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Literature summary for 2.4.2.22 extracted from

  • Roy, S.; Karmakar, T.; Nagappa, L.K.; Prahlada Rao, V.S.; Balasubramanian, S.; Balaram, H.
    Role of W181 in modulating kinetic properties of Plasmodium falciparum hypoxanthine guanine xanthine phosphoribosyltransferase (2016), Proteins, 84, 1658-1669 .
    View publication on PubMed
Search for more literature for 2.4.2.22

Activating Compound

Activating Compound Comment Organism Structure
IMP
-
 Plasmodium falciparum

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Plasmodium falciparum

Protein Variants

Protein Variants Comment Organism
W181F the mutant retains its ability to catalyse the phosphoribosylation of hypoxanthine, guanine and xanthine, albeit with significantly lower specific activities than the wild type enzyme. The mutant shows an increase in Km for 5-phospho-alpha-D-ribose 1-diphosphate by 3.4fold under unactivated condition and a decrease in catalytic efficiency by 76fold under activated condition as compared to that of the wild type enzyme Plasmodium falciparum
W181S the mutant retains its ability to catalyse the phosphoribosylation of hypoxanthine, guanine and xanthine, albeit with significantly lower specific activities than the wild type enzyme. The mutant shows 10fold reduced xanthine phosphoribosylation activity compared to the wild type enzyme Plasmodium falciparum
W181S the mutant retains its ability to catalyze the phosphoribosylation of hypoxanthine, guanine and xanthine, albeit with significantly lower specific activities than the wild type enzyme. The mutant shows an increase in Km for 5-phospho-alpha-D-ribose 1-diphosphate by 2.1fold under unactivated condition and a decrease in catalytic efficiency by more than 11fold under activated condition as compared to that of the wild type enzyme Plasmodium falciparum
W181Y the mutant retains its ability to catalyse the phosphoribosylation of hypoxanthine, guanine and xanthine, albeit with significantly lower specific activities than the wild type enzyme. The mutant shows an increase in Km for 5-phospho-alpha-D-ribose 1-diphosphate by 2.6fold under unactivated condition and a decrease in catalytic efficiency by more than 5fold under activated condition as compared to that of the wild type enzyme Plasmodium falciparum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.053
-
 5-phospho-alpha-D-ribose 1-diphosphate IMP-activated wild type enzyme, at pH 7.4, temperature not specified in the publication Plasmodium falciparum
0.094
-
 5-phospho-alpha-D-ribose 1-diphosphate IMP-activated mutant enzyme W181Y, at pH 7.4, temperature not specified in the publication Plasmodium falciparum
0.233
-
 5-phospho-alpha-D-ribose 1-diphosphate IMP-activated mutant enzyme W181F, at pH 7.4, temperature not specified in the publication Plasmodium falciparum
0.251
-
 5-phospho-alpha-D-ribose 1-diphosphate IMP-activated mutant enzyme W181S, at pH 7.4, temperature not specified in the publication Plasmodium falciparum
1.084
-
 5-phospho-alpha-D-ribose 1-diphosphate unactivated wild type enzyme, at pH 7.4, temperature not specified in the publication Plasmodium falciparum
2.286
-
 5-phospho-alpha-D-ribose 1-diphosphate unactivated mutant enzyme W181S, at pH 7.4, temperature not specified in the publication Plasmodium falciparum
2.783
-
 5-phospho-alpha-D-ribose 1-diphosphate unactivated mutant enzyme W181Y, at pH 7.4, temperature not specified in the publication Plasmodium falciparum
3.668
-
 5-phospho-alpha-D-ribose 1-diphosphate unactivated mutant enzyme W181F, at pH 7.4, temperature not specified in the publication Plasmodium falciparum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5-phospho-alpha-D-ribose 1-diphosphate + guanine Plasmodium falciparum
-
 GMP + diphosphate
-
 ?
5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine Plasmodium falciparum
-
 IMP + diphosphate
-
 ?
5-phospho-alpha-D-ribose 1-diphosphate + xanthine Plasmodium falciparum
-
 XMP + diphosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Q-Sepharose column chromatography, CM Sepharose column chromatography and Sephacryl S-200 gel filtration Plasmodium falciparum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5-phospho-alpha-D-ribose 1-diphosphate + guanine
-
 Plasmodium falciparum GMP + diphosphate
-
 ?
5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine
-
 Plasmodium falciparum IMP + diphosphate
-
 ?
5-phospho-alpha-D-ribose 1-diphosphate + xanthine
-
 Plasmodium falciparum XMP + diphosphate
-
 ?

Subunits

Subunits Comment Organism
tetramer
-
 Plasmodium falciparum

Synonyms

Synonyms Comment Organism
HGXPRT
-
 Plasmodium falciparum
hypoxanthine-guanine-xanthine phosphoribosyltransferase
-
 Plasmodium falciparum

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.1
-
 5-phospho-alpha-D-ribose 1-diphosphate IMP-activated mutant enzyme W181F, at pH 7.4, temperature not specified in the publication Plasmodium falciparum
0.1
-
 5-phospho-alpha-D-ribose 1-diphosphate unactivated mutant enzyme W181Y, at pH 7.4, temperature not specified in the publication Plasmodium falciparum
0.2
-
 5-phospho-alpha-D-ribose 1-diphosphate unactivated mutant enzyme W181F, at pH 7.4, temperature not specified in the publication Plasmodium falciparum
0.2
-
 5-phospho-alpha-D-ribose 1-diphosphate unactivated wild type enzyme, at pH 7.4, temperature not specified in the publication Plasmodium falciparum
0.32
-
 5-phospho-alpha-D-ribose 1-diphosphate unactivated mutant enzyme W181S, at pH 7.4, temperature not specified in the publication Plasmodium falciparum
0.5
-
 5-phospho-alpha-D-ribose 1-diphosphate IMP-activated mutant enzyme W181Y, at pH 7.4, temperature not specified in the publication Plasmodium falciparum
0.67
-
 5-phospho-alpha-D-ribose 1-diphosphate IMP-activated mutant enzyme W181S, at pH 7.4, temperature not specified in the publication Plasmodium falciparum
1.6
-
 5-phospho-alpha-D-ribose 1-diphosphate IMP-activated wild type enzyme, at pH 7.4, temperature not specified in the publication Plasmodium falciparum

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.36
-
 5-phospho-alpha-D-ribose 1-diphosphate unactivated mutant enzyme W181Y, at pH 7.4, temperature not specified in the publication Plasmodium falciparum
0.4
-
 5-phospho-alpha-D-ribose 1-diphosphate IMP-activated mutant enzyme W181F, at pH 7.4, temperature not specified in the publication Plasmodium falciparum
0.54
-
 5-phospho-alpha-D-ribose 1-diphosphate unactivated mutant enzyme W181F, at pH 7.4, temperature not specified in the publication Plasmodium falciparum
1.39
-
 5-phospho-alpha-D-ribose 1-diphosphate unactivated mutant enzyme W181S, at pH 7.4, temperature not specified in the publication Plasmodium falciparum
1.84
-
 5-phospho-alpha-D-ribose 1-diphosphate unactivated wild type enzyme, at pH 7.4, temperature not specified in the publication Plasmodium falciparum
2.6
-
 5-phospho-alpha-D-ribose 1-diphosphate IMP-activated mutant enzyme W181S, at pH 7.4, temperature not specified in the publication Plasmodium falciparum
5.3
-
 5-phospho-alpha-D-ribose 1-diphosphate IMP-activated mutant enzyme W181Y, at pH 7.4, temperature not specified in the publication Plasmodium falciparum
30.1
-
 5-phospho-alpha-D-ribose 1-diphosphate IMP-activated wild type enzyme, at pH 7.4, temperature not specified in the publication Plasmodium falciparum