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Literature summary extracted from

  • Blankenfeldt, W.; Asuncion, M.; Lam, J.S.; Naismith, J.H.
    The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate thymidylyltransferase (RmlA) (2000), EMBO J., 19, 6652-6663.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.7.24 sitting-drop vapour-diffusion method in polyethylene glycol 6000, 0.1 M sodium citrate, pH 4.6 and 0.5 M Li2SO4 as precipitant, crystallization as apoenzyme or co-crystallization with dTTP or thymidine and alpha-D-glucose 1-phosphate or dTDP-D-glucose or dTDP-L-rhamnose Pseudomonas aeruginosa

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.7.24 dTDP-L-rhamnose
-
 Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.24 dTTP + alpha-D-glucose 1-phosphate Pseudomonas aeruginosa
-
 dTDP-glucose + diphosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.24 Pseudomonas aeruginosa
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.24 dTTP + alpha-D-glucose 1-phosphate
-
 Pseudomonas aeruginosa dTDP-glucose + diphosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.7.24 tetramer each monomer consisting of three functional subunits Pseudomonas aeruginosa