Structural basis for the substrate specificity and the absence of dehalogenation activity in 2-chloromuconate cycloisomerase from Rhodococcus opacus 1CP |
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Authors: | Marina Kolomytseva Marta Ferraroni Alexey Chernykh Ludmila Golovleva Andrea Scozzafava |
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Affiliation: | 1. Dipartimento di Chimica “Ugo Schiff”, Università di Firenze, Via della Lastruccia 3, I-50019 Sesto Fiorentino, FI, Italy;2. G.K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, 142290 Pushchino, Nauka Prospect 5, Moscow region, Russia |
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Abstract: | 2-Chloromuconate cycloisomerase from the Gram-positive bacterium Rhodococcus opacus 1CP (Rho-2-CMCI) is an enzyme of a modified ortho-pathway, in which 2-chlorophenol is degraded using 3-chlorocatechol as the central intermediate. In general, the chloromuconate cycloisomerases catalyze not only the cycloisomerization, but also the process of dehalogenation of the chloromuconate to dienelactone. However Rho-2-CMCI, unlike the homologous enzymes from the Gram-negative bacteria, is very specific for only one position of the chloride on the substrate chloromuconate. Furthermore, Rho-2-CMCI is not able to dehalogenate the 5-chloromuconolactone and therefore it cannot generate the dienelactone. |
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Keywords: | Modified ortho-pathway Aromatic catabolism X-ray crystallography Muconate Dehalogenation |
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