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Literature summary for 4.1.1.7 extracted from

  • Nemeria, N.; Korotchkina, L.; McLeish, M.J.; Kenyon, G.L.; Patel, M.S.; Jordan, F.
    Elucidation of the chemistry of enzyme-bound thiamin diphosphate prior to substrate binding: defining internal equilibria among tautomeric and ionization states (2007), Biochemistry, 46, 10739-10744.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Pseudomonas putida
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzoylformate
-
Pseudomonas putida benzaldehyde + CO2
-
?

Synonyms

Synonyms Comment Organism
BFDC
-
Pseudomonas putida

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6 8.5
-
Pseudomonas putida

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate the 4'-aminopyrimidine ring of the thiamine diphosphate coenzyme participates in catalysis, likely as an intramolecular general acid-base catalyst via the unusual 1',4'-iminopyrimidine tautomer Pseudomonas putida