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

BRENDA support

Literature summary for 1.14.13.4 extracted from

  • Strickland, S.; Massey, V.
    The purification and properties of the flavoprotein melilotate hydroxylase (1973), J. Biol. Chem., 248, 2944-2952.
    View publication on PubMed
Search for more literature for 1.14.13.4

Inhibitors

Inhibitors Comment Organism Structure
FeCl3
-
 Pseudomonas sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
65000
-
 4 * 65000, SDS-PAGE Pseudomonas sp.
238000 250000 gel filtration, ultracentrifugation Pseudomonas sp.

Organism

Organism UniProt Comment Textmining
Pseudomonas sp.
-
-
-

Oxidation Stability

Oxidation Stability Organism
enzyme is rapidly reduced by irradiation with visible light in presence of EDTA or by dithionite Pseudomonas sp.

Purification (Commentary)

Purification (Comment) Organism
-
 Pseudomonas sp.

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
35.3
-
-
 Pseudomonas sp.

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
tetramer 4 * 65000, SDS-PAGE Pseudomonas sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Pseudomonas sp.

Cofactor

Cofactor Comment Organism Structure
FAD flavoprotein Pseudomonas sp.
FAD 1 mol FAD per protein of MW 65000 Pseudomonas sp.
FAD FAD: prosthetic group Pseudomonas sp.
NADH
-
 Pseudomonas sp.