Literature summary for 1.14.15.35 extracted from

Roberts, A.G.; Diaz, M.D.; Lampe, J.N.; Shireman, L.M.; Grinstead, J.S.; Dabrowski, M.J.; Pearson, J.T.; Bowman, M.K.; Atkins, W.M.; Campbell, A.P.
NMR studies of ligand binding to P450(eryF) provides insight into the mechanism of cooperativity (2006), Biochemistry, 45, 1673-1684.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
NMR studies on lgad binding. Binding of 9-aminophenanthrene and testosterone occurs with apparent negative homotropic cooperativity for testosterone and positive homotropic cooperativity for 9-aminophenanthrene with Hill-equation-derived dissociation constants of 4 and 200 microM, respectively. Binding occurs on intermediate and fast chemical exhange time scales, respectively. The 15N-Phe NMR resonances most affected are the same in each titration, suggesting that the two ligands contact the same phenylalanines within the active site of P450eryF	Saccharopolyspora erythraea

Crystallization (Comment)

Organism

NMR studies on lgad binding. Binding of 9-aminophenanthrene and testosterone occurs with apparent negative homotropic cooperativity for testosterone and positive homotropic cooperativity for 9-aminophenanthrene with Hill-equation-derived dissociation constants of 4 and 200 microM, respectively. Binding occurs on intermediate and fast chemical exhange time scales, respectively. The 15N-Phe NMR resonances most affected are the same in each titration, suggesting that the two ligands contact the same phenylalanines within the active site of P450eryF

Saccharopolyspora erythraea

Organism

Organism	UniProt	Comment	Textmining
Saccharopolyspora erythraea	Q00441	-	-
Saccharopolyspora erythraea NRRL 2338	Q00441	-	-

Synonyms

Synonyms	Comment	Organism
cytochrome P450eryF	-	Saccharopolyspora erythraea
eryF	-	Saccharopolyspora erythraea

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Release 2023.1 (January 2023)