Literature summary for 2.7.1.105 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.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
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	-	?
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

Organism	UniProt	Comment	Textmining
Rattus norvegicus	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
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

Source Tissue	Comment	Organism	Textmining
testis	-	Rattus norvegicus	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
ATP + beta-D-fructose 6-phosphate	-	Rattus norvegicus	ADP + beta-D-fructose 2,6-bisphosphate	-	r
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	-	?
ATP + beta-D-fructose 6-phosphate	responsible for regulation of fructose 2,6-bisphosphate-concentration	Rattus norvegicus	ADP + beta-D-fructose 2,6-bisphosphate	-	?
additional information	also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)	Rattus norvegicus	?	-	?

Subunits

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