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Literature summary for 3.1.3.11 extracted from

  • Du, J.; Say, R.F.; Lü, W.; Fuchs, G.; Einsle, O.
    Active-site remodelling in the bifunctional fructose-1,6-bisphosphate aldolase/phosphatase (2011), Nature, 478, 534-537.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
C-terminally His6-tagged enzyme is heterologously produced in Escherichia coli Pyrobaculum neutrophilum

Crystallization (Commentary)

Crystallization (Comment) Organism
crystals are grown at 20°C by the hanging-drop vapour-diffusion method. Three-dimensional structures of the enzyme in a ligand-free state as well as in complex with the substrates glycerone phosphate and D-glyceraldehyde 3-phosphate and the product D-fructose 1,6-bisphosphate to resolutions up to 1.3?A Pyrobaculum neutrophilum

Protein Variants

Protein Variants Comment Organism
D233N mutant protein is impaired in both aldolase and phosphatase activity Pyrobaculum neutrophilum
E357Q mutation abolishes phosphatase activity, no effect on aldolase activity Pyrobaculum neutrophilum
K232R mutation abolishes aldolase activity, phosphatase activity is enhanced Pyrobaculum neutrophilum
Y229F mutation abolishes aldolase activity, phosphatase activity is slightly reduced Pyrobaculum neutrophilum
Y358F mutation abolishes phosphatase activity, no effect on aldolase activity Pyrobaculum neutrophilum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-fructose 1,6-bisphosphate + H2O Pyrobaculum neutrophilum the bifunctional, thermostable enzyme (EC 4.1.2.13/EC 3.1.3.11) catalyses two subsequent steps in gluconeogenesis in most archaea and in deeply branching bacterial lineages D-fructose 6-phosphate + phosphate
-
?
D-fructose 1,6-bisphosphate + H2O Pyrobaculum neutrophilum DSM 2338 the bifunctional, thermostable enzyme (EC 4.1.2.13/EC 3.1.3.11) catalyses two subsequent steps in gluconeogenesis in most archaea and in deeply branching bacterial lineages D-fructose 6-phosphate + phosphate
-
?

Organism

Organism UniProt Comment Textmining
Pyrobaculum neutrophilum B1YAL1 i.e. Thermoproteus neutrophilus
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Pyrobaculum neutrophilum DSM 2338 B1YAL1 i.e. Thermoproteus neutrophilus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-fructose 1,6-bisphosphate + H2O the bifunctional, thermostable enzyme (EC 4.1.2.13/EC 3.1.3.11) catalyses two subsequent steps in gluconeogenesis in most archaea and in deeply branching bacterial lineages Pyrobaculum neutrophilum D-fructose 6-phosphate + phosphate
-
?
D-fructose 1,6-bisphosphate + H2O the bifunctional, thermostable enzyme (EC 4.1.2.13/EC 3.1.3.11) catalyses two subsequent steps in gluconeogenesis. It catalyses a multi-step reaction by remodelling its active site according to the respective catalytic requirements Pyrobaculum neutrophilum D-fructose 6-phosphate + phosphate
-
?
D-fructose 1,6-bisphosphate + H2O the bifunctional, thermostable enzyme (EC 4.1.2.13/EC 3.1.3.11) catalyses two subsequent steps in gluconeogenesis in most archaea and in deeply branching bacterial lineages Pyrobaculum neutrophilum DSM 2338 D-fructose 6-phosphate + phosphate
-
?
D-fructose 1,6-bisphosphate + H2O the bifunctional, thermostable enzyme (EC 4.1.2.13/EC 3.1.3.11) catalyses two subsequent steps in gluconeogenesis. It catalyses a multi-step reaction by remodelling its active site according to the respective catalytic requirements Pyrobaculum neutrophilum DSM 2338 D-fructose 6-phosphate + phosphate
-
?

Synonyms

Synonyms Comment Organism
FBP aldolase/phosphatase EC 4.1.2.13/EC 3.1.3.11. A bifunctional, thermostable enzyme that catalyses two subsequent steps in gluconeogenesis in most archaea and in deeply branching bacterial lineages Pyrobaculum neutrophilum
fructose-1,6-bisphosphate (FBP) aldolase/phosphatase EC 4.1.2.13/EC 3.1.3.11. A bifunctional, thermostable enzyme that catalyses two subsequent steps in gluconeogenesis in most archaea and in deeply branching bacterial lineages Pyrobaculum neutrophilum
fructose-1,6-bisphosphate aldolase/phosphatase EC 4.1.2.13/EC 3.1.3.11. A bifunctional, thermostable enzyme that catalyses two subsequent steps in gluconeogenesis in most archaea and in deeply branching bacterial lineages Pyrobaculum neutrophilum
Tneu_0133 locus name Pyrobaculum neutrophilum
TnFBPAP
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Pyrobaculum neutrophilum