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Literature summary for 1.14.13.4 extracted from

  • Levy, C.C.
    Melilotate hydroxylase. Purification of the enzyme and the nature of the prosthetic group (1967), J. Biol. Chem., 242, 747-753.
    View publication on PubMed

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
65000
-
sucrose density gradient centrifugation, gel filtration Arthrobacter sp.

Organism

Organism UniProt Comment Textmining
Arthrobacter sp.
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Arthrobacter sp.

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
12.5
-
-
Arthrobacter sp.

Storage Stability

Storage Stability Organism
-20°C, stable for 3 weeks, highly purified enzyme, concentrated by dialysis Arthrobacter sp.
-70°C, stable for 1 week Arthrobacter sp.

Substrates and Products (Substrate)

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

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Arthrobacter sp.

Cofactor

Cofactor Comment Organism Structure
FAD flavoprotein Arthrobacter sp.
FAD FAD: prosthetic group Arthrobacter sp.
NADH
-
Arthrobacter sp.