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J. Biol. Chem., Vol. 276, Issue 24, 20966-20972, June 15, 2001
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From the Departments of Pyruvate kinase (PK) from the cyanobacterium
Synechococcus PCC 6301 was purified 1,300-fold to
electrophoretic homogeneity and a final specific activity of 222 µmol
of pyruvate produced/min/mg of protein. The enzyme was shown to have a
pI of 5.7 and to exist as a 280-kDa homotetramer composed of 66-kDa
subunits. This PK appears to be immunologically related to
Bacillus PK and a green algal chloroplast PK, but not to
rabbit muscle PK, or vascular plant cytosolic and plastidic PKs. The
N-terminal amino acid sequence of the Synechococcus PK
exhibited maximal (67%) identity with the corresponding region of a
putative PK-A sequence deduced from the genome of the cyanobacterium,
Synechocystis PCC 6803. Synechococcus PK was
relatively heat-labile and displayed a broad pH optimum around pH 7.0. Its activity was not influenced by K+, but required high
concentrations of Mg2+, and was relatively nonspecific with
respect to the nucleoside diphosphate substrate. Potent allosteric
regulation by various effectors was observed (activators: hexose
monophosphates, ribose 5-phosphate, glycerol 3-phosphate, and AMP;
inhibitors: fructose 1,6-bisphosphate, inorganic phosphate, ATP, and
several Krebs' cycle intermediates). The enzyme exhibited marked
positive cooperativity for phosphoenolpyruvate, which was eliminated or
reduced by the presence of the allosteric activators. The results are
discussed in terms of the phylogeny and probable central role of PK in
the control of cyanobacterial glycolysis.
Structural and Regulatory Properties of Pyruvate Kinase from the
Cyanobacterium Synechococcus PCC 6301*
,, Biology and
§ Biochemistry, Queen's University, Kingston,
Ontario K7L 3N6, Canada
*
This work was supported by research and equipment grants
from the Natural Sciences and Engineering Research Council of Canada (NSERC) (to W. C. P.).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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