scholarly journals A Comparison Between Lignans from Creosote Bush and Flaxseed and Their Potential to Inhibit Cytochrome P450 Enzyme Activity

10.5772/34317 ◽  
2012 ◽  
Author(s):  
Jennifer Billinsky ◽  
Katherine Maloney ◽  
Ed Krol ◽  
Jane Alcor
Keyword(s):  
Enzyme Activity ◽  
Cytochrome P450 ◽  
Cytochrome P450 Enzyme ◽  
Creosote Bush ◽  
P450 Enzyme

scholarly journals Characterization of Medicago truncatula (barrel medic) hydroperoxide lyase (CYP74C3), a water-soluble detergent-free cytochrome P450 monomer whose biological activity is defined by monomer–micelle association

2006 ◽  
Vol 395 (3) ◽  
pp. 641-652 ◽  
Author(s):  
Richard K. Hughes ◽  
Eric J. Belfield ◽  
Mylrajan Muthusamay ◽  
Anuja Khan ◽  
Arthur Rowe ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Cytochrome P450 ◽  
Medicago Truncatula ◽  
Water Soluble ◽  
Hydroperoxide Lyase ◽  
Cytochrome P450 Enzyme ◽  
Cytochrome P450 Enzymes ◽  
P450 Enzyme ◽  
Detergent Micelles

We describe the detailed biochemical characterization of CYP74C3 (cytochrome P450 subfamily 74C3), a recombinant plant cytochrome P450 enzyme with HPL (hydroperoxide lyase) activity from Medicago truncatula (barrel medic). Steady-state kinetic parameters, substrate and product specificities, RZ (Reinheitszahl or purity index), molar absorption coefficient, haem content, and new ligands for an HPL are reported. We show on the basis of gel filtration, sedimentation velocity (sedimentation coefficient distribution) and sedimentation equilibrium (molecular mass) analyses that CYP74C3 has low enzyme activity as a detergent-free, water-soluble, monomer. The enzyme activity can be completely restored by re-activation with detergent micelles, but not detergent monomers. Corresponding changes in the spin state equilibrium, and probably co-ordination of the haem iron, are novel for cytochrome P450 enzymes and suggest that detergent micelles have a subtle effect on protein conformation, rather than substrate presentation, which is sufficient to improve substrate binding and catalytic-centre activity by an order of magnitude. The kcat/Km of up to 1.6×108 M−1·s−1 is among the highest recorded, which is remarkable for an enzyme whose reaction mechanism involves the scission of a C–C bond. We carried out both kinetic and biophysical studies to demonstrate that this effect is a result of the formation of a complex between a protein monomer and a single detergent micelle. Association with a detergent micelle rather than oligomeric state represents a new mechanism of activation for membrane-associated cytochrome P450 enzymes. Highly concentrated and monodispersed samples of detergent-free CYP74C3 protein may be well suited for the purposes of crystallization and structural resolution of the first plant cytochrome P450 enzyme.

Assessing orally bioavailable commercial silver nanoparticle product on human cytochrome P450 enzyme activity

2014 ◽  
Vol 9 (4) ◽  
pp. 474-481 ◽  
Author(s):  
Mark A. Munger ◽  
Greg Hadlock ◽  
Greg Stoddard ◽  
Matthew H. Slawson ◽  
Diana G. Wilkins ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Cytochrome P450 ◽  
Silver Nanoparticle ◽  
Cytochrome P450 Enzyme ◽  
Human Cytochrome ◽  
P450 Enzyme ◽  
Orally Bioavailable ◽  
Human Cytochrome P450 Enzyme

Effect of Age and Postoperative Time on Cytochrome P450 Enzyme Activity Following Liver Transplantation

2005 ◽  
Vol 45 (6) ◽  
pp. 666-673 ◽  
Author(s):  
Shanshan Liu ◽  
Reginald F. Frye ◽  
Robert A. Branch ◽  
Raman Venkataramanan ◽  
John J. Fung ◽  
...  
Keyword(s):  
Liver Transplantation ◽  
Enzyme Activity ◽  
Cytochrome P450 ◽  
Cytochrome P450 Enzyme ◽  
P450 Enzyme ◽  
Postoperative Time ◽  
Effect Of Age

scholarly journals Time-Dependent Induction of Hepatic Cytochrome P450 Enzyme Activity and mRNA Expression by Bilobalide in Rats

2009 ◽  
Vol 109 (3) ◽  
pp. 459-462 ◽  
Author(s):  
Yuko Taki ◽  
Yuko Yamazaki ◽  
Fumio Shimura ◽  
Shizuo Yamada ◽  
Keizo Umegaki
Keyword(s):  
Enzyme Activity ◽  
Cytochrome P450 ◽  
Mrna Expression ◽  
Time Dependent ◽  
Cytochrome P450 Enzyme ◽  
P450 Enzyme ◽  
Hepatic Cytochrome

Effect of cardiopulmonary bypass on cytochrome P450 enzyme activity: implications for pharmacotherapy

2017 ◽  
Vol 50 (2) ◽  
pp. 109-124 ◽  
Author(s):  
Santosh Kumar Sreevatsav Adiraju ◽  
Kiran Shekar ◽  
John F. Fraser ◽  
Maree T. Smith ◽  
Sussan Ghassabian
Keyword(s):  
Enzyme Activity ◽  
Cytochrome P450 ◽  
Cardiopulmonary Bypass ◽  
Cytochrome P450 Enzyme ◽  
P450 Enzyme
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