Lithuanian
Albanian
Arabic
Armenian
Azerbaijani
Belarusian
Bengali
Bosnian
Catalan
Czech
Danish
Deutsch
Dutch
English
Estonian
Finnish
Français
Greek
Haitian Creole
Hebrew
Hindi
Hungarian
Icelandic
Indonesian
Irish
Italian
Japanese
Korean
Latvian
Lithuanian
Macedonian
Mongolian
Norwegian
Persian
Polish
Portuguese
Romanian
Russian
Serbian
Slovak
Slovenian
Spanish
Swahili
Swedish
Turkish
Ukrainian
Vietnamese
Български
中文(简体)
中文(繁體)
Biochemical Journal 2018-02

Structural and functional characterisation of the cytochrome P450 enzyme CYP268A2 from Mycobacterium marinum.

Straipsnius versti gali tik registruoti vartotojai
Prisijungti Registracija
Nuoroda įrašoma į mainų sritį
Stella A Child
Elise F Naumann
John B Bruning
Stephen G Bell

Raktažodžiai

Santrauka

Members of the cytochrome P450 monooxygenase family CYP268 are found across a broad range of Mycobacterium species including the pathogens Mycobacterium avium, M. colombiense, M. kansasii, and Mmarinum CYP268A2, from M. marinum, which is the first member of this family to be studied, was purified and characterised. CYP268A2 was found to bind a variety of substrates with high affinity, including branched and straight chain fatty acids (C10-C12), acetate esters, and aromatic compounds. The enzyme was also found to bind phenylimidazole inhibitors but not larger azoles, such as ketoconazole. The monooxygenase activity of CYP268A2 was efficiently reconstituted using heterologous electron transfer partner proteins. CYP268A2 hydroxylated geranyl acetate and trans-pseudoionone at a terminal methyl group to yield (2E,6E)-8-hydroxy-3,7-dimethylocta-2,6-dien-1-yl acetate and (3E,5E,9E)-11-hydroxy-6,10-dimethylundeca-3,5,9-trien-2-one, respectively. The X-ray crystal structure of CYP268A2 was solved to a resolution of 2.0 Å with trans-pseudoionone bound in the active site. The overall structure was similar to that of the related phytanic acid monooxygenase CYP124A1 enzyme from Mycobacterium tuberculosis, which shares 41% sequence identity. The active site is predominantly hydrophobic, but includes the Ser99 and Gln209 residues which form hydrogen bonds with the terminal carbonyl group of the pseudoionone. The structure provided an explanation on why CYP268A2 shows a preference for shorter substrates over the longer chain fatty acids which bind to CYP124A1 and the selective nature of the catalysed monooxygenase activity.

Prisijunkite prie mūsų
„Facebook“ puslapio

Išsamiausia vaistinių žolelių duomenų bazė, paremta mokslu

  • Dirba 55 kalbomis
  • Žolelių gydymas, paremtas mokslu
  • Vaistažolių atpažinimas pagal vaizdą
  • Interaktyvus GPS žemėlapis - pažymėkite vaistažoles vietoje (netrukus)
  • Skaitykite mokslines publikacijas, susijusias su jūsų paieška
  • Ieškokite vaistinių žolelių pagal jų poveikį
  • Susitvarkykite savo interesus ir sekite naujienas, klinikinius tyrimus ir patentus

Įveskite simptomą ar ligą ir perskaitykite apie žoleles, kurios gali padėti, įveskite žolę ir pamatykite ligas bei simptomus, nuo kurių ji naudojama.
* Visa informacija pagrįsta paskelbtais moksliniais tyrimais

Google Play badgeApp Store badge