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Literature summary for 2.4.2.8 extracted from

  • Eng, W.S.; Keough, D.T.; Hockova, D.; Winzor, D.J.; Guddat, L.W.
    Oligomeric state of hypoxanthine-guanine phosphoribosyltransferase from Mycobacterium tuberculosis (2017), Biochimie, 135, 6-14 .
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
phosphate the tetrameric enzyme activity increases in phosphate buffer, while the dimeric state, which occurs when excess magnesium ions are removed, is unable to be rapidly activated by phosphate and magnesium. Phosphate alone cannot activate the enzyme, magnesium ions are also required Mycobacterium tuberculosis

Inhibitors

Inhibitors Comment Organism Structure
2-((2-(guanin-9-yl)ethyl)(2-((2-hydroxyethyl)((2-phosphonoethyl)amino)ethyl)amino)ethyl)phosphonic acid
-
Mycobacterium tuberculosis
2-(2-((2-(hypoxanthine-9-yl)ethyl)((2-phosphonoethyl)amino)ethyl)((2-phosphonoethyl)amino)ethyl)phosphonic acid
-
Mycobacterium tuberculosis
2-([3-(guanin-9-yl)-2-(2-bis(hydroxyphosphoryl)ethoxy)propoxy]ethyl)phosphonic acid
-
Mycobacterium tuberculosis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ dependent on. Phosphate alone cannot activate the enzyme, magnesium ions are also required Mycobacterium tuberculosis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
45400
-
dimeric enzyme, sedimentation equilibrium Mycobacterium tuberculosis
72600
-
enzyme in dimer-tetramer equilibrium, gel filtration Mycobacterium tuberculosis
96000
-
tetrameric enzyme, gel filtration Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate Mycobacterium tuberculosis
-
GMP + diphosphate
-
r
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate Mycobacterium tuberculosis H37Rv
-
GMP + diphosphate
-
r
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate Mycobacterium tuberculosis ATCC 25618
-
GMP + diphosphate
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate Mycobacterium tuberculosis
-
IMP + diphosphate
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate Mycobacterium tuberculosis H37Rv
-
IMP + diphosphate
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate Mycobacterium tuberculosis ATCC 25618
-
IMP + diphosphate
-
r

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WHQ9
-
-
Mycobacterium tuberculosis ATCC 25618 P9WHQ9
-
-
Mycobacterium tuberculosis H37Rv P9WHQ9
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2524
-
purified enzyme in phosphate buffer, pH 7.4, 25°C Mycobacterium tuberculosis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
-
Mycobacterium tuberculosis GMP + diphosphate
-
r
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
-
Mycobacterium tuberculosis H37Rv GMP + diphosphate
-
r
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
-
Mycobacterium tuberculosis ATCC 25618 GMP + diphosphate
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
-
Mycobacterium tuberculosis IMP + diphosphate
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
-
Mycobacterium tuberculosis H37Rv IMP + diphosphate
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
-
Mycobacterium tuberculosis ATCC 25618 IMP + diphosphate
-
r

Subunits

Subunits Comment Organism
dimer
-
Mycobacterium tuberculosis
More dimer-tetramer equilibrium, the major peak is in a dimeric state. DTT is absent from the buffers containing MtHGPRT as there is only one cysteine residue per subunit and this enzyme does not undergo oxidation in the absence of reducing agents. MtHGPRT elutes as three different oligomeric species. MtHGPRT in the Tris-chloride-Mg2+ comprises a mixture of oligomeric states coexisting in a self-association equilibrium. Both tetrameric and dimeric forms of the enzyme are active after column chromatography. The specific activity of the tetramer appears higher than that of the dimer. Crystals of enzyme-diphosphate-GMP complex are used for structure determination, detailed overview Mycobacterium tuberculosis
tetramer
-
Mycobacterium tuberculosis

Synonyms

Synonyms Comment Organism
hypoxanthine-guanine phosphoribosyltransferase
-
Mycobacterium tuberculosis
MtHGPRT
-
Mycobacterium tuberculosis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Mycobacterium tuberculosis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
assay at Mycobacterium tuberculosis

General Information

General Information Comment Organism
additional information crystals of enzyme-diphosphate-GMP complex are used for structure determination, detailed overview Mycobacterium tuberculosis