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Literature summary for 1.13.11.8 extracted from

  • Arciero, D.M.; Lipscomb, J.D.; Huynh, B.H.; Kent, T.A.; Munck, E.
    EPR and Mossbauer studies of protocatechuate 4,5-dioxygenase. Characterization of a new Fe2+ environment (1983), J. Biol. Chem., 258, 14981-14991.
    View publication on PubMed
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Crystallization (Commentary)

Crystallization (Comment) Organism
under strictly anaerobic conditions Comamonas testosteroni

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ characterization of Fe2+ environment with EPR and Mössbauer studies Comamonas testosteroni
Fe2+ iron is present in active enzyme in the high-spin ferrous state Comamonas testosteroni

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
17700
-
 alpha2, beta2. 2 * 17700 + 2 * 33800, dimer of a heterodimer, SDS-PAGE Comamonas testosteroni
33800
-
 alpha2, beta2. 2 * 17700 + 2 * 33800, dimer of a heterodimer, SDS-PAGE Comamonas testosteroni
142000
-
 gel filtration Comamonas testosteroni

Organism

Organism UniProt Comment Textmining
Comamonas testosteroni
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Comamonas testosteroni

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
212
-
-
 Comamonas testosteroni

Subunits

Subunits Comment Organism
tetramer alpha2, beta2. 2 * 17700 + 2 * 33800, dimer of a heterodimer, SDS-PAGE Comamonas testosteroni