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Literature summary extracted from

  • Hasemann, C.A.; Istvan, E.S.; Uyeda, K.; Deisenhofer, J.
    The crystal structure of the bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase reveals distinct domain homologies (1996), Structure, 4, 1017-1029.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.1.105 the crystal structure of mutant enzyme, the two subunits in the homodimer are arranged in a head-to-head manner, each monomer consists of independent kinase and phosphatase domains, the kinase domains are in close contact, forming an extended hydrophobic core between them, while the phosphatase domains are essentially independent of one another, enzyme is related to the nucleotide monophosphate kinases, and the catalytic domain of G proteins Rattus norvegicus

Protein Variants

EC Number Protein Variants Comment Organism
2.7.1.105 additional information mutant enzyme, in which the four tryptophan residues in the isoenzyme are mutated to phenylalanine, structure Rattus norvegicus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.1.105 55000
-
 2 * 55000, SDS-PAGE Rattus norvegicus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.1.105 ATP + beta-D-fructose 6-phosphate Rattus norvegicus enzyme plays an indirect yet key role in the regulation of glucose metabolism ADP + beta-D-fructose 2,6-bisphosphate
-
 ?
2.7.1.105 ATP + beta-D-fructose 6-phosphate Rattus norvegicus responsible for regulation of fructose 2,6-bisphosphate-concentration ADP + beta-D-fructose 2,6-bisphosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.105 Rattus norvegicus
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.7.1.105 ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate bifunctional protein: 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase, reverse reaction catalysed by fructose 2,6-bisphosphatase: 3.1.3.46 Rattus norvegicus
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.1.105 testis
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.105 ATP + beta-D-fructose 6-phosphate
-
 Rattus norvegicus ADP + beta-D-fructose 2,6-bisphosphate
-
 r
2.7.1.105 ATP + beta-D-fructose 6-phosphate enzyme plays an indirect yet key role in the regulation of glucose metabolism Rattus norvegicus ADP + beta-D-fructose 2,6-bisphosphate
-
 ?
2.7.1.105 ATP + beta-D-fructose 6-phosphate responsible for regulation of fructose 2,6-bisphosphate-concentration Rattus norvegicus ADP + beta-D-fructose 2,6-bisphosphate
-
 ?
2.7.1.105 additional information also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46) Rattus norvegicus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.1.105 dimer 2 * 55000, SDS-PAGE Rattus norvegicus