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Literature summary for 2.7.4.16 extracted from

  • Webb, E.; Downs, D.
    Characterization of thiL, encoding thiamin-monophosphate kinase, in Salmonella typhimurium (1997), J. Biol. Chem., 272, 15702-15707.
    View publication on PubMed
Search for more literature for 2.7.4.16

Cloned(Commentary)

Cloned (Comment) Organism
encoded by thiL, thiL is not transcriptionally regulated by thiamine or thiamine diphosphate Salmonella enterica subsp. enterica serovar Typhimurium

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
35000
-
 recombinant enzyme, amino acid sequence Salmonella enterica subsp. enterica serovar Typhimurium

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + thiamine phosphate Salmonella enterica subsp. enterica serovar Typhimurium enzyme plays an important role in the thiamine diphosphate biosynthetic pathway, thiamine diphosphate is the regulatory molecule for thiamine synthesis and predicts the existence of a sensor/regulatory protein ADP + thiamine diphosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Salmonella enterica subsp. enterica serovar Typhimurium P55881 LT2
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + thiamine phosphate no substrates: thiamine, GTP, CTP, UTP, AMP Salmonella enterica subsp. enterica serovar Typhimurium ADP + thiamine diphosphate
-
 ?
ATP + thiamine phosphate enzyme plays an important role in the thiamine diphosphate biosynthetic pathway, thiamine diphosphate is the regulatory molecule for thiamine synthesis and predicts the existence of a sensor/regulatory protein Salmonella enterica subsp. enterica serovar Typhimurium ADP + thiamine diphosphate
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 35000, SDS-PAGE Salmonella enterica subsp. enterica serovar Typhimurium