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Literature summary for 1.7.3.3 extracted from

  • Rajagopalan, P.; Chandramoorthy, H.; Elbessoumy, A.
    Pilot scale production and characterization of uricase from Penicillium purpurescens (2017), Indian J. Biotechnol., 16, 570-577 .
No PubMed abstract available
Search for more literature for 1.7.3.3

Activating Compound

Activating Compound Comment Organism Structure
2-mercaptoethanol enzyme activity is strongly enhanced in presence of 5 mM 2-mercaptoethanol Penicillium purpurescens
dithiothreitol enzyme activity is strongly enhanced in presence of 5 mM dithiothreitol Penicillium purpurescens
L-cysteine enzyme activity is strongly enhanced in presence of 5 mM L-cysteine Penicillium purpurescens

Inhibitors

Inhibitors Comment Organism Structure
Ba2+ 1 mM Ba2+ partially truncates enzyme activity to near 50% Penicillium purpurescens
EDTA enzyme activity is completely inhibited in presence of 5 mM EDTA Penicillium purpurescens
Hg2+ 1 mM Hg2+ partially truncates enzyme activity to less than 50% Penicillium purpurescens
KCN enzyme activity is completely inhibited in presence of 5 mM KCN Penicillium purpurescens
Ni2+ 1 mM Ni2+ partially truncates enzyme activity to near 50% Penicillium purpurescens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.5
-
 Urate at pH 9.0 and 30°C Penicillium purpurescens

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ enzyme activity is strongly enhanced in presence of 1 mM Ca2+ Penicillium purpurescens
Cu2+ enzyme activity is strongly enhanced in presence of 1 mM Cu2+ Penicillium purpurescens
Fe2+ enzyme activity is strongly enhanced in presence of 1 mM Fe2+ Penicillium purpurescens
additional information Mn2+, Mg2+, and K+ do not have much effect on the enzyme activity Penicillium purpurescens
Na+ enzyme activity is strongly enhanced in presence of 1 mM Na+ Penicillium purpurescens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
urate + O2 + H2O Penicillium purpurescens
-
 allantoin + H2O2
-
 ?
urate + O2 + H2O Penicillium purpurescens ATCC 10485
-
 allantoin + H2O2
-
 ?

Organism

Organism UniProt Comment Textmining
Penicillium purpurescens
-
-
-
Penicillium purpurescens ATCC 10485
-
-
-

Purification (Commentary)

Purification (Comment) Organism
ammonium sulfate precipitation, DEAE-Sephadex A50 colum chromatography, and Sephadex-G75 gel filtration Penicillium purpurescens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
urate + O2 + H2O
-
 Penicillium purpurescens allantoin + H2O2
-
 ?
urate + O2 + H2O
-
 Penicillium purpurescens ATCC 10485 allantoin + H2O2
-
 ?

Subunits

Subunits Comment Organism
? x * 42000, SDS-PAGE Penicillium purpurescens

Synonyms

Synonyms Comment Organism
uricase
-
 Penicillium purpurescens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 at higher temperatures than 30°C, the enzyme activity decreases sharply Penicillium purpurescens

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
70
-
 the enzyme retains 100% of activity at temperature up to 70°C for 45 min. Increasing the temperature beyond 80°C starts reducing the stability of enzyme to 15 min rather than 30 or 45 min time period. At 100°C the enzyme activity is considerably decreased at all-time points tested Penicillium purpurescens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
-
 Penicillium purpurescens

pH Range

pH Minimum pH Maximum Comment Organism
6 9 the enzyme is mostly active over a broad pH range of 6.0 to 9.0 Penicillium purpurescens

pH Stability

pH Stability pH Stability Maximum Comment Organism
6 10 the purified enzyme remains stable over a wide range of pH between 6.0-10.0 for 2 h Penicillium purpurescens