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Literature summary extracted from

  • Mizuguchi, H.; Cook, P.F.; Hasemann, C.A.; Uyeda, K.
    Chemical mechanism of the fructose-6-phosphate,2-kinase reaction from the pH dependence of kinetic parameters of site-directed mutants of active site basic residues (1997), Biochemistry, 36, 8775-8784.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.105
-
 Rattus norvegicus

Protein Variants

EC Number Protein Variants Comment Organism
2.7.1.105 K172A increase in Km of beta-D-fructose 6-phosphate Rattus norvegicus
2.7.1.105 K172E increase in Km of MgATP2-, increase in Km of beta-D-fructose 6-phosphate Rattus norvegicus
2.7.1.105 K172H increase in Km of MgATP2- Rattus norvegicus
2.7.1.105 K172R increase in Km of beta-D-fructose 6-phosphate Rattus norvegicus
2.7.1.105 K51A increase in Km of beta-D-fructose 6-phosphate Rattus norvegicus
2.7.1.105 K51H increase in Km of MgATP2-, increase in Km of beta-D-fructose 6-phosphate Rattus norvegicus
2.7.1.105 additional information ATP binding and the effect of pH on the kinetics are characterized Rattus norvegicus
2.7.1.105 R136K increase in Km of MgATP2- Rattus norvegicus
2.7.1.105 R136L increase in Km of beta-D-fructose 6-phosphate Rattus norvegicus
2.7.1.105 R193H increase in Km of MgATP2-, increase in Km of beta-D-fructose 6-phosphate Rattus norvegicus
2.7.1.105 R193L increase in Km of beta-D-fructose 6-phosphate Rattus norvegicus
2.7.1.105 R78H increase in Km of MgATP2- Rattus norvegicus
2.7.1.105 R78L increase in Km of MgATP2- Rattus norvegicus
2.7.1.105 R79H increase in Km of MgATP2- Rattus norvegicus
2.7.1.105 R79L increase in Km of MgATP2- Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.1.105 additional information
-
 additional information
-
 Rattus norvegicus
2.7.1.105 0.04
-
 beta-D-fructose 6-phosphate pH 7.5, 30°C, wild-type enzyme, testis Rattus norvegicus
2.7.1.105 0.1
-
 ATP pH 7.5, 30°C, testis Rattus norvegicus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.105 Mg2+ K51 is essential for binding of Mg(mantATP) Rattus norvegicus

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.1.105 mutant enzyme 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 additional information also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46) Rattus norvegicus ?
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.1.105 30
-
 assay at Rattus norvegicus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.1.105 additional information
-
 additional information comparison of kcat/Km values of wild-type and mutant enzymes Rattus norvegicus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.1.105 additional information
-
 comparison of pH-profiles of wild-type and mutant enzymes Rattus norvegicus
2.7.1.105 7.3 8.4 wild-type enzyme Rattus norvegicus