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Literature summary for 2.5.1.2 extracted from

  • Hutter, J.A.; Slama, J.T.
    Inhibition of thiaminase I from Bacillus thiaminolyticus. Evidence supporting a covalent 1,6-dihydropyrimidinyl-enzyme intermediate (1987), Biochemistry, 26, 1969-1973.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
4-Amino-5-(anilinomethyl)-6-chloro-2-methylpyrimidine complete irreversible inhibition 2 times faster than 4-amino-6-chloro-2-methylpyrimidine Paenibacillus thiaminolyticus
4-Amino-6-chloro-2-methylpyrimidine complete irreversible inhibition, activity protected by thiamine and quinolone Paenibacillus thiaminolyticus
additional information 4-amino-2-methyl pyrimidine does not inactivate nor competitively inhibits the enzyme Paenibacillus thiaminolyticus

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Paenibacillus thiaminolyticus
-
-

Organism

Organism UniProt Comment Textmining
Paenibacillus thiaminolyticus
-
BMM strain
-
Paenibacillus thiaminolyticus BMM
-
BMM strain
-

Source Tissue

Source Tissue Comment Organism Textmining
cell culture
-
Paenibacillus thiaminolyticus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
thiamine + aniline
-
Paenibacillus thiaminolyticus 5-(anilinomethyl)-2-methylpyrimidin-4-amine + 4-methyl-5-(2-hydroxyethyl)-thiazole
-
?
thiamine + aniline
-
Paenibacillus thiaminolyticus BMM 5-(anilinomethyl)-2-methylpyrimidin-4-amine + 4-methyl-5-(2-hydroxyethyl)-thiazole
-
?
thiamine + quinoline
-
Paenibacillus thiaminolyticus 4-methyl-5-(2-hydroxyethyl)-thiazole + 1-[(4-amino-2-methylpyrimidin-5-yl)methyl]quinolinium
-
?
thiamine + quinoline
-
Paenibacillus thiaminolyticus BMM 4-methyl-5-(2-hydroxyethyl)-thiazole + 1-[(4-amino-2-methylpyrimidin-5-yl)methyl]quinolinium
-
?

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.096
-
4-Amino-5-(anilinomethyl)-6-chloro-2-methylpyrimidine
-
Paenibacillus thiaminolyticus