| Title |
Protocatechuate 3,4-dioxygenase from thermophilic Geobacillus sp. strain / |
| Translation of Title |
Geobacillus sp. Protokatechuato 3,4-dioksigenazė. |
| Authors |
Bubinas, Audrius ; Giedraitytė, Gražina ; Kalėdienė, Lilija |
| Full Text |
|
| Is Part of |
Biologija. 2007, Nr. 1. ISSN 1392-0146 |
| Keywords [eng] |
Thermophilic bacteria ; Naphthalene ; Protocatechuate 3,4-dioxygenase ; Purification |
| Abstract [eng] |
Protocatechuate 3,4-dioxygenase ( EC 1.13.11.3 ) catalyses the ring cleavage step in catabolism of aromatic compounds through the protocatechuate branch of the b-ketoadipate pathway. The protocatechuate 3,4-dioxygenase was purified to homogeneity from the thermophilic Geobacillus strain grown on naphthalene for the first time. The enzyme was purified about 24-fold with a specific activity of 34.2 U mg of protein-1 by a purification procedure including ammonium sulfate fractionation and column chromatographies on DEAE– cellulose and hydroxylapatite. The relative molecular mass of the native enzyme estimated on gel chromatography of Sephadex G-200 was 480 kDa. The pH and temperature optima for enzyme activity were 8 and 60 oC, respectively. A half-live of the protocatechuate 3,4-dioxygenase at the optimum temperature was 40 min. The kinetic parameters of the Geobacillus strain protocatehuate 3,4-dioxygenase were determinated. The enzyme gave typical saturation kinetics and had an apparent Km of 7 mM for protocatechuate and 33 mM for catechol. |
| Type |
Journal article |
| Language |
English |
| Publication date |
2007 |
