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Literature summary extracted from

  • Iturrate, L.; Sanchez-Moreno, I.; Oroz-Guinea, I.; Perez-Gil, J.; Garcia-Junceda, E.
    Preparation and characterization of a bifunctional aldolase/kinase enzyme: a more efficient biocatalyst for C-C bond formation (2010), Chemistry, 16, 4018-4030.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.29 expressed in Escherichia coli BL21(DE3) cells Citrobacter freundii
4.1.2.13 expressed in Escherichia coli BL21(DE3) cells Staphylococcus carnosus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.1.29 0.00122
-
 dihydroxyacetone pH and temperature not specified in the publication Citrobacter freundii
4.1.2.13 0.0146
-
 D-fructose 1,6-bisphosphate native enzyme, in Tris-HCl buffer (40 mM, pH 8.0), at 25°C Staphylococcus carnosus
4.1.2.13 0.0188
-
 D-fructose 1,6-bisphosphate recombinant fusion protein DLF, in Tris-HCl buffer (40 mM, pH 8.0), at 25°C Staphylococcus carnosus

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.29 Citrobacter freundii
-
-
-
2.7.1.29 Citrobacter freundii CECT 4626
-
-
-
4.1.2.13 Staphylococcus carnosus
-
-
-
4.1.2.13 Staphylococcus carnosus CECT 4491
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.1.29 Ni+2/IDA agarose column chromatography and Superdex 75 gel filtration Citrobacter freundii
4.1.2.13 nickel/iminodiacetic acid agarose column chromatography and Superdex 75 gel filtration Staphylococcus carnosus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.29 ATP + dihydroxyacetone
-
 Citrobacter freundii ADP + dihydroxyacetone phosphate
-
 ?
2.7.1.29 ATP + dihydroxyacetone
-
 Citrobacter freundii CECT 4626 ADP + dihydroxyacetone phosphate
-
 ?
4.1.2.13 D-fructose 1,6-bisphosphate
-
 Staphylococcus carnosus glycerone phosphate + D-glyceraldehyde 3-phosphate
-
 ?
4.1.2.13 D-fructose 1,6-bisphosphate
-
 Staphylococcus carnosus CECT 4491 glycerone phosphate + D-glyceraldehyde 3-phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.1.29 dimer
-
 Citrobacter freundii

Synonyms

EC Number Synonyms Comment Organism
2.7.1.29 DhaK
-
 Citrobacter freundii
2.7.1.29 dihydroxyacetone kinase
-
 Citrobacter freundii
4.1.2.13 DLF bifunctional enzyme, consists of monomeric fructose-1,6-bisphosphate aldolase from Staphylococcus carnosus and the homodimeric dihydroxyacetone kinase from Citrobacter freundii CECT 4626 with an intervening linker of five amino acid residues Staphylococcus carnosus
4.1.2.13 FBPA
-
 Staphylococcus carnosus
4.1.2.13 fructose-1,6-bisphosphate aldolase
-
 Staphylococcus carnosus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.7.1.29 48.7
-
 the melting temperature is 48.7°C Citrobacter freundii
4.1.2.13 90
-
 FBPA shows an almost complete recuperation (92%) of the secondary structure after denaturation at 90°C Staphylococcus carnosus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.1.29 24.13
-
 dihydroxyacetone pH and temperature not specified in the publication Citrobacter freundii
4.1.2.13 16.76
-
 D-fructose 1,6-bisphosphate native enzyme, in Tris-HCl buffer (40 mM, pH 8.0), at 25°C Staphylococcus carnosus
4.1.2.13 20.3
-
 D-fructose 1,6-bisphosphate recombinant fusion protein DLF, in Tris-HCl buffer (40 mM, pH 8.0), at 25°C Staphylococcus carnosus

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.1.29 ATP dependent on Citrobacter freundii

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.7.1.29 19800
-
 dihydroxyacetone pH and temperature not specified in the publication Citrobacter freundii
4.1.2.13 1080
-
 D-fructose 1,6-bisphosphate recombinant fusion protein DLF, in Tris-HCl buffer (40 mM, pH 8.0), at 25°C Staphylococcus carnosus
4.1.2.13 1160
-
 D-fructose 1,6-bisphosphate native enzyme, in Tris-HCl buffer (40 mM, pH 8.0), at 25°C Staphylococcus carnosus