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In vitro reconstitution of the catabolic reactions catalyzed by PcaHG, PcaB, and PcaL: the protocatechuate branch of the beta-ketoadipate pathway in Rhodococcus jostii RHA1

Yamanashi, Tomoya and Kim, Seungyoung and Hara, Hirofumi and Funa, Nobutaka (2015) In vitro reconstitution of the catabolic reactions catalyzed by PcaHG, PcaB, and PcaL: the protocatechuate branch of the beta-ketoadipate pathway in Rhodococcus jostii RHA1. Bioscience, Biotechnology and Biochemistry, 79 (5). pp. 830-835. ISSN 0916-8451

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Official URL: http://dx.doi.org/10.1080/09168451.2014.993915

Abstract

The ß-ketoadipate pathway is a major pathway involved in the catabolism of the aromatic compounds in microbes. The recent progress in genome sequencing has led to a rapid accumulation of genes from the ß-ketoadipate pathway in the available genetic database, yet the functions of these genes remain uncharacterized. In this study, the protocatechuate branch of the ß-ketoadipate pathway of Rhodococcus jostii was reconstituted in vitro. Analysis of the reaction products of PcaHG, PcaB, and PcaL was achieved by high-performance liquid chromatography. These reaction products, ß-ketoadipate enol-lactone, 3-carboxy-cis,cis-muconate, y-carboxymuconolactone, muconolactone, and ß-ketoadipate, were further characterized using LC-MS and nuclear magnetic resonance. In addition, the in vitro reaction of PcaL, a bidomain protein consisting of y-carboxy-muconolactone decarboxylase and ß-ketoadipate enol-lactone hydrolase activities, was demonstrated for the first time. This work provides a basis for analyzing the catalytic properties of enzymes involved in the growing number of ß-ketoadipate pathways deposited in the genetic database

Item Type:Article
Uncontrolled Keywords:peek, apatite
Subjects:T Technology > T Technology (General)
Divisions:Malaysia-Japan International Institute of Technology
ID Code:55814
Deposited By: Fazli Masari
Deposited On:06 Oct 2016 06:07
Last Modified:15 Feb 2017 01:08

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