Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Medrano, F.J.; Wenck, M.A.; Eakin, A.E.; Craig, S.P., 3rd
    Functional roles for amino acids in active site loop II of a hypoxanthine phosphoribosyltransferase (2003), Biochim. Biophys. Acta, 1650, 105-116.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.2.8 expression of active wild-type and of mutant enzymes in Escherichia coli strain DH5alpha Trypanosoma cruzi

Protein Variants

EC Number Protein Variants Comment Organism
2.4.2.8 additional information saturation mutagenesis for randomly exchange of amino acids of the active site loop II, construction of diverse mutants of the residues S102 to Q112, kinetic analysis and determination of catalytic efficiencies in the forward and reverse reaction, overview Trypanosoma cruzi

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.2.8 additional information
-
 additional information kinetic analysis in the forward and reverse reaction of the wild-type enzyme and diverse mutant enzymes, overview Trypanosoma cruzi

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.4.2.8 Mg2+
-
 Trypanosoma cruzi

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.2.8 IMP + diphosphate Trypanosoma cruzi
-
 hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.4.2.8 Trypanosoma cruzi
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.2.8 recombinant wild-type and mutant enzymes from Escherichia coli strain DH5alpha by GMP affinity chromatography Trypanosoma cruzi

Reaction

EC Number Reaction Comment Organism Reaction ID
2.4.2.8 IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate reaction mechanism, the flexible loop II, comprising 12 amino acid residues, closes over the active site of the enzyme as it approaches the transition state, the loop is required for full activity, structure-function relationship for the conserved residues Trypanosoma cruzi
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.4.2.8 additional information
-
 kinetic analysis and determination of catalytic efficiencies in the forward and reverse reaction for the wild-type and diverse mutant enzymes, overview Trypanosoma cruzi

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.2.8 IMP + diphosphate
-
 Trypanosoma cruzi hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
-
 r

Synonyms

EC Number Synonyms Comment Organism
2.4.2.8 HPRT
-
 Trypanosoma cruzi
2.4.2.8 inosine monophosphate:pyrophosphate phosphoribosyltransferase
-
 Trypanosoma cruzi

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.2.8 37
-
 assay at, forward and reverse reaction Trypanosoma cruzi

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.4.2.8 additional information
-
 additional information wild-type and diverse mutant enzymes, overview Trypanosoma cruzi

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.2.8 7.5
-
 assay at, forward and reverse reaction Trypanosoma cruzi