l-tryptophan 2, 3-dioxygenaseof a moderate thermophile, Baccilus brevis: Purification, properties and a substrate-mediated stabilization of the quaternary structure
M Matsumura, K Osada, S Aiba - … et Biophysica Acta (BBA)-Protein Structure …, 1984 - Elsevier
Abstract l-Tryptophan 2, 3-dioxygenase (l-tryptophan: oxygen 2, 3-oxidoreductase
(decycling), EC 1.13. 11.11) from Bacillus brevis, a moderately thermophilic bacteria, was
purified to apparent homogeneity. The enzyme had a molecular weight of 110 000 and
consisted of four subunits of equal molecular size. The enzyme exhibited the typical
absorption spectra of a protohemoprotein. The amino acid composition and catalytic
properties of the thermophilic enzyme were almost similar to those of its mesophilic …
(decycling), EC 1.13. 11.11) from Bacillus brevis, a moderately thermophilic bacteria, was
purified to apparent homogeneity. The enzyme had a molecular weight of 110 000 and
consisted of four subunits of equal molecular size. The enzyme exhibited the typical
absorption spectra of a protohemoprotein. The amino acid composition and catalytic
properties of the thermophilic enzyme were almost similar to those of its mesophilic …