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Literature summary extracted from

  • Schopfer, L.M.; Massey, V.
    Kinetic and mechanistic studies on the reduction of melilotate hydroxylase by reduced pyridine nucleotides (1979), J. Biol. Chem., 254, 10634-10643.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.13.4 0.0027
-
 3-(2-hydroxyphenyl)propanoate
-
 Pseudomonas sp.
1.14.13.4 0.02
-
 O2 stopped flow Pseudomonas sp.

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.4 Pseudomonas sp.
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.14.13.4 3-(2-hydroxyphenyl)propanoate + NADH + H+ + O2 = 3-(2,3-dihydroxyphenyl)propanoate + NAD+ + H2O mechanism Pseudomonas sp.
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.4 3-(2-hydroxyphenyl)propanoate + NADH + O2
-
 Pseudomonas sp. 3-(2,3-dihydroxyphenyl)propanoate + NAD+ + H2O
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.14.13.4 3.87 4.48 3-(2-hydroxyphenyl)propanoate
-
 Pseudomonas sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.4 NADH
-
 Pseudomonas sp.