex (2019), J. Biomol. Struct. Dyn., 37, 4460-4464 .
    View publication on PubMed

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.4.2.7 Mg2+ required, enzyme binding structure, overview Thermus thermophilus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.2.7 adenine + 5-phospho-alpha-D-ribose 1-diphosphate Thermus thermophilus
-
 AMP + diphosphate
-
 r
2.4.2.7 adenine + 5-phospho-alpha-D-ribose 1-diphosphate Thermus thermophilus DSM 7039
-
 AMP + diphosphate
-
 r
2.4.2.7 adenine + 5-phospho-alpha-D-ribose 1-diphosphate Thermus thermophilus ATCC BAA-163
-
 AMP + diphosphate
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.4.2.7 Thermus thermophilus Q72I82
-
-
2.4.2.7 Thermus thermophilus ATCC BAA-163 Q72I82
-
-
2.4.2.7 Thermus thermophilus DSM 7039 Q72I82
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.2.7 adenine + 5-phospho-alpha-D-ribose 1-diphosphate
-
 Thermus thermophilus AMP + diphosphate
-
 r
2.4.2.7 adenine + 5-phospho-alpha-D-ribose 1-diphosphate
-
 Thermus thermophilus DSM 7039 AMP + diphosphate
-
 r
2.4.2.7 adenine + 5-phospho-alpha-D-ribose 1-diphosphate
-
 Thermus thermophilus ATCC BAA-163 AMP + diphosphate
-
 r
2.4.2.7 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 ?
-
-
2.4.2.7 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 ?
-
-
2.4.2.7 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

EC Number Synonyms Comment Organism
2.4.2.7 APRT
-
 Thermus thermophilus
2.4.2.7 TT_C1250
-
 Thermus thermophilus

General Information

EC Number General Information Comment Organism
2.4.2.7 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
2.4.2.7 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
2.4.2.7 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