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Literature summary for 5.5.1.1 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]

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

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Pseudomonas putida
-
-
-

Substrates and Products (Substrate)

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

Turnover Number [1/s]

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

pH Stability

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