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https://olympias.lib.uoi.gr/jspui/handle/123456789/9771Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Koukkou, A. I. | en |
| dc.contributor.author | Drainas, C. | en |
| dc.contributor.author | Rohmer, M. | en |
| dc.date.accessioned | 2015-11-24T16:51:42Z | - |
| dc.date.available | 2015-11-24T16:51:42Z | - |
| dc.identifier.issn | 0378-1097 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/9771 | - |
| dc.rights | Default Licence | - |
| dc.subject | zymomonas mobilis | en |
| dc.subject | squalene synthase | en |
| dc.subject | triterpenes | en |
| dc.subject | hopanoid | en |
| dc.subject | squalene | en |
| dc.subject | partial-purification | en |
| dc.subject | biosynthesis | en |
| dc.subject | hopanoids | en |
| dc.subject | synthetase | en |
| dc.title | Towards the characterization of squalene synthase activity in extracts of Zymomonas mobilis | en |
| heal.type | journalArticle | - |
| heal.type.en | Journal article | en |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.identifier.primary | DOI 10.1111/j.1574-6968.1996.tb08349.x | - |
| heal.identifier.secondary | <Go to ISI>://A1996UX51900028 | - |
| heal.identifier.secondary | http://onlinelibrary.wiley.com/store/10.1111/j.1574-6968.1996.tb08349.x/asset/j.1574-6968.1996.tb08349.x.pdf?v=1&t=hmsyb38i&s=afb51b7a1b26d254e44af7be46bc1c0dac02b1fa | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας | el |
| heal.publicationDate | 1996 | - |
| heal.abstract | Extracts of Zymomonas mobilis in the presence of NADPH converted tritium-labelled farnesyl diphosphate (FPP) into squalene, resulting from the activity of squalene synthase, as well as diploptene and diplopterol, derived from further squalene cyclisation. An unidentified isoprenoid representing up to 70% of the conversion products of FPP and different from presqualene alcohol was also formed, even in the absence of NADPH. Addition of squalestatin 1, an inhibitor of squalene synthase, blocked biosynthesis from FPP of the three former triterpenes, in accordance with the role of squalene synthase in their formation, as well as that of the unknown compound. | en |
| heal.publisher | Wiley-Blackwell | en |
| heal.journalName | FEMS Microbiol Lett | en |
| heal.journalType | peer reviewed | - |
| heal.fullTextAvailability | TRUE | - |
| Appears in Collections: | Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ | |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| Koukkou-1996-Towards the characte.pdf | 385.91 kB | Adobe PDF | View/Open Request a copy |
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