Affiliation:
1. FB 9 Mikrobiologie, Universität GH Essen, D-45117 Essen,1 and
2. Institut für Mikrobiologie und Genetik, Universität Göttingen, D-37077 Göttingen,2Germany
Abstract
ABSTRACT
Flux into the glycolytic pathway of most cells is controlled via allosteric regulation of the irreversible, committing step catalyzed by ATP-dependent phosphofructokinase (PFK) (ATP-PFK; EC
2.7.1.11
), the key enzyme of glycolysis. In some organisms, the step is catalyzed by PP
i
-dependent PFK (PP
i
-PFK; EC
2.7.1.90
), which uses PP
i
instead of ATP as the phosphoryl donor, conserving ATP and rendering the reaction reversible under physiological conditions. We have determined the enzymic properties of PP
i
-PFK from the anaerobic, hyperthermophilic archaeon
Thermoproteus tenax
, purified the enzyme to homogeneity, and sequenced the gene. The ∼100-kDa PP
i
-PFK from
T. tenax
consists of 37-kDa subunits; is not regulated by classical effectors of ATP-PFKs such as ATP, ADP, fructose 2,6-bisphosphate, or metabolic intermediates; and shares 20 to 50% sequence identity with known PFK enzymes. Phylogenetic analyses of biochemically characterized PFKs grouped the enzymes into three monophyletic clusters: PFK group I represents only classical ATP-PFKs from
Bacteria
and
Eucarya
; PFK group II contains only PP
i
-PFKs from the genus
Propionibacterium
, plants, and amitochondriate protists; whereas group III consists of PFKs with either cosubstrate specificity, i.e., the PP
i
-dependent enzymes from
T. tenax
and
Amycolatopsis methanolica
and the ATP-PFK from
Streptomyces coelicolor
. Comparative analyses of the pattern of conserved active-site residues strongly suggest that the group III PFKs originally bound PP
i
as a cosubstrate.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
84 articles.
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