Cloned (Comment) | Organism |
---|---|
- |
Mycobacterium tuberculosis |
- |
Campylobacter jejuni |
- |
Lactococcus lactis |
Crystallization (Comment) | Organism |
---|---|
hanging drop vapor diffusion method | Mycobacterium tuberculosis |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
AMP | - |
Campylobacter jejuni | |
AMP | - |
Lactococcus lactis | |
AMP | - |
Mycobacterium tuberculosis | |
L-histidine | - |
Campylobacter jejuni | |
L-histidine | - |
Lactococcus lactis | |
L-histidine | - |
Mycobacterium tuberculosis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required for activity | Mycobacterium tuberculosis | |
Mg2+ | required for activity | Campylobacter jejuni | |
Mg2+ | required for activity | Lactococcus lactis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate | Mycobacterium tuberculosis | - |
ATP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
r | |
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate | Campylobacter jejuni | - |
ATP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
r | |
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate | Lactococcus lactis | - |
ATP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
r | |
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate | Mycobacterium tuberculosis H37Rv | - |
ATP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
r | |
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate | Campylobacter jejuni RM1221 | - |
ATP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Campylobacter jejuni | Q5HSJ4 | - |
- |
Campylobacter jejuni RM1221 | Q5HSJ4 | - |
- |
Lactococcus lactis | Q02129 | - |
- |
Mycobacterium tuberculosis | P9WMN1 | - |
- |
Mycobacterium tuberculosis H37Rv | P9WMN1 | - |
- |
Purification (Comment) | Organism |
---|---|
metal affinity column chromatography | Campylobacter jejuni |
metal affinity column chromatography | Lactococcus lactis |
metal affinity column chromatography and Sephacryl S-200 gel filtration | Mycobacterium tuberculosis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate | - |
Mycobacterium tuberculosis | ATP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
r | |
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate | - |
Campylobacter jejuni | ATP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
r | |
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate | - |
Lactococcus lactis | ATP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
r | |
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate | - |
Mycobacterium tuberculosis H37Rv | ATP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
r | |
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate | - |
Campylobacter jejuni RM1221 | ATP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
r |
Subunits | Comment | Organism |
---|---|---|
homohexamer or heterooctamer | the long-form enzyme is a homohexamer with each chain comprised of the catalytic core, and a covalent C-terminal regulatory domain containing the allosteric binding site for histidine. The short-form is a hetero-octamer containing two catalytic dimers that associate with a second discrete domain (denoted HisZ) for allosteric regulation by the binding of histidine | Mycobacterium tuberculosis |
homohexamer or heterooctamer | the long-form enzyme is a homohexamer with each chain comprised of the catalytic core, and a covalent C-terminal regulatory domain containing the allosteric binding site for histidine. The short-form is a hetero-octamer containing two catalytic dimers that associate with a second discrete domain (denoted HisZ) for allosteric regulation by the binding of histidine | Campylobacter jejuni |
homohexamer or heterooctamer | the long-form enzyme is a homohexamer with each chain comprised of the catalytic core, and a covalent C-terminal regulatory domain containing the allosteric binding site for histidine. The short-form is a hetero-octamer containing two catalytic dimers that associate with a second discrete domain (denoted HisZ) for allosteric regulation by the binding of histidine | Lactococcus lactis |
Synonyms | Comment | Organism |
---|---|---|
adenosine triphosphate phosphoribosyltransferase | - |
Mycobacterium tuberculosis |
adenosine triphosphate phosphoribosyltransferase | - |
Campylobacter jejuni |
adenosine triphosphate phosphoribosyltransferase | - |
Lactococcus lactis |
ATP-PRT | - |
Mycobacterium tuberculosis |
ATP-PRT | - |
Campylobacter jejuni |
ATP-PRT | - |
Lactococcus lactis |