Literature summary for 1.14.15.1 extracted from

Rydzewski, J.; Nowak, W.
Thermodynamics of camphor migration in cytochrome P450cam by atomistic simulations (2017), Sci. Rep., 7, 7736 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
atomistic simulations study. The diffusion of camphor along the pathway near the substrate recognition site is thermodynamically preferred. The diffusion near the substrate recognition site is triggered by a transition from a heterogeneous collection of closed ligand-bound conformers to the basin comprising the open conformations of cytochrome P450cam. The accompanying conformational change includesthe retraction of the F and G helices and the disorder of the B' helix	Pseudomonas putida

Crystallization (Comment)

Organism

atomistic simulations study. The diffusion of camphor along the pathway near the substrate recognition site is thermodynamically preferred. The diffusion near the substrate recognition site is triggered by a transition from a heterogeneous collection of closed ligand-bound conformers to the basin comprising the open conformations of cytochrome P450cam. The accompanying conformational change includesthe retraction of the F and G helices and the disorder of the B' helix

Pseudomonas putida

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas putida	P00183	-	-

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Release 2023.1 (January 2023)