Bünz P V, Falchetto R, Cook A M
Institute of Microbiology, ETH-Zentrum, Zürich, Switzerland.
Biodegradation. 1993;4(3):171-8. doi: 10.1007/BF00695119.
Sphingomonas sp. strain RW1, when grown in salicylate-salts medium, synthesized the enzymes for the degradation of dibenzofuran. The reaction subsequent to meta cleavage of the first benzene ring was found to be catalyzed by two isofunctional hydrolases, H1 and H2, which were purified by chromatography on anion exchange, hydrophobic interaction and gel filtration media. Each enzyme was able to hydrolyze 2-hydroxy-6-oxo-6-(2-hydroxyphenyl)hexa-2,4-dienoate and 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate to produce salicylate and benzoate, respectively. SDS/PAGE of each purified enzyme showed a single band of M(r) 31,000 (H1) or 29,000 (H2). The N-terminal amino acid sequences of the two proteins showed 50% homology.
鞘氨醇单胞菌属菌株RW1在水杨酸盐培养基中生长时，会合成降解二苯并呋喃的酶。发现第一个苯环间位裂解后的反应由两种同功水解酶H1和H2催化，它们通过阴离子交换、疏水相互作用和凝胶过滤介质上的色谱法进行纯化。每种酶都能够分别水解2-羟基-6-氧代-6-(2-羟基苯基)己-2,4-二烯酸酯和2-羟基-6-氧代-6-苯基己-2,4-二烯酸酯，生成水杨酸酯和苯甲酸酯。每种纯化酶的SDS/PAGE显示出一条分子量为31,000（H1）或29,000（H2）的条带。这两种蛋白质的N端氨基酸序列显示出50%的同源性。
