Batista, Ana P. ; Kletzin, Arnulf ; Pereira, Manuela M. (2008)
The dihydrolipoamide dehydrogenase from the crenarchaeon Acidianus ambivalens.
In: FEMS microbiology letters, 281 (2)
Artikel, Bibliographie
Kurzbeschreibung (Abstract)
A dihydrolipoamide dehydrogenase (DLDH) was purified and characterized for the first time from a crenarchaeon, Acidianus ambivalens. The holoenzyme consists of two identical subunits with a molecular mass of 45.4 kDa per monomer. It contains FAD as a prosthetic group and uses NAD+ as the preferential substrate, but can also reduce NADP+. The Michaelis-Menten constants of the forward (NAD+ reduction) and reverse (NADH oxidation) reactions were KM (dihydrolipoamide)=0.70 mM, KM (NAD+)=0.71 mM, KM (lipoamide)=1.26 mM and KM (NADH)=3.15 microM. A comparative study of NADH:lipoamide oxidoreductase and NADH:K3[Fe(CN)6] oxidoreductase activities was performed, the optimal temperature and pH being different for each: 55 degrees C, pH 7 and 89 degrees C, pH 5.5, respectively. Although DLDH is generally part of the alpha-ketoacid dehydrogenase complexes in Bacteria and Eukarya, none of these complexes has yet been isolated from Sulfolobales. The metabolic role of DLDH in these organisms is discussed.
| Typ des Eintrags: | Artikel |
|---|---|
| Erschienen: | 2008 |
| Autor(en): | Batista, Ana P. ; Kletzin, Arnulf ; Pereira, Manuela M. |
| Art des Eintrags: | Bibliographie |
| Titel: | The dihydrolipoamide dehydrogenase from the crenarchaeon Acidianus ambivalens. |
| Sprache: | Englisch |
| Publikationsjahr: | 2008 |
| Titel der Zeitschrift, Zeitung oder Schriftenreihe: | FEMS microbiology letters |
| Jahrgang/Volume einer Zeitschrift: | 281 |
| (Heft-)Nummer: | 2 |
| Kurzbeschreibung (Abstract): | A dihydrolipoamide dehydrogenase (DLDH) was purified and characterized for the first time from a crenarchaeon, Acidianus ambivalens. The holoenzyme consists of two identical subunits with a molecular mass of 45.4 kDa per monomer. It contains FAD as a prosthetic group and uses NAD+ as the preferential substrate, but can also reduce NADP+. The Michaelis-Menten constants of the forward (NAD+ reduction) and reverse (NADH oxidation) reactions were KM (dihydrolipoamide)=0.70 mM, KM (NAD+)=0.71 mM, KM (lipoamide)=1.26 mM and KM (NADH)=3.15 microM. A comparative study of NADH:lipoamide oxidoreductase and NADH:K3[Fe(CN)6] oxidoreductase activities was performed, the optimal temperature and pH being different for each: 55 degrees C, pH 7 and 89 degrees C, pH 5.5, respectively. Although DLDH is generally part of the alpha-ketoacid dehydrogenase complexes in Bacteria and Eukarya, none of these complexes has yet been isolated from Sulfolobales. The metabolic role of DLDH in these organisms is discussed. |
| Fachbereich(e)/-gebiet(e): | 10 Fachbereich Biologie > Sulfur Biochemistry and Microbial Bioenergetics ?? fb10_mikrobiologie ?? 10 Fachbereich Biologie |
| Hinterlegungsdatum: | 01 Sep 2009 10:28 |
| Letzte Änderung: | 05 Mär 2013 09:22 |
| PPN: | |
| Export: | |
| Suche nach Titel in: | TUfind oder in Google |
 |
Frage zum Eintrag |
Optionen (nur für Redakteure)
 |
Redaktionelle Details anzeigen |
Drucken
Impressum