Cloned (Comment) | Organism |
---|---|
C-terminally His6-tagged enzyme is heterologously produced in Escherichia coli | Pyrobaculum neutrophilum |
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 | 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 | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
Glycerone phosphate + D-glyceraldehyde 3-phosphate | 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 1,6-bisphosphate | - |
? | |
Glycerone phosphate + D-glyceraldehyde 3-phosphate | 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 1,6-bisphosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pyrobaculum neutrophilum | B1YAL1 | i.e. Thermoproteus neutrophilus | - |
Pyrobaculum neutrophilum DSM 2338 | B1YAL1 | i.e. Thermoproteus neutrophilus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
Glycerone phosphate + D-glyceraldehyde 3-phosphate | 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 1,6-bisphosphate | - |
? | |
Glycerone phosphate + D-glyceraldehyde 3-phosphate | 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 1,6-bisphosphate | - |
? | |
Glycerone phosphate + D-glyceraldehyde 3-phosphate | 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 1,6-bisphosphate | - |
? | |
Glycerone phosphate + D-glyceraldehyde 3-phosphate | 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 1,6-bisphosphate | - |
? |
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 | - |
Pyrobaculum neutrophilum |