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Literature summary for 2.4.2.7 extracted from
- Glutamate dehydrogenase from Thermus thermophilus is activated by AMP and leucine as a complex with catalytically inactive adenine phosphoribosyltransferase homolog (2019), J. Bacteriol., 201, e00710-18 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene TT_C1249, sequence comparisons, recombinant coexpression of N-terminally His-tagged ARTh with GDH in Escherichia coli | Thermus thermophilus |
| gene TT_C1250, sequence comparisons | Thermus thermophilus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | construction of an aprth knockout strain (Tt27DELTAAPRTh) and an aprth-overexpressing strain (Tt27NStHisAPRTh) of Thermus thermophilus in minimal medium. The Tt27DELTAAPRTh strain exhibits delayed growth and requires approximately 36 h to reach the early stationary phase, whereas the wild-type strain reached this phase after 21 h of cultivation. The Tt27NStHisAPRTh strain exhibits better growth than even the wild-type strain | Thermus thermophilus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| AMP + diphosphate | Thermus thermophilus | - |
adenine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
r |  |
| AMP + diphosphate | Thermus thermophilus DSM 7039 | - |
adenine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
r | |
| AMP + diphosphate | Thermus thermophilus ATCC BAA-163 | - |
adenine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermus thermophilus | Q72I82 | - |
- |
| Thermus thermophilus | Q72I83 | - |
- |
| Thermus thermophilus ATCC BAA-163 | Q72I82 | - |
- |
| Thermus thermophilus ATCC BAA-163 | Q72I83 | - |
- |
| Thermus thermophilus DSM 7039 | Q72I82 | - |
- |
| Thermus thermophilus DSM 7039 | Q72I83 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| copurification of N-terminally His-tagged ARTh and GDH from Escherichia coli | Thermus thermophilus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| AMP + diphosphate | - |
Thermus thermophilus | adenine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
r | |
| AMP + diphosphate | - |
Thermus thermophilus DSM 7039 | adenine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
r | |
| AMP + diphosphate | - |
Thermus thermophilus ATCC BAA-163 | adenine + 5-phospho-alpha-D-ribose 1-diphosphate | - |
r | |
| additional information | the enzyme APRT is specific for adenine, very poor activity with guanine, hypoxanthine, and xanthine | Thermus thermophilus | ? | - |
- |
|
| additional information | the enzyme encoded by gene TT_C1249 exhibits no detectable activity toward adenine, guanine, hypoxanthine, or xanthine. TTC1249 is a homologue of APRT (APRTh). Lack of activity of APRTh may be due to the replacement of the residues involved in binding the monophosphate of nucleotide | Thermus thermophilus | ? | - |
- |
|
| additional information | the enzyme APRT is specific for adenine, very poor activity with guanine, hypoxanthine, and xanthine | Thermus thermophilus DSM 7039 | ? | - |
- |
|
| additional information | the enzyme encoded by gene TT_C1249 exhibits no detectable activity toward adenine, guanine, hypoxanthine, or xanthine. TTC1249 is a homologue of APRT (APRTh). Lack of activity of APRTh may be due to the replacement of the residues involved in binding the monophosphate of nucleotide | Thermus thermophilus DSM 7039 | ? | - |
- |
|
| additional information | the enzyme APRT is specific for adenine, very poor activity with guanine, hypoxanthine, and xanthine | Thermus thermophilus ATCC BAA-163 | ? | - |
- |
|
| additional information | the enzyme encoded by gene TT_C1249 exhibits no detectable activity toward adenine, guanine, hypoxanthine, or xanthine. TTC1249 is a homologue of APRT (APRTh). Lack of activity of APRTh may be due to the replacement of the residues involved in binding the monophosphate of nucleotide | Thermus thermophilus ATCC BAA-163 | ? | - |
- |
|
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| APRT | - |
Thermus thermophilus |
| APRTh | - |
Thermus thermophilus |
| TTC1249 | - |
Thermus thermophilus |
| TTC1250 | - |
Thermus thermophilus |
| TT_C1249 | - |
Thermus thermophilus |
| TT_C1250 | - |
Thermus thermophilus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the TTC1250 gene encoding APRT, has 41% amino acid sequence identity to gene TTC1249 encoding APRTh, an catalytically inactve APRT homologue | Thermus thermophilus |
| evolution | the TTC1250 gene, which also encodes APRT, has 41% amino acid sequence identity to gene TTC1249 encoding APRTh | Thermus thermophilus |
| physiological function | enzyme adenine phosphoribosyltransferase homologue occurs in complex with Thermus thermophilus glutamate dehydrogenase. APRTh mediates the allosteric activation of GDH by AMP, but shows no adenine phosphoribosyltransferase activity. Presence of complicated regulatory mechanisms of GDH mediated by multiple compounds to control the carbonnitrogen balance in bacterial cells. APRTh functions in the cell and supports the optimal growth of Thermus thermophilus in minimal medium | Thermus thermophilus |
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