ExplorEnz: EC 2.7.1.11

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2.7.1.11

Accepted name:

6-phosphofructokinase

Reaction:

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate

Other name(s):

phosphohexokinase; phosphofructokinase I; phosphofructokinase (phosphorylating); 6-phosphofructose 1-kinase; ATP-dependent phosphofructokinase; D-fructose-6-phosphate 1-phosphotransferase; fructose 6-phosphate kinase; fructose 6-phosphokinase; nucleotide triphosphate-dependent phosphofructokinase; phospho-1,6-fructokinase; PFK

Systematic name:

ATP:D-fructose-6-phosphate 1-phosphotransferase

Comments:

D-Tagatose 6-phosphate and sedoheptulose 7-phosphate can act as acceptors. UTP, CTP and ITP can act as donors. Not identical with EC 2.7.1.105 6-phosphofructo-2-kinase.

Links to other databases:

BRENDA, EXPASY, GTD, KEGG, METACYC, PDB, CAS registry number: 9001-80-3

References:

1.	Axelrod, B., Saltman, P., Bandurski, R.S. and Baker, R.S. Hexokinase in higher plants. J. Biol. Chem. 197 (1952) 89–96. [PMID: 12981037]
2.	Ling, K.H., Pastkau, V., Marcus, F. and Lardy, H.A. Phosphofructokinase. I. Skeletal muscle. Methods Enzymol. 9 (1966) 425–429.
3.	Mansour, T.E. Phosphofructokinase. II. Heart muscle. Methods Enzymol. 9 (1966) 430–436.
4.	Odeide, R., Guilloton, M., Dupuis, B., Ravon, D. and Rosenberg, A.J. Study of an enzyme allosteric to 2 substrates: phosphofructokinase of rat muscle. I. Preparation and crystallization of the enzyme. Bull. Soc. Chim. Biol. 50 (1968) 2023–2033. [PMID: 4237772]
5.	Parmeggiano, A., Luft, J.H., Love, D.S. and Krebs, E.G. Crystallization and properties of rabbit skeletal muscle phosphofructokinase. J. Biol. Chem. 241 (1966) 4625–4637. [PMID: 4224472]
6.	Racker, E. Spectrophotometric measurement of hexokinase and phosphohexokinase activity. J. Biol. Chem. 167 (1947) 843–854.
7.	Sols, A. and Salas, M.L. Phosphofructokinase. III. Yeast. Methods Enzymol. 9 (1966) 436–442.
8.	Uyeda, K. and Kurooka, S. Crystallization and properties of phosphofructokinase from Clostridium pasteurianum. J. Biol. Chem. 245 (1970) 3315–3324. [PMID: 4248230]

[EC 2.7.1.11 created 1961]