There are two major P450 classes in terms of the native RP systems, namely, the prokaryotic Class I P450 consisting of three stand-alone components (redoxin reductase/redoxin/P450) that are all cytosolically soluble proteins and the two-component eukaryotic Class II P450 comprised of P450 and cytochrome P450 reductase (CPR), both of which are membrane-bound proteins. (nature.com)
Cytochrome P450 enzymes (P450s or CYPs) are a superfamily of heme-thiolate proteins widespread in all kingdoms of life 1 . (nature.com)
The enzyme, which transfers electrons from NADPH to adrenodoxin molecules, is the first component in the mitochondrial cytochrome P450 electron transfer systems, and is involved in the biosynthesis of all steroid hormones. (expasy.org)
Furthermore, Autodisplay has proven for being a robust expres sion platform for that surface show of enzymes usually together with cytochrome P450 enzymes of bacterial and hu man origin. (pkainhibitors.com)
In addition, no cost radicals can oxidize the heme catalytic group of cytochrome P450, resulting in enzymatic inactivation [33,34]. (piminhibitor.com)
Most steroidogenic reactions are catalysed by enzymes of the cytochrome P450 family. (wikidoc.org)
Oxidase2
a) Cytochrome oxidase is a hemoprotein widely distributed in plants and animal tissues. (biologydiscussion.com)
2 at-oms of Cu are also present which are asso-ciated with the cytochrome oxidase ac-tivity. (biologydiscussion.com)
A bacterial protein from Pseudomonas, Bordetella, or Alcaligenes which operates as an electron transfer unit associated with the cytochrome chain. (lookformedical.com)
The various cytochrome subclasses are organized by the type of HEME and by the wavelength range of their reduced alpha-absorption bands. (lookformedical.com)
Membrane-bound1
The 30-kDa membrane-bound c-type cytochrome protein of mitochondria that functions as an electron donor to CYTOCHROME C GROUP in the mitochondrial and bacterial RESPIRATORY CHAIN. (lookformedical.com)
Protein1
It is a cytochrome protein that contains IRON and MOLYBDENUM. (lookformedical.com)
Enzymes2
Phylogenetic analysis indicated that a tryptophan residue corresponding to Trp359 is conserved across FprA-type enzymes and in adrenodoxin reductases. (manchester.ac.uk)
Key enzymes in the overall reactions are nicotinamide-adenine dinucleotide phosphate reductase (NADPH)-cytochrome C reductase, the flavin enzyme involved in the oxidation of NADPH, cytochrome P- 450, which in its reduced form is generally considered to be A, and NADPH cytochrome P-450 reductase, which functions in the reduction of oxidized cytochrome P-450. (nih.gov)
Mycobacterium2
abstract = "Mtb (Mycobacterium tuberculosis) FprA (flavoprotein reductase A) is an NAD(P)H-dependent FAD-binding reductase that is structurally related to mammalian adrenodoxin reductase, and which supports the catalytic function of Mtb cytochrome P450s. (manchester.ac.uk)
9. Kinetic, spectroscopic and thermodynamic characterization of the Mycobacterium tuberculosis adrenodoxin reductase homologue FprA. (nih.gov)
Metabolism1
Scheme showing how NADH and cytochrome bs might contribute to the electron transfer system employed in the microsomal metabolism of drugs SOURCE: Estabrook, R. (11). (nih.gov)
Adrenal1
NHIP = non-heme iron protein (in the adrenal, adrenodoxin) SOURCE: Omura, T. (43,48). (nih.gov)
Reaction2
In this way, cytochrome bs might serve as a second electron donor to cytochrome P- 450 and thus satisfy the requirement of two electrons for the overall reaction. (nih.gov)
18. Design of a cytochrome P450BM3 reaction system linked by two-step cofactor regeneration catalyzed by a soluble transhydrogenase and glycerol dehydrogenase. (nih.gov)
Functional1
2. Functional interactions in cytochrome P450BM3. (nih.gov)
Redox1
Through redox partners combination screening, we reveal the optimal redox partner pair of S. scrofa adrenodoxin and C. hircus adrenodoxin reductase. (hhu.de)
System1
Much of the speculation regarding the components of the microsom- al drug metabolizing system existed because attempts to solubilize cytochrome P-450 in active form had failed, and it was necessary to employ crude microsomal preparations. (nih.gov)
Type1
this, in turn, would seem to depend upon whether the drug combines with cytochrome P-450 as a type I or as a type II sompound (17, 18, 19) as discussed below. (nih.gov)