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Literature summary extracted from

  • Fushinobu, S.; Nishimasu, H.; Hattori, D.; Song, H.J.; Wakagi, T.
    Structural basis for the bifunctionality of fructose-1,6-bisphosphate aldolase/phosphatase (2011), Nature, 478, 538-541.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.2.13 sitting-drop vapour-diffusion method at 25°C, crystallization of the enzyme in the presence of glycerone phosphate and Mg2+, determination of the crystal structure at 1.5 A resolution. Crystal structure of the bifunctional enzyme (fructose-bisphosphate aldolase/fructose-bisphosphatase) at 1.5 A resolution in the aldolase form, where a critical lysine residue forms a Schiff base with glycerone phosphate. A structural comparison of the aldolase form with a phosphatase form reveals a dramatic conformational change in the active site, demonstrating that the enzyme metamorphoses its active-site architecture to exhibit dual activities Sulfurisphaera tokodaii

Protein Variants

EC Number Protein Variants Comment Organism
3.1.3.11 Y229F the kcat/Km-value of the bifunctional enzyme (EC 3.1.3.11/EC 4.1.2.13) for D-fructose 1,6-bisphosphate is 1.1fold higher than the wild-type value, no fructose-bisphosphate aldolase activity Sulfurisphaera tokodaii
3.1.3.11 Y348F the kcat/Km-value of the bifunctional enzyme (EC 3.1.3.11/EC 4.1.2.13) for D-fructose 1,6-bisphosphate is 3.5fold lower than the wild-type value, the kcat/Km-value for the fructose-bisphosphate aldolase reaction of the bifunctional enzyme (EC 3.1.3.11/EC 4.1.2.13) in the anabolic direction is 16fold lower than wild-type value Sulfurisphaera tokodaii
4.1.2.13 Y229F the kcat/Km-value of the bifunctional enzyme (EC 3.1.3.11/EC 4.1.2.13) for D-fructose 1,6-bisphosphate is 1.1fold higher than the wild-type value, no fructose-bisphosphate aldolase activity Sulfurisphaera tokodaii
4.1.2.13 Y348F the kcat/Km-value of the bifunctional enzyme (EC 3.1.3.11/EC 4.1.2.13) for D-fructose 1,6-bisphosphate is 3.5fold lower than the wild-type value, the kcat/Km-value for the fructose-bisphosphate aldolase reaction of the bifunctional enzyme (EC 3.1.3.11/EC 4.1.2.13) in the anabolic direction is 16fold lower than wild-type value Sulfurisphaera tokodaii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.3.11 0.027
-
 D-fructose 1,6-bisphosphate pH 7.8, 48°C, mutant enzyme Y229F Sulfurisphaera tokodaii
3.1.3.11 0.027
-
 D-fructose 1,6-bisphosphate pH 7.8, 48°C, wild-type enzyme Sulfurisphaera tokodaii
3.1.3.11 0.036
-
 D-fructose 1,6-bisphosphate pH 7.8, 48°C, mutant enzyme Y348F Sulfurisphaera tokodaii
4.1.2.13 0.19
-
 D-glyceraldehyde 3-phosphate pH 8.0, 48°C, wild-type enzyme Sulfurisphaera tokodaii
4.1.2.13 0.19
-
 glycerone phosphate pH 8.0, 48°C, wild-type enzyme Sulfurisphaera tokodaii
4.1.2.13 0.34
-
 D-glyceraldehyde 3-phosphate pH 8.0, 48°C, mutant enzyme Y348F Sulfurisphaera tokodaii
4.1.2.13 0.34
-
 glycerone phosphate pH 8.0, 48°C, mutant enzyme Y348F Sulfurisphaera tokodaii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.2.13 Mg2+ the glycerone phosphate group coordinates three Mg2+ ions (Mg2–Mg4) Sulfurisphaera tokodaii

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.11 Sulfurisphaera tokodaii F9VMT6
-
-
3.1.3.11 Sulfurisphaera tokodaii 7 F9VMT6
-
-
4.1.2.13 Sulfurisphaera tokodaii F9VMT6
-
-
4.1.2.13 Sulfurisphaera tokodaii 7 F9VMT6
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.11 D-fructose 1,6-bisphosphate + H2O the bifunctional enzyme also shows activity of EC 4.1.2.13. The crystal structures of the enzyme in the two forms reveals that it achieves its bifunctionality by transforming its active-site architecture, through the toggle switch-like motions of the three mobile loop regions Sulfurisphaera tokodaii D-fructose 6-phosphate + phosphate
-
 r
3.1.3.11 D-fructose 1,6-bisphosphate + H2O the bifunctional enzyme also shows activity of EC 4.1.2.13. The crystal structures of the enzyme in the two forms reveals that it achieves its bifunctionality by transforming its active-site architecture, through the toggle switch-like motions of the three mobile loop regions Sulfurisphaera tokodaii 7 D-fructose 6-phosphate + phosphate
-
 r
4.1.2.13 Glycerone phosphate + D-glyceraldehyde 3-phosphate the bifunctional enzyme also shows activity of EC 3.1.3.11. The crystal structures of the enzyme in the two forms reveals that it achieves its bifunctionality by transforming its active-site architecture, through the toggle switch-like motions of the three mobile loop regions Sulfurisphaera tokodaii D-Fructose 1,6-bisphosphate
-
 r
4.1.2.13 Glycerone phosphate + D-glyceraldehyde 3-phosphate the bifunctional enzyme also shows activity of EC 3.1.3.11. The crystal structures of the enzyme in the two forms reveals that it achieves its bifunctionality by transforming its active-site architecture, through the toggle switch-like motions of the three mobile loop regions Sulfurisphaera tokodaii 7 D-Fructose 1,6-bisphosphate
-
 r

Synonyms

EC Number Synonyms Comment Organism
3.1.3.11 FBP aldolase/phosphatase bifunctional enzyme EC 3.1.3.11/EC 4.1.2.13 Sulfurisphaera tokodaii
3.1.3.11 FBPA/P bifunctional enzyme EC 3.1.3.11/EC 4.1.2.13 Sulfurisphaera tokodaii
3.1.3.11 fructose-1,6-bisphosphate aldolase/phosphatase bifunctional enzyme EC 3.1.3.11/EC 4.1.2.13 Sulfurisphaera tokodaii
3.1.3.11 STK_03180 locus name. The bifunctional enzyme also shows activity of EC 4.1.2.13 Sulfurisphaera tokodaii
4.1.2.13 FBP aldolase/phosphatase bifunctional enzyme EC 3.1.3.11/EC 4.1.2.13 Sulfurisphaera tokodaii
4.1.2.13 FBPA/P bifunctional enzyme EC 3.1.3.11/EC 4.1.2.13 Sulfurisphaera tokodaii
4.1.2.13 fructose-1,6-bisphosphate aldolase/phosphatase bifunctional enzyme EC 3.1.3.11/EC 4.1.2.13 Sulfurisphaera tokodaii
4.1.2.13 STK_03180 locus name. The bifunctional enzyme also shows activity of EC 3.1.3.11 Sulfurisphaera tokodaii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.3.11 48
-
 assay at Sulfurisphaera tokodaii

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.3.11 0.26
-
 D-fructose 1,6-bisphosphate pH 7.8, 48°C, mutant enzyme Y348F Sulfurisphaera tokodaii
3.1.3.11 0.62
-
 D-fructose 1,6-bisphosphate pH 7.8, 48°C, wild-type enzyme Sulfurisphaera tokodaii
3.1.3.11 0.66
-
 D-fructose 1,6-bisphosphate pH 7.8, 48°C, mutant enzyme Y229F Sulfurisphaera tokodaii
4.1.2.13 0.026
-
 D-fructose 1,6-bisphosphate pH 8.0, 48°C, mutant enzyme Y348F Sulfurisphaera tokodaii
4.1.2.13 0.027
-
 D-fructose 1,6-bisphosphate pH 8.0, 48°C, wild-type enzyme Sulfurisphaera tokodaii
4.1.2.13 0.1
-
 D-glyceraldehyde 3-phosphate pH 8.0, 48°C, mutant enzyme Y348F Sulfurisphaera tokodaii
4.1.2.13 0.1
-
 glycerone phosphate pH 8.0, 48°C, mutant enzyme Y348F Sulfurisphaera tokodaii
4.1.2.13 0.91
-
 D-glyceraldehyde 3-phosphate pH 8.0, 48°C, wild-type enzyme Sulfurisphaera tokodaii
4.1.2.13 0.91
-
 glycerone phosphate pH 8.0, 48°C, wild-type enzyme Sulfurisphaera tokodaii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.3.11 7.8
-
 assay at Sulfurisphaera tokodaii

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.1.3.11 7.2
-
 D-fructose 1,6-bisphosphate pH 7.8, 48°C, mutant enzyme Y348F Sulfurisphaera tokodaii
3.1.3.11 23
-
 D-fructose 1,6-bisphosphate pH 7.8, 48°C, wild-type enzyme Sulfurisphaera tokodaii
3.1.3.11 25
-
 D-fructose 1,6-bisphosphate pH 7.8, 48°C, mutant enzyme Y229F Sulfurisphaera tokodaii
4.1.2.13 0.29
-
 D-glyceraldehyde 3-phosphate pH 8.0, 48°C, mutant enzyme Y348F Sulfurisphaera tokodaii
4.1.2.13 0.29
-
 glycerone phosphate pH 8.0, 48°C, mutant enzyme Y348F Sulfurisphaera tokodaii
4.1.2.13 4.7
-
 D-glyceraldehyde 3-phosphate pH 8.0, 48°C, wild-type enzyme Sulfurisphaera tokodaii
4.1.2.13 4.7
-
 glycerone phosphate pH 8.0, 48°C, wild-type enzyme Sulfurisphaera tokodaii