Evidence for an operative glyoxylate cycle in the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius

Helge Uhrigshardt, Michael Walden, Harald John, Arnd Petersen, Stefan Anemüller*

*Korrespondierende/r Autor/-in für diese Arbeit
22 Zitate (Scopus)

Abstract

Both key enzymes for the glyoxylate cycle, isocitrate lyase (EC 4.1.3.1) and malate synthase (EC 4.1.3.2), were purified and characterized from the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius. Whereas the former enzyme was copurified with the aconitase, the latter enzyme could be enriched to apparent homogeneity. Amino acid sequencing of three internal peptides of the isocitrate lyase revealed the presence of highly conserved residues. With respect to cofactor requirement and quarternary structure the crenarchaeal malate synthase might represent a novel type of this enzyme family. High activities of both glyoxylate cycle enzymes could already be detected in extracts of glucose grown cells and both increased about two-fold in extracts of acetate grown cells.

OriginalspracheEnglisch
ZeitschriftFEBS Letters
Jahrgang513
Ausgabenummer2-3
Seiten (von - bis)223-229
Seitenumfang7
ISSN0014-5793
DOIs
PublikationsstatusVeröffentlicht - 27.02.2002

Strategische Forschungsbereiche und Zentren

  • Forschungsschwerpunkt: Infektion und Entzündung - Zentrum für Infektions- und Entzündungsforschung Lübeck (ZIEL)

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