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Literature summary extracted from

  • Hasson, M.S.; Muscate, A.; McLeish, M.J.; Polovnikova, L.S.; Gerlt, J.A.; Kenyon, G.L.; Petsko, G.A.; Ringe, D.
    The crystal structure of benzoylformate decarboxylase at 1.6 A resolution: diversity of catalytic residues in thiamin diphosphate-dependent enzymes (1998), Biochemistry, 37, 9918-9930.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.1.7
-
 Pseudomonas putida

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.1.7 Ca2+ bound to the cofactor in each subunit Pseudomonas putida
4.1.1.7 Mg2+ bound on a 2fold axis of the tetramer Pseudomonas putida

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.1.7 Benzoylformate Pseudomonas putida third enzyme in the mandelate pathway ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.7 Pseudomonas putida P20906
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.7
-
 Pseudomonas putida

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.7 benzoylformate
-
 Pseudomonas putida benzaldehyde + CO2
-
 ?
4.1.1.7 Benzoylformate third enzyme in the mandelate pathway Pseudomonas putida ?
-
 ?