Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Ngai, K.L.; Ornston, L.N.; Kallen, R.G.
    Enzymes of the beta-ketoadipate pathway in Pseudomonas putida: kinetic and magnetic resonance studies of the cis,cis-muconate cycloisomerase catalyzed reaction (1983), Biochemistry, 22, 5223-5230.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.5.1.1 0.424
-
muconolactone
-
Pseudomonas putida

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.5.1.1 Mn2+ divalent metal ion required, enzyme contains a single binding site per subunit, Km: 0.003-0.0045 mM Pseudomonas putida

Organism

EC Number Organism UniProt Comment Textmining
5.5.1.1 Pseudomonas putida
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.5.1.1 cis,cis-Muconate i.e. cis,cis-2,4-hexadiendioate, , r Pseudomonas putida (+)-Muconolactone
-
?
5.5.1.1 cis,cis-muconate
-
Pseudomonas putida muconolactone
-
?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.5.1.1 1.4
-
muconolactone
-
Pseudomonas putida
5.5.1.1 13.9
-
cis,cis-muconate expressed per catalytic center Pseudomonas putida

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
5.5.1.1 5.2 8.3 25°C, stable Pseudomonas putida