Struktura in imunokemijske lastnosti NADPH-citokrom P450 reduktaze iz glive Rhizopus nigricans : doktorska disertacija = Structure and immunochemical properties of NADPH-cytochrom P450 reductase from fungus Rhizopus nigricans : doctoral thesis
Makovec, Tomaž, 1959-
Cytochrome P450 (P450) -mediated conversion steps are suggested to be a part of many speciflc fungal biotransformation processes. A well-studied class of bioconversions carried out by fungal P450 ...enryme systems is the stereo-specific hydroxylation of pharmaceutically interesting compounds, especially progesterone. It is remarkable that all the Saccharomyces cerevisiae P450s are involved in housekeeping activities, while many P450s in fllamentous fungi are involved in nonessential detoxyfication reactions or thesynthesis of complex secondary metabolites. The best studied P450-mediated reactions concem the degradation of polyaromatic hydrocarbons such as benz<a>pyrene, the biotransformataion of pharmaceutically important steroids like progesterone and lanosterol, and the assimilation of long chain alkanes. Most fungal hydroxylation systems identifled so far belong to type I rnonooxygenases and are expected to be located on endoplasmic reticulum. This systems are composed of two enrymesČ NADPH-cytochrome P450 reductase (CPR) (EC1.6.2.4) and P450. The function of CPR is to receive two electrons from NADPH and transfer `em sequentially to P450. The enzyme contains one molecule of both FAD and FMN. The transfer of electrons has been shown to occur in the order NADPH to FAD, then to FMN, and finally to P450. This sequential transferof two electrons occurs by redox cycling between the one-electron-reduced enzyme and the three-electronreduced form. Structural studies with rat or rabbit liver CPR have revealed that CPR is an amphipathic protein containing a large hydrophilic catalytic domain. Limited proteolylis of microsomal CPR yields two major peptide fragmentsč flavin containing hydrophylic domain (70-72 kDa) that can reduce non-physiological, artificial electron acceptors such a cytochrome c (but not P450) and a small (5-6 kDa) N-terminal hydrophobic membrane domain which is required for P450 reduction. (Abstract truncated at 2000 characters)
Type of material - dissertation
Publication and manufacture - Ljubljana : [T. Makovec], 2001
doktorske disertacije MAKOVEC Tomaž Struktura IN: 020010577
available - outside loan, loan period: 1 months
MF, Central Medical Library, Lj.
doktorske disertacije MAKOVEC Tomaž Struktura IN: 020010578
available - outside loan, loan period: 1 months
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