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- Name help_outline β-D-fructose 6-phosphate Identifier CHEBI:57634 (Beilstein: 6422468) help_outline Charge -2 Formula C6H11O9P InChIKeyhelp_outline BGWGXPAPYGQALX-ARQDHWQXSA-L SMILEShelp_outline OC[C@@]1(O)O[C@H](COP([O-])([O-])=O)[C@@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 18 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline ATP Identifier CHEBI:30616 (Beilstein: 3581767) help_outline Charge -4 Formula C10H12N5O13P3 InChIKeyhelp_outline ZKHQWZAMYRWXGA-KQYNXXCUSA-J SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,284 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline β-D-fructose 1,6-bisphosphate Identifier CHEBI:32966 (Beilstein: 7104287) help_outline Charge -4 Formula C6H10O12P2 InChIKeyhelp_outline RNBGYGVWRKECFJ-ARQDHWQXSA-J SMILEShelp_outline O[C@H]1[C@H](O)[C@@](O)(COP([O-])([O-])=O)O[C@@H]1COP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 7 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline ADP Identifier CHEBI:456216 (Beilstein: 3783669) help_outline Charge -3 Formula C10H12N5O10P2 InChIKeyhelp_outline XTWYTFMLZFPYCI-KQYNXXCUSA-K SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 841 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,521 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:16109 | RHEA:16110 | RHEA:16111 | RHEA:16112 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Crystallization and properties of rabbit skeletal muscle phosphofructokinase.
Parmeggiani A., Luft J.H., Love D.S., Krebs E.G.
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Crystallization and properties of phosphofructokinase from Clostridium pasteurianum.
Uyeda K., Kurooka S.
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Phosphonexokinase in higher plants.
AXELROD B., SALTMAN P., BANDURSKI R.S., BAKER R.S.
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Structure and allosteric regulation of eukaryotic 6-phosphofructokinases.
Schoneberg T., Kloos M., Bruser A., Kirchberger J., Strater N.
Although the crystal structures of prokaryotic 6-phosphofructokinase, a key enzyme of glycolysis, have been available for almost 25 years now, structural information about the more complex and highly regulated eukaryotic enzymes is still lacking until now. This review provides an overview of the c ... >> More
Although the crystal structures of prokaryotic 6-phosphofructokinase, a key enzyme of glycolysis, have been available for almost 25 years now, structural information about the more complex and highly regulated eukaryotic enzymes is still lacking until now. This review provides an overview of the current knowledge of eukaryotic 6-phosphofructokinase based on recent crystal structures, kinetic analyses and site-directed mutagenesis data with special focus on the molecular architecture and the structural basis of allosteric regulation. << Less
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Crystal structure of human platelet phosphofructokinase-1 locked in an activated conformation.
Kloos M., Bruser A., Kirchberger J., Schoneberg T., Strater N.
Phosphofructokinase-1 (Pfk) acts as the main control point of flux through glycolysis. It is involved in complex allosteric regulation and Pfk mutations have been linked to cancer development. Whereas the 3D structure and structural basis of allosteric regulation of prokaryotic Pfk has been studie ... >> More
Phosphofructokinase-1 (Pfk) acts as the main control point of flux through glycolysis. It is involved in complex allosteric regulation and Pfk mutations have been linked to cancer development. Whereas the 3D structure and structural basis of allosteric regulation of prokaryotic Pfk has been studied in great detail, our knowledge about the molecular basis of the allosteric behaviour of the more complex mammalian Pfk is still very limited. To characterize the structural basis of allosteric regulation, the subunit interfaces and the functional consequences of modifications in Tarui's disease and cancer, we analysed the physiological homotetramer of human platelet Pfk at up to 2.67 Å resolution in two crystal forms. The crystallized enzyme is permanently activated by a deletion of the 22 C-terminal residues. Complex structures with ADP and fructose-6-phosphate (F6P) and with ATP suggest a role of three aspartates in the deprotonation of the OH-nucleophile of F6P and in the co-ordination of the catalytic magnesium ion. Changes at the dimer interface, including an asymmetry observed in both crystal forms, are the primary mechanism of allosteric regulation of Pfk by influencing the F6P-binding site. Whereas the nature of this conformational switch appears to be largely conserved in bacterial, yeast and mammalian Pfk, initiation of these changes differs significantly in eukaryotic Pfk. << Less
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[Study of an enzyme allosteric to 2 substrates: phosphofructokinase of rat muscle. I. Preparation and crystallization of the enzyme].
Odeide R., Guilloton M., Dupuis B., Ravon D., Rosenberg A.J.
Bull Soc Chim Biol (Paris) 50:2023-2033(1968) [PubMed] [EuropePMC]