Characterization of the Secondary Structure and Membrane Interaction of the Putative Membrane Anchor Domains of Prostaglandin I2Synthase and Cytochrome P450 2C1

1998 ◽  
Vol 352 (1) ◽  
pp. 78-84 ◽  
Author(s):  
Yue-zhen Lin ◽  
Kenneth K. Wu ◽  
Ke-He Ruan
Keyword(s):  
Cytochrome P450 ◽  
Secondary Structure ◽  
Membrane Anchor ◽  
Membrane Interaction

scholarly journals Membrane anchoring facilitates colocalization of enzymes in plant cytochrome P450 redox systems

2021 ◽  
Vol 4 (1) ◽  
Author(s):  
Tomas Laursen ◽  
Hiu Yue Monatrice Lam ◽  
Kasper Kildegaard Sørensen ◽  
Pengfei Tian ◽  
Cecilie Cetti Hansen ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Single Molecule ◽  
Cascade Reactions ◽  
Endoplasmic Reticulum Membrane ◽  
Redox Systems ◽  
Membrane Anchor ◽  
Multienzyme Complexes ◽  
Nucleation Sites ◽  
Membrane Anchoring

AbstractPlant metabolism depends on cascade reactions mediated by dynamic enzyme assemblies known as metabolons. In this context, the cytochrome P450 (P450) superfamily catalyze key reactions underpinning the unique diversity of bioactive compounds. In contrast to their soluble bacterial counterparts, eukaryotic P450s are anchored to the endoplasmic reticulum membrane and serve as metabolon nucleation sites. Hence, membrane anchoring appears to play a pivotal role in the evolution of complex biosynthetic pathways. Here, a model membrane assay enabled characterization of membrane anchor dynamics by single molecule microscopy. As a model system, we reconstituted the membrane anchor of cytochrome P450 oxidoreductase (POR), the ubiquitous electron donor to all microsomal P450s. The transmembrane segment in the membrane anchor of POR is relatively conserved, corroborating its functional importance. We observe dynamic colocalization of the POR anchors in our assay suggesting that membrane anchoring might promote intermolecular interactions and in this way impact assembly of metabolic multienzyme complexes.

Characterization of Tamm-Horsfall Urinary Glycoprotein

1973 ◽  
Vol 31 ◽  
pp. 420-421
Author(s):  
John P. Robinson ◽  
J. David Puett
Keyword(s):  
Electron Microscopy ◽  
Circular Dichroism ◽  
Secondary Structure ◽  
Quaternary Structure ◽  
Normal Adult ◽  
Morphological Properties ◽  
Adult Males ◽  
Circular Dichroïsm ◽  
Urinary Glycoprotein

Much work has been reported on the chemical, physical and morphological properties of urinary Tamm-Horsfall glycoprotein (THG). Although it was once reported that cystic fibrotic (CF) individuals had a defective THG, more recent data indicate that THG and CF-THG are similar if not identical.No studies on the conformational aspects have been reported on this glycoprotein using circular dichroism (CD). We examined the secondary structure of THG and derivatives under various conditions and have correlated these results with quaternary structure using electron microscopy.THG was prepared from normal adult males and CF-THG from a 16-year old CF female by the method of Tamm and Horsfall. CF female by the method of Tamm and Horsfall.

Purification and Characterization of Cytochrome P450 from an Isobutene-forming Microorganism,Rhodotorula minuta

1993 ◽  
Vol 57 (9) ◽  
pp. 1599-1601 ◽  
Author(s):  
Hideo Fukuda ◽  
Takao Fujii ◽  
Hironori Daimon ◽  
Makoto Iwata ◽  
Takahira Ogawa ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Purification And Characterization ◽  
Rhodotorula Minuta

Characterization of Diuron N-Demethylation by Mammalian Hepatic Microsomes and cDNA-Expressed Human Cytochrome P450 Enzymes

2007 ◽  
Vol 35 (9) ◽  
pp. 1634-1641 ◽  
Author(s):  
Khaled Abass ◽  
Petri Reponen ◽  
Miia Turpeinen ◽  
Jorma Jalonen ◽  
Olavi Pelkonen
Keyword(s):  
Cytochrome P450 ◽  
Cytochrome P450 Enzymes ◽  
Hepatic Microsomes ◽  
Human Cytochrome
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