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https://olympias.lib.uoi.gr/jspui/handle/123456789/9563Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Malandrinos, G. | en |
| dc.contributor.author | Louloudi, M. | en |
| dc.contributor.author | Hadjiliadis, N. | en |
| dc.date.accessioned | 2015-11-24T16:50:04Z | - |
| dc.date.available | 2015-11-24T16:50:04Z | - |
| dc.identifier.issn | 0020-1693 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/9563 | - |
| dc.rights | Default Licence | - |
| dc.subject | thiamin complexes | en |
| dc.subject | metal complexes | en |
| dc.subject | thiamin catalysis | en |
| dc.subject | diphosphate-dependent enzymes | en |
| dc.subject | crystal-structure | en |
| dc.subject | pyruvate decarboxylase | en |
| dc.subject | angstrom resolution | en |
| dc.subject | metal-complexes | en |
| dc.subject | transketolase | en |
| dc.subject | model | en |
| dc.subject | cadmium(ii) | en |
| dc.subject | catalysis | en |
| dc.subject | zinc(ii) | en |
| dc.title | Ternary systems of Zn2+ and Cd2+, 2-(alpha-hydroxyethyl)thiamin pyrophosphate (HETPP) and the pentapeptide Asp-Asp-Asn-Lys-Ile. Implications for the mechanism of thiamin enzymes | en |
| heal.type | journalArticle | - |
| heal.type.en | Journal article | en |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.identifier.primary | Doi 10.1016/S0020-1693(03)00056-2 | - |
| heal.identifier.secondary | <Go to ISI>://000183673100039 | - |
| heal.identifier.secondary | http://ac.els-cdn.com/S0020169303000562/1-s2.0-S0020169303000562-main.pdf?_tid=476f9e880788118e9166e29aede6dd60&acdnat=1333034595_e249a4bde8a744ca4d1bf687bccc799a | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας | el |
| heal.publicationDate | 2003 | - |
| heal.abstract | To obtain structural information on the active-site of thiamin-dependent enzymes in solution, the interaction of Zn2+ and Cd2+ ions with the pentapeptide Asp-Asp-Asn-Lys-Ile surrounding the thiamin pyrophosphate moiety in the transketolase enzyme, and the tertiary Zn2+/or Cd2+-pentapeptide-HETPP systems have been studied by NMR spectroscopy in aqueous solutions at physiological pH. The HETPP, 2-(alpha-hydroxyethyl)thiamin pyrophosphate, represents an active intermediate of thiamin catalytic cycle formed after the addition of pyruvate substrate on thiamin molecule. The present data show the existence of the tertiary metal-[pentapeptide]-[HETPP] complexes at physiological pH, where the metal coordination sphere is completed by both peptide backbone and HETPP molecule. The metal coordinated HETPP molecule adopts the so-called S conformation in solution. The importance of the present findings correlated with previous results is discussed and possible functional implications are suggested. (C) 2003 Elsevier Science B.V. All rights reserved. | en |
| heal.publisher | Elsevier | en |
| heal.journalName | Inorganica Chimica Acta | 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 | |
|---|---|---|---|---|
| Malandrinos-2003-Ternary systems of Z.pdf | 214.99 kB | Adobe PDF | View/Open Request a copy |
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