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Literature summary for 1.11.1.7 extracted from

  • Ciaccio, C.; Gambacurta, A.; De Sanctis, G.; Spagnolo, D.; Sakarikou, C.; Petrella, G.; Coletta, M.
    rhEPO (recombinant human eosinophil peroxidase): expression in Pichia pastoris and biochemical characterization (2006), Biochem. J., 395, 295-301.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Pichia pastoris Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.076
-
SCN- 20°C, pH 6.5 Homo sapiens
1.3
-
Br- 20°C, pH 6.5 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein production of rhEPO by Pichia pastoris as a glycosylated dimer Homo sapiens
proteolytic modification production of rhEPO by Pichia pastoris as a glycosylated dimer precursor of approximately 80 kDa. Proteolytic processing, similar to that in the native host, to generate two chains of approximately 50 kDa and 20 kDa Homo sapiens

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Br- + H2O2
-
Homo sapiens ?
-
?
Cl- + H2O2
-
Homo sapiens ?
-
?
pyrogallol + H2O2
-
Homo sapiens purpurogallin + H2O
-
?
SCN- + H2O2
-
Homo sapiens OSCN- + H2O
-
?

Synonyms

Synonyms Comment Organism
rhEPO recombinant human eosinophil peroxidase Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.46
-
Br- 20°C, pH 6.5 Homo sapiens
13.6
-
SCN- 20°C, pH 6.5 Homo sapiens