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  • 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)
    Vrsta gradiva - disertacija
    Založništvo in izdelava - Ljubljana : [T. Makovec], 2001
    Jezik - slovenski
    COBISS.SI-ID - 2283796

Knjižnica Signatura – lokacija, inventarna št. ... Status izvoda
Narodna in univerzitetna knjižnica, Ljubljana GS II 525634 glavno skladišče prosto - za čitalnico
MF, Centralna medicinska knjižnica, Ljubljana doktorske disertacije
MAKOVEC Tomaž Struktura
IN: 020010578 		prosto - na dom, čas izposoje: 1 mes.
MF, Centralna medicinska knjižnica, Ljubljana doktorske disertacije
MAKOVEC Tomaž Struktura
IN: 020010577 		prosto - na dom, čas izposoje: 1 mes.
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