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Literature summary for 2.4.2.8 extracted from

  • Munagala, N.R.; Chin, M.S.; Wang, C.C.
    Steady-state kinetics of the hypoxanthine-guanine-xanthine phosphoribosyltransferase from Tritrichomonas foetus: the role of threonine-47 (1998), Biochemistry, 37, 4045-4051.
    View publication on PubMed
Search for more literature for 2.4.2.8

Application

Application Comment Organism
medicine target for anti-trichomonial therapy Tritrichomonas suis

Cloned(Commentary)

Cloned (Comment) Organism
functional expression of wild-type and mutant T47K in an enzyme-deficient Escherichia coli strain Tritrichomonas suis

Crystallization (Commentary)

Crystallization (Comment) Organism
analysis of crystal structure Tritrichomonas suis

Protein Variants

Protein Variants Comment Organism
T47K site-directed mutagenesis, exchange of diphosphate binding site residue, 4-10fold decreased Km for diphosphate compared to the wild-type Tritrichomonas suis

Inhibitors

Inhibitors Comment Organism Structure
5-phospho-alpha-D-ribose 1-diphosphate product inhibition Tritrichomonas suis
diphosphate product inhibition Tritrichomonas suis
GMP product inhibition Tritrichomonas suis
IMP product inhibition Tritrichomonas suis
XMP product inhibition Tritrichomonas suis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetics Tritrichomonas suis
additional information
-
 additional information wild-type and mutant T47K Tritrichomonas suis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
guanine + 5-phospho-alpha-D-ribose 1-diphosphate Tritrichomonas suis
-
 GMP + diphosphate
-
 ?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate Tritrichomonas suis
-
 IMP + diphosphate
-
 ?
additional information Tritrichomonas suis salvage incorporation of exogenous purine nucleotides, no de novo synthesis ?
-
 ?
additional information Tritrichomonas suis enzyme is essential for salvaging exogenous purine bases ?
-
 ?

Organism

Organism UniProt Comment Textmining
Tritrichomonas suis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type enzyme and mutant/s from Escherichia coli Tritrichomonas suis

Reaction

Reaction Comment Organism Reaction ID
IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate ordered bi-bi mechanism Tritrichomonas suis
a
IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate Thr47 binds diphosphate Tritrichomonas suis
a
IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate kinetic model Tritrichomonas suis
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 kinetics in forward and reverse reaction Tritrichomonas suis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
-
 Tritrichomonas suis GMP + diphosphate
-
 ?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
-
 Tritrichomonas suis GMP + diphosphate
-
 r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
-
 Tritrichomonas suis IMP + diphosphate
-
 ?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate most effective substrate Tritrichomonas suis IMP + diphosphate diphosphate is bound by Thr47 r
additional information salvage incorporation of exogenous purine nucleotides, no de novo synthesis Tritrichomonas suis ?
-
 ?
additional information enzyme is essential for salvaging exogenous purine bases Tritrichomonas suis ?
-
 ?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
-
 Tritrichomonas suis XMP + diphosphate
-
 r

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.71
-
 hypoxanthine mutant T47K Tritrichomonas suis

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
-
 additional information kinetics of product inhibition in forward reaction Tritrichomonas suis