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Literature summary extracted from

  • Miallau, L.; Hunter, W.N.; McSweeney, S.M.; Leonard, G.A.
    Structures of Staphylococcus aureus D-tagatose-6-phosphate kinase implicate domain motions in specificity and mechanism (2007), J. Biol. Chem., 282, 19948-19957.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.144 expression in Escherichia coli Staphylococcus aureus
2.7.1.144 native enzyme and L124M, L125M double mutant expressed in Escherichia coli BL21(DE3) Staphylococcus aureus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.1.144 high resolution structures of D-tagatose-6-phosphate kinase (LacC) in two crystal forms. The structures define LacC in apoform, in binary complexes with ADP or the cofactor analogue adenosine 5'-(beta,gamma-imino)triphosphate, and in a ternary complex with adenosine 5'-(beta,gamma-imino)triphosphate and D-tagatose-6-phosphate. LacC adopts a closed structure required for phosphoryl transfer only when both substrate and co-factor are bound Staphylococcus aureus
2.7.1.144 native and L124M, L125M double mutant crystallized by hanging drop vapor diffusion method in apoform, in binary complexes with ADP or the cofactor analogue AMP-PNP, and in a ternary complex with AMP-PNP and D-tagatose-6-phosphate, wild-type protein give crystals that diffracte only to low resolution, the SeMet double mutant protein produced much more ordered crystals Staphylococcus aureus

Protein Variants

EC Number Protein Variants Comment Organism
2.7.1.144 L124M/L125M wild-type protein give crystals that diffracte only to low resolution, the SeMet double mutant protein produced much more ordered crystals Staphylococcus aureus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.144 Mg2+ required, two ions bound to the active site when substrate and cofactor are bound Staphylococcus aureus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.1.144 ATP + D-tagatose 6-phosphate Staphylococcus aureus second step of the D-tagatose-6-phosphate pathway which is the direct catabolic pathway for lactose ADP + D-tagatose 1,6-bisphosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.144 Staphylococcus aureus P0A0B9
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.1.144 native and mutant protein from Escherichia coli Staphylococcus aureus

Reaction

EC Number Reaction Comment Organism Reaction ID
2.7.1.144 ATP + D-tagatose 6-phosphate = ADP + D-tagatose 1,6-bisphosphate mechanism suggested Staphylococcus aureus
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.144 ATP + D-tagatose 6-phosphate second step of the D-tagatose-6-phosphate pathway which is the direct catabolic pathway for lactose Staphylococcus aureus ADP + D-tagatose 1,6-bisphosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.1.144 dimer gel filtration data, crystal structure analysis, two monomers associate via interactions between their lid domains, which come together to form a beta-barrel structure known as a beta-clasp Staphylococcus aureus

Synonyms

EC Number Synonyms Comment Organism
2.7.1.144 D-tagatose-6-phosphate kinase
-
 Staphylococcus aureus
2.7.1.144 Lacc
-
 Staphylococcus aureus
2.7.1.144 Lacc belongs to the pfkB family of carbohydrate kinases, which form a subset of the ribokinase superfamily Staphylococcus aureus
2.7.1.144 phosphotagatokinase
-
 Staphylococcus aureus

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.1.144 ATP
-
 Staphylococcus aureus