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Literature summary extracted from

  • Moggre, G.J.; Poulin, M.B.; Tyler, P.C.; Schramm, V.L.; Parker, E.J.
    Transition state analysis of adenosine triphosphate phosphoribosyltransferase (2017), ACS Chem. Biol., 12, 2662-2670 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.2.17
-
Mycobacterium tuberculosis
2.4.2.17
-
Campylobacter jejuni
2.4.2.17
-
Lactococcus lactis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.4.2.17 hanging drop vapor diffusion method Mycobacterium tuberculosis

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.2.17 AMP
-
Campylobacter jejuni
2.4.2.17 AMP
-
Lactococcus lactis
2.4.2.17 AMP
-
Mycobacterium tuberculosis
2.4.2.17 L-histidine
-
Campylobacter jejuni
2.4.2.17 L-histidine
-
Lactococcus lactis
2.4.2.17 L-histidine
-
Mycobacterium tuberculosis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.4.2.17 Mg2+ required for activity Mycobacterium tuberculosis
2.4.2.17 Mg2+ required for activity Campylobacter jejuni
2.4.2.17 Mg2+ required for activity Lactococcus lactis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.2.17 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate Mycobacterium tuberculosis
-
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
r
2.4.2.17 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate Campylobacter jejuni
-
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
r
2.4.2.17 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate Lactococcus lactis
-
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
r
2.4.2.17 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate Mycobacterium tuberculosis H37Rv
-
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
r
2.4.2.17 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate Campylobacter jejuni RM1221
-
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
r

Organism

EC Number Organism UniProt Comment Textmining
2.4.2.17 Campylobacter jejuni Q5HSJ4
-
-
2.4.2.17 Campylobacter jejuni RM1221 Q5HSJ4
-
-
2.4.2.17 Lactococcus lactis Q02129
-
-
2.4.2.17 Mycobacterium tuberculosis P9WMN1
-
-
2.4.2.17 Mycobacterium tuberculosis H37Rv P9WMN1
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.2.17 metal affinity column chromatography Campylobacter jejuni
2.4.2.17 metal affinity column chromatography Lactococcus lactis
2.4.2.17 metal affinity column chromatography and Sephacryl S-200 gel filtration Mycobacterium tuberculosis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.2.17 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
Mycobacterium tuberculosis ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
r
2.4.2.17 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
Campylobacter jejuni ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
r
2.4.2.17 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
Lactococcus lactis ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
r
2.4.2.17 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
Mycobacterium tuberculosis H37Rv ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
r
2.4.2.17 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
Campylobacter jejuni RM1221 ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
r

Subunits

EC Number Subunits Comment Organism
2.4.2.17 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
2.4.2.17 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
2.4.2.17 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

EC Number Synonyms Comment Organism
2.4.2.17 adenosine triphosphate phosphoribosyltransferase
-
Mycobacterium tuberculosis
2.4.2.17 adenosine triphosphate phosphoribosyltransferase
-
Campylobacter jejuni
2.4.2.17 adenosine triphosphate phosphoribosyltransferase
-
Lactococcus lactis
2.4.2.17 ATP-PRT
-
Mycobacterium tuberculosis
2.4.2.17 ATP-PRT
-
Campylobacter jejuni
2.4.2.17 ATP-PRT
-
Lactococcus lactis