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Literature summary extracted from

  • Giannese, F.; Berg, M.; Van der Veken, P.; Castagna, V.; Tornaghi, P.; Augustyns, K.; Degano, M.
    Structures of purine nucleosidase from Trypanosoma brucei bound to isozyme-specific trypanocidals and a novel metalorganic inhibitor (2013), Acta Crystallogr. Sect. D, 69, 1553-1566.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.2.1 expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3) Trypanosoma brucei

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.2.1 purified recombinant detagged enzyme, in complex with iminoribitol-based competitive inhibitors UAMC-00363, immucillin-A and UAMC-00312, X-ray diffraction structure determination and analysis at 1.28-2.18 A resolution Trypanosoma brucei

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.2.1 Co2+ mixed-type inhibition Trypanosoma brucei
3.2.2.1 Cu2+ non-competitive inhibition Trypanosoma brucei
3.2.2.1 immucillin-A competitive inhibition Trypanosoma brucei
3.2.2.1 Mn2+ mixed-type inhibition Trypanosoma brucei
3.2.2.1 additional information high-affinity inhibition of the enzyme by iminoribitol-based compounds. Metallorganic complexes can compete for binding at the active site of nucleoside hydrolase enzymes, mimicking the positively charged transition state of the enzymatic reaction, different modes of iminoribitol ring binding at a conserved active site, overview. Divalent metal ions can act as noncompetitive enzyme inhibitors, stabilizing a nonproductive conformation of the catalytic loop Trypanosoma brucei
3.2.2.1 Ni2+ mixed-type inhibition Trypanosoma brucei
3.2.2.1 UAMC-00312 competitive inhibition Trypanosoma brucei
3.2.2.1 UAMC-00363 a trypanocidal compound, competitive inhibition Trypanosoma brucei
3.2.2.1 Zn2+ mixed-type inhibition Trypanosoma brucei

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.2.1 0.016
-
 adenosine recombinant enzyme, pH 7.3, 37°C Trypanosoma brucei
3.2.2.1 0.051
-
 Inosine recombinant enzyme, pH 7.3, 37°C Trypanosoma brucei
3.2.2.1 0.075
-
 guanosine recombinant enzyme, pH 7.3, 37°C Trypanosoma brucei

Organism

EC Number Organism UniProt Comment Textmining
3.2.2.1 Trypanosoma brucei
-
 subsp. brucei
-
3.2.2.1 Trypanosoma brucei TREU927
-
 subsp. brucei
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.2.1 recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, the tag is cleaved off by thrombin, followed by gel filtration Trypanosoma brucei

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.2.1 adenosine + H2O
-
 Trypanosoma brucei adenine + D-ribose
-
 ?
3.2.2.1 adenosine + H2O
-
 Trypanosoma brucei TREU927 adenine + D-ribose
-
 ?
3.2.2.1 guanosine + H2O
-
 Trypanosoma brucei guanine + D-ribose
-
 ?
3.2.2.1 guanosine + H2O
-
 Trypanosoma brucei TREU927 guanine + D-ribose
-
 ?
3.2.2.1 inosine + H2O
-
 Trypanosoma brucei hypoxanthine + D-ribose
-
 ?
3.2.2.1 inosine + H2O
-
 Trypanosoma brucei TREU927 hypoxanthine + D-ribose
-
 ?
3.2.2.1 additional information cytidine, uridine, and 4-nitrophenyl-riboside are poor substrates Trypanosoma brucei ?
-
 ?
3.2.2.1 additional information cytidine, uridine, and 4-nitrophenyl-riboside are poor substrates Trypanosoma brucei TREU927 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.2.1 IAGNH
-
 Trypanosoma brucei
3.2.2.1 purine-specific nucleoside hydrolase
-
 Trypanosoma brucei

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.2.1 37
-
 assay at Trypanosoma brucei

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.2.1 17.3
-
 adenosine recombinant enzyme, pH 7.3, 37°C Trypanosoma brucei
3.2.2.1 37.3
-
 guanosine recombinant enzyme, pH 7.3, 37°C Trypanosoma brucei
3.2.2.1 61
-
 Inosine recombinant enzyme, pH 7.3, 37°C Trypanosoma brucei

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.2.1 7.3
-
 assay at Trypanosoma brucei

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.2.2.1 0.0009
-
 Cu2+ noncompetitive, recombinant enzyme, pH 7.3, 37°C Trypanosoma brucei
3.2.2.1 0.0028
-
 Zn2+ competitive, recombinant enzyme, pH 7.3, 37°C Trypanosoma brucei
3.2.2.1 0.0167
-
 Zn2+ noncompetitive, recombinant enzyme, pH 7.3, 37°C Trypanosoma brucei
3.2.2.1 0.028
-
 Ni2+ competitive, recombinant enzyme, pH 7.3, 37°C Trypanosoma brucei
3.2.2.1 0.16
-
 Co2+ competitive, recombinant enzyme, pH 7.3, 37°C Trypanosoma brucei
3.2.2.1 0.29
-
 Mn2+ competitive, recombinant enzyme, pH 7.3, 37°C Trypanosoma brucei
3.2.2.1 0.39
-
 Ni2+ noncompetitive, recombinant enzyme, pH 7.3, 37°C Trypanosoma brucei
3.2.2.1 1
-
 Mn2+ noncompetitive, recombinant enzyme, pH 7.3, 37°C Trypanosoma brucei
3.2.2.1 1
-
 Co2+ noncompetitive, recombinant enzyme, pH 7.3, 37°C Trypanosoma brucei

General Information

EC Number General Information Comment Organism
3.2.2.1 additional information molecular mechanism underlying the conformational change necessary for enzymatic catalysis, overview Trypanosoma brucei

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.2.2.1 499
-
 guanosine recombinant enzyme, pH 7.3, 37°C Trypanosoma brucei
3.2.2.1 1090
-
 adenosine recombinant enzyme, pH 7.3, 37°C Trypanosoma brucei
3.2.2.1 1190
-
 Inosine recombinant enzyme, pH 7.3, 37°C Trypanosoma brucei