|PROSITE documentation PDOC00336
Phosphofructokinase (EC 184.108.40.206) (PFK) [1,2] is a key regulatory enzyme in
the glycolytic pathway. It catalyzes the phosphorylation by ATP of fructose
6-phosphate to fructose 1,6-bisphosphate. In bacteria PFK is a tetramer of
identical 36 Kd subunits. In mammals it is a tetramer of 80 Kd subunits. Each
80 Kd subunit consist of two homologous domains which are highly related to
the bacterial 36 Kd subunits. In Human there are three, tissue-specific, types
of PFK isozymes: PFKM (muscle), PFKL (liver), and PFKP (platelet). In yeast
PFK is an octamer composed of four 100 Kd α chains (gene PFK1) and four
100 Kd β chains (gene PFK2); like the mammalian 80 Kd subunits, the yeast
100 Kd subunits are composed of two homologous domains.
As a signature pattern for PFK we selected a region that contains three basic
residues involved in fructose-6-phosphate binding.
Escherichia coli has two phosphofructokinase isozymes which are encoded
by genes pfkA (major) and pfkB (minor). The pfkB isozyme is not evolutionary
related to other prokaryotic or eukaryotic PFK's (see <PDOC00504>).
April 2006 / Pattern revised.
PROSITE method (with tools and information) covered by this documentation:
|PHOSPHOFRUCTOKINASE, PS00433; Phosphofructokinase signature (PATTERN)
The R/K, the H and the Q/R are involved in fructose-6-P binding
|Sequences known to belong to this class detected by the pattern:
|Other sequence(s) detected in Swiss-Prot:
|Matching PDB structures:
1MTO 1PFK 1ZXX 2PFK ... [ALL]
||Poorman R.A., Randolph A., Kemp R.G., Heinrikson R.L.
||Evolution of phosphofructokinase--gene duplication and creation of new effector sites.
||Heinisch J., Ritzel R.G., von Borstel R.C., Aguilera A., Rodicio R., Zimmermann F.K.
||The phosphofructokinase genes of yeast evolved from two duplication events.
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