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Literature summary for 4.1.99.17 extracted from

  • Ernst, D.C.; Borchert, A.J.; Downs, D.M.
    Perturbation of the metabolic network in Salmonella enterica reveals cross-talk between coenzyme A and thiamine pathways (2018), PLoS ONE, 13, e0197703 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.1.99.17

Activating Compound

Activating Compound Comment Organism Structure
additional information CoA or acetyl-CoA has no demonstrable effect on the HMP-P synthase ThiC in vitro Salmonella enterica subsp. enterica

Protein Variants

Protein Variants Comment Organism
additional information construction of strains DM13651 (zxx-8029::Tn10d(Tc) thiC1128 panE::Cm) and DM13652 (zxx-8029::Tn10d(Tc) thiC1129 panE::Cm), phenotypic analysis. Growth of representative suppressor strain DM13897 (thiC1129 panE::Cm ilvY3213) compared to parental strain DM13652 (thiC1129 panE::Cm) in minimal glucose medium: the parental thiC panE strain fails to grow on minimal glucose medium, but a suppressor derivative (DM13897) grows well. Growth of the parental strain is restored by the addition of thiamine (100 nM) or pantothenate Salmonella enterica subsp. enterica
ThiCE218K site-directed mutagenesis, compromised ThiC variant weakly constrains the HMP pathway and the constraint is additive such that the combination of ThiCE218K or ThiCV267M with a lesion in panE prevents growth on minimal glucose medium Salmonella enterica subsp. enterica
ThiCV267M site-directed mutagenesis, compromised ThiC variant weakly constrains the HMP pathway and the constraint is additive such that the combination of ThiCE218K or ThiCV267M with a lesion in panE prevents growth on minimal glucose medium Salmonella enterica subsp. enterica

Inhibitors

Inhibitors Comment Organism Structure
additional information CoA or acetyl-CoA has no demonstrable effect on the HMP-P synthase ThiC in vitro Salmonella enterica subsp. enterica

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine Salmonella enterica subsp. enterica
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 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
 ?

Organism

Organism UniProt Comment Textmining
Salmonella enterica subsp. enterica Q9L9I7 serovar typhimurium LT2
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine
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 Salmonella enterica subsp. enterica 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO
-
 ?

Synonyms

Synonyms Comment Organism
HMP-P synthase
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 Salmonella enterica subsp. enterica
thiC
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 Salmonella enterica subsp. enterica

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine
-
 Salmonella enterica subsp. enterica

General Information

General Information Comment Organism
metabolism ThiC catalyzes formation of HMP-P from the branch-point metabolite aminoimidazole ribotide (AIR), which is subsequently phosphorylated prior to being condensed with THZ-P to form thiamine-phosphate. Perturbation of the metabolic network in Salmonella enterica reveals cross-talk between coenzyme A and thiamine pathways connecting CoA and ThiC activity in vivo, pathways overview Salmonella enterica subsp. enterica
physiological function thiamine pyrophosphate is an essential cofactor, and is made of two independently synthesized moieties, 4-methyl-5-(2-hydroxyethyl)-thiazole phosphate (THZ-P) and 4-amino-5-(hydroxymethyl)-2-methylpyrimidine phosphate (HMP-P), the latter is synthesized involving enzyme ThiC Salmonella enterica subsp. enterica