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Literature summary for 2.4.2.17 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
Search for more literature for 2.4.2.17

Cloned(Commentary)

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

Crystallization (Commentary)

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

Inhibitors

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

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 Campylobacter jejuni
-
 ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
 r
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 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

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

Purification (Commentary)

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 and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
 Campylobacter jejuni ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
 r
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
-
 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

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 Lactococcus lactis
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 Mycobacterium tuberculosis

Synonyms

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