Structure and increased thermostability of Rhodococcus sp. naphthalene 1,2-dioxygenase.

ABSTRACT: Rieske nonheme iron oxygenases form a large class of aromatic ring-hydroxylating dioxygenases found in microorganisms. These enzymes enable microorganisms to tolerate and even exclusively utilize aromatic compounds for growth, making them good candidates for use in synthesis of chiral intermediates and bioremediation. Studies of the chemical stability and thermostability of these enzymes thus become important. We report here the structure of free and substrate (indole)-bound forms of naphthalene dioxygenase from Rhodococcus sp. strain NCIMB12038. The structure of the Rhodococcus enzyme reveals that, despite a approximately 30% sequence identity between these naphthalene dioxygenases, their overall structures superpose very well with a root mean square deviation of less than 1.6 A. The diff

SUBMITTER: Gakhar L 

PROVIDER: S-EPMC1272967 | biostudies-literature | 2005 Nov

REPOSITORIES: biostudies-literature