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Literature summary extracted from

  • Esipov, R.; Timofeev, V.; Sinitsyna, E.; Tuzova, E.; Esipova, L.; Kostromina, M.; Kuranova, I.; Miroshnikov, A.
    Three-dimensional structure of recombinant adenine phosphoribosyltransferase from thermophilic bacterial strain Thermus thermophilus HB27 (2018), Russ. J. Bioorg. Chem., 44, 504-510 .
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.2.7 gene tth1250, recombinant enzyme expression in Escherichia coli strain BL21(DE3) Thermus thermophilus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.4.2.7 purified recombinant enzyme, crystals grow via capillary counter-diffusion technique, X-ray diffraction structure determination and analysis at 2.5 A resolution, molecular replacement amd modeling Thermus thermophilus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.4.2.7 Mg2+ required 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
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.2.7 recombinant enzyme from Escherichia coli strain BL21(DE3) Thermus thermophilus

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.4.2.7 14
-
 purified recombinant enzyme, pH and temperature not specified in the publication Thermus thermophilus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.2.7 2,6-diaminpurine + 5-phospho-alpha-D-ribose 1-diphosphate
-
 Thermus thermophilus 2,6-diaminpurine 5'-phosphoribosyl nucleotide + diphosphate
-
 r
2.4.2.7 2,6-diaminpurine + 5-phospho-alpha-D-ribose 1-diphosphate
-
 Thermus thermophilus DSM 7039 2,6-diaminpurine 5'-phosphoribosyl nucleotide + diphosphate
-
 r
2.4.2.7 2,6-diaminpurine + 5-phospho-alpha-D-ribose 1-diphosphate
-
 Thermus thermophilus ATCC BAA-163 2,6-diaminpurine 5'-phosphoribosyl nucleotide + diphosphate
-
 r
2.4.2.7 2-chloroadenine + 5-phospho-alpha-D-ribose 1-diphosphate
-
 Thermus thermophilus 2-chloro-AMP + diphosphate
-
 r
2.4.2.7 2-chloroadenine + 5-phospho-alpha-D-ribose 1-diphosphate
-
 Thermus thermophilus DSM 7039 2-chloro-AMP + diphosphate
-
 r
2.4.2.7 2-chloroadenine + 5-phospho-alpha-D-ribose 1-diphosphate
-
 Thermus thermophilus ATCC BAA-163 2-chloro-AMP + diphosphate
-
 r
2.4.2.7 2-fluoroadenine + 5-phospho-alpha-D-ribose 1-diphosphate
-
 Thermus thermophilus 2-fluoro-AMP + diphosphate
-
 r
2.4.2.7 2-fluoroadenine + 5-phospho-alpha-D-ribose 1-diphosphate
-
 Thermus thermophilus DSM 7039 2-fluoro-AMP + diphosphate
-
 r
2.4.2.7 2-fluoroadenine + 5-phospho-alpha-D-ribose 1-diphosphate
-
 Thermus thermophilus ATCC BAA-163 2-fluoro-AMP + diphosphate
-
 r
2.4.2.7 2-methoxyadenine + 5-phospho-alpha-D-ribose 1-diphosphate
-
 Thermus thermophilus 2-methoxyadenosine 5'-monophosphate + diphosphate
-
 r
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 transfer to N9 of adenine 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 transfer to N9 of adenine 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 adenine + 5-phospho-alpha-D-ribose 1-diphosphate transfer to N9 of adenine Thermus thermophilus ATCC BAA-163 AMP + diphosphate
-
 r
2.4.2.7 N1-methoxyadenine + 5-phospho-alpha-D-ribose 1-diphosphate
-
 Thermus thermophilus N1-methoxyadenosine 5'-monophosphate + diphosphate
-
 r

Subunits

EC Number Subunits Comment Organism
2.4.2.7 homodimer secondary structure analysis, at the N-terminal end of the polypeptide chain, the hood domain is located encompassing a beta-sheet made of two antiparallel beta-strands, beta1 and beta2, and a disordered fragment following the beta2 strand, extending to the alpha1 helix Thermus thermophilus
2.4.2.7 More enzyme crystals belonging to the P21 spatial group contain six identical enzyme subunits per asymmetric unit. Subunits are connected with a double axis pairwise and form three dimers (AB, CD, and EF). The polypeptide chain of a TthHB27APRT subunit contains 178 amino acid residues forming ten beta strands and four alpha helices. Enzyme structure analysis and comparisons, e.g. with APRT of TthHB8, overview Thermus thermophilus

Synonyms

EC Number Synonyms Comment Organism
2.4.2.7 APRT
-
 Thermus thermophilus
2.4.2.7 TTH1250 locus name Thermus thermophilus
2.4.2.7 TthAPRT
-
 Thermus thermophilus
2.4.2.7 TthHB27APRT
-
 Thermus thermophilus
2.4.2.7 type I PRT
-
 Thermus thermophilus

General Information

EC Number General Information Comment Organism
2.4.2.7 evolution Thermus thermophilus strain HB27 enzyme TthHB27APRT belongs to the type I phosphoribosyltransferases. These share the alpha/beta type folding of the polypeptide chain and the presence of a specific sequence of 13 amino acid residues involved in binding of diphosphate (PRPP-binding motif), together with a structurally variable subdomain (the so-called, hood domain) involved in base recognition Thermus thermophilus
2.4.2.7 metabolism type I phosphoribosyltransferases play an important role in common and salvage pathways of purine, pyrimidine, and pyrimidine coenzyme synthesis, as well as biosynthesis of histidine and tryptophan in lower organisms Thermus thermophilus
2.4.2.7 additional information structure analysis and comparisons, detailed overview Thermus thermophilus