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J. Biol. Chem., Vol. 276, Issue 31, 28710-28718, August 3, 2001
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From the 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 PPi-dependent
phosphofructokinase. As revealed by phylogenetic analyses, orthologs of
the T. tenax and P. furiosus enzyme appear to
be present in almost all sequenced archaeal genomes, as well as in some
bacterial genomes, strongly suggesting that this new enzyme family
represents the typical archaeal FBP aldolase. Because this new family
shows no significant sequence similarity to classical Class I and II
enzymes, a new name is proposed, archaeal type Class I FBP aldolases
(FBP aldolase Class IA).
Archaeal Fructose-1,6-bisphosphate Aldolases Constitute a New
Family of Archaeal Type Class I Aldolase*
§,,,
, Department of Microbiology,
Universität Essen, 45117 Essen, the ¶ Institute of
Evolutionary Biology, Department of Biology, Universität
Konstanz, 78547 Konstanz, the Institute of Biotechnology,
Department of Biochemistry and Biotechnology,
Martin-Luther-Universität Halle, 06120 Halle (Saale), Germany,
and the ** Laboratory of Microbiology, Wageningen University,
NL-6703 CT Wageningen, The Netherlands
*
This work was supported by the Deutsche
Forschungsgemeinschaft and by the Earth and Life Sciences Foundation,
which is subsidized by the Netherlands Organization for Scientific
Research.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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