Literature summary extracted from

Savino, C.; Montemiglio, L.C.; Sciara, G.; Miele, A.E.; Kendrew, S.G.; Jemth, P.; Gianni, S.; Vallone, B.
Investigating the structural plasticity of a cytochrome P450: three-dimensional structures of P450 EryK and binding to its physiological substrate (2009), J. Biol. Chem., 284, 29170-29179.

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
1.14.13.154	recombinant His-tagged EryK is overexpressed in the Escherichia coli BL21	Saccharopolyspora erythraea

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
1.14.13.154	vapor diffusion at 21°C, three crystal forms of EryK are obtained in different crystallization conditions: with His tag (His6-EryK) in low salt conditions, without tag (EryK) in high salt, and in complex with its substrate erythromycin D (ErD-EryK)	Saccharopolyspora erythraea

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.14.13.154	Saccharopolyspora erythraea	P48635	-	-

Subunits

EC Number	Subunits	Comment	Organism
1.14.13.154	monomer	-	Saccharopolyspora erythraea

Synonyms

EC Number	Synonyms	Comment	Organism
1.14.13.154	EryK	-	Saccharopolyspora erythraea

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
1.14.13.154	cytochrome P-450	a heme-thiolate protein (P-450)	Saccharopolyspora erythraea

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)