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Literature summary for 2.7.1.90 extracted from

  • Arimoto, T.; Ansai, T.; Yu, W.; Turner, A.J.; Takehara, T.
    Kinetic analysis of PPi-dependent phosphofructokinase from Porphyromonas gingivalis (2002), FEMS Microbiol. Lett., 207, 35-38.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli BL21(DE3) Porphyromonas gingivalis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.11
-
D-fructose 1,6-bisphosphate 37°C Porphyromonas gingivalis
2.2
-
D-fructose 6-phosphate 37°C Porphyromonas gingivalis

Organism

Organism UniProt Comment Textmining
Porphyromonas gingivalis Q9FAF8
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant from Escherichia coli, 32fold to homogeneity Porphyromonas gingivalis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
278
-
purified recombinant enzyme Porphyromonas gingivalis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
diphosphate + D-fructose 6-phosphate equilibrium lies in reverse direction Porphyromonas gingivalis phosphate + D-fructose 1,6-bisphosphate
-
r
diphosphate + D-fructose 6-phosphate specific for diphosphate as phosphor donor Porphyromonas gingivalis phosphate + D-fructose 1,6-bisphosphate
-
r

Synonyms

Synonyms Comment Organism
FBPase
-
Porphyromonas gingivalis
fructose 1,6-bisphosphatase
-
Porphyromonas gingivalis
PFP
-
Porphyromonas gingivalis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Porphyromonas gingivalis