Literature summary for 1.14.15.1 extracted from

Liou, S.H.; Myers, W.K.; Oswald, J.D.; Britt, R.D.; Goodin, D.B.
Putidaredoxin binds to the same site on cytochrome P450cam in the open and closed conformation (2017), Biochemistry, 56, 4371-4378 .

Search for more literature for 1.14.15.1

Crystallization (Commentary)

Crystallization (Comment)	Organism
double electron-electron resonance studies. The geometry of the complex is nearly identical for the open and closed states of P450cam. Putaredoxin makes a single distinct interaction with its binding site on the enzyme and triggers the conformational change through very subtle structural interactions	Pseudomonas putida

Protein Variants

Protein Variants	Comment	Organism
Q227C	mutation used for double electron-electron resonance studies	Pseudomonas putida
Q272C	mutation used for double electron-electron resonance studies	Pseudomonas putida
S190C	mutation used for double electron-electron resonance studies. Residues S48C and S190C are at opposite ends of the substrate access channel to provide a longer distance measurement	Pseudomonas putida
S48C	mutation used for double electron-electron resonance studies. Residues S48C and S190C are at opposite ends of the substrate access channel to provide a longer distance measurement	Pseudomonas putida

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas putida	P00183	-	-

Synonyms

Synonyms	Comment	Organism
CYP101A1	-	Pseudomonas putida
P450cam	-	Pseudomonas putida

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)