Jun 2, 2001

Archaeal fructose-1,6-bisphosphate aldolases constitute a new family of archaeal type class I aldolase

The Journal of Biological Chemistry
Bettina SiebersCorné H Verhees

Abstract

Fructose-1,6-bisphosphate (FBP) aldolase activity has been detected previously in several Archaea. However, no obvious orthologs of the bacterial and eucaryal Class I and II FBP aldolases have yet been identified in sequenced archaeal genomes. Based on a recently described novel type of bacterial aldolase, we report on the identification and molecular characterization of the first archaeal FBP aldolases. We have analyzed the FBP aldolases of two hyperthermophilic Archaea, the facultatively heterotrophic Crenarchaeon Thermoproteus tenax and the obligately heterotrophic Euryarchaeon Pyrococcus furiosus. For enzymatic studies the fba genes of T. tenax and P. furiosus were expressed in Escherichia coli. The recombinant FBP aldolases show preferred substrate specificity for FBP in the catabolic direction and exhibit metal-independent Class I FBP aldolase activity via a Schiff-base mechanism. Transcript analyses reveal that the expression of both archaeal genes is induced during sugar fermentation. Remarkably, the fbp gene of T. tenax is co-transcribed with the pfp gene that codes for the reversible PP(i)-dependent phosphofructokinase. As revealed by phylogenetic analyses, orthologs of the T. tenax and P. furiosus enzyme appear to be...Continue Reading

Mentioned in this Paper

Trichomonas tenax
Phanaeus furiosus
Toechima tenax
Genome, Archaeal
PFKM
Fructose
Enzymes, antithrombotic
Transcription, Genetic
Proteins, Recombinant DNA
Mutagenesis, Site-Directed

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