Cloned (Comment) | Organism |
---|---|
gene tth1250, recombinant enzyme expression in Escherichia coli strain BL21(DE3) | Thermus thermophilus |
Crystallization (Comment) | Organism |
---|---|
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 | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | 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 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant enzyme from Escherichia coli strain BL21(DE3) | Thermus thermophilus |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
14 | - |
purified recombinant enzyme, pH and temperature not specified in the publication | Thermus thermophilus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2,6-diaminpurine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Thermus thermophilus | 2,6-diaminpurine 5'-phosphoribosyl nucleotide + diphosphate | - |
r | |
2,6-diaminpurine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Thermus thermophilus DSM 7039 | 2,6-diaminpurine 5'-phosphoribosyl nucleotide + diphosphate | - |
r | |
2,6-diaminpurine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Thermus thermophilus ATCC BAA-163 | 2,6-diaminpurine 5'-phosphoribosyl nucleotide + diphosphate | - |
r | |
2-chloroadenine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Thermus thermophilus | 2-chloro-AMP + diphosphate | - |
r | |
2-chloroadenine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Thermus thermophilus DSM 7039 | 2-chloro-AMP + diphosphate | - |
r | |
2-chloroadenine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Thermus thermophilus ATCC BAA-163 | 2-chloro-AMP + diphosphate | - |
r | |
2-fluoroadenine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Thermus thermophilus | 2-fluoro-AMP + diphosphate | - |
r | |
2-fluoroadenine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Thermus thermophilus DSM 7039 | 2-fluoro-AMP + diphosphate | - |
r | |
2-fluoroadenine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Thermus thermophilus ATCC BAA-163 | 2-fluoro-AMP + diphosphate | - |
r | |
2-methoxyadenine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Thermus thermophilus | 2-methoxyadenosine 5'-monophosphate + diphosphate | - |
r | |
adenine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Thermus thermophilus | AMP + diphosphate | - |
r | |
adenine + 5-phospho-alpha-D-ribose 1-diphosphate | transfer to N9 of adenine | 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 | transfer to N9 of adenine | Thermus thermophilus DSM 7039 | AMP + diphosphate | - |
r | |
adenine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Thermus thermophilus ATCC BAA-163 | AMP + diphosphate | - |
r | |
adenine + 5-phospho-alpha-D-ribose 1-diphosphate | transfer to N9 of adenine | Thermus thermophilus ATCC BAA-163 | AMP + diphosphate | - |
r | |
N1-methoxyadenine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
Thermus thermophilus | N1-methoxyadenosine 5'-monophosphate + diphosphate | - |
r |
Subunits | Comment | Organism |
---|---|---|
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 |
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 | Comment | Organism |
---|---|---|
APRT | - |
Thermus thermophilus |
TTH1250 | locus name | Thermus thermophilus |
TthAPRT | - |
Thermus thermophilus |
TthHB27APRT | - |
Thermus thermophilus |
type I PRT | - |
Thermus thermophilus |
General Information | Comment | Organism |
---|---|---|
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 |
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 |
additional information | structure analysis and comparisons, detailed overview | Thermus thermophilus |