Literature summary 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.

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
1.11.1.7	expression in Pichia pastoris	Homo sapiens

KM Value [mM]

EC Number	KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
1.11.1.7	0.076	-	SCN-	20°C, pH 6.5	Homo sapiens
1.11.1.7	1.3	-	Br-	20°C, pH 6.5	Homo sapiens

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.11.1.7	Homo sapiens	-	-	-

Posttranslational Modification

EC Number	Posttranslational Modification	Comment	Organism
1.11.1.7	glycoprotein	production of rhEPO by Pichia pastoris as a glycosylated dimer	Homo sapiens
1.11.1.7	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)

EC Number	Purification (Comment)	Organism
1.11.1.7	recombinant enzyme	Homo sapiens

Substrates and Products (Substrate)

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

Synonyms

EC Number	Synonyms	Comment	Organism
1.11.1.7	rhEPO	recombinant human eosinophil peroxidase	Homo sapiens

Turnover Number [1/s]

EC Number	Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
1.11.1.7	0.46	-	Br-	20°C, pH 6.5	Homo sapiens
1.11.1.7	13.6	-	SCN-	20°C, pH 6.5	Homo sapiens

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Release 2023.1 (January 2023)