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红球菌属红平红球菌135菌株和红球菌属红串红球菌89菌株中儿茶酚1,2-双加氧酶的分离与特性分析:与普通和修饰邻位裂解途径的类似酶的比较

Isolation and characterization of catechol 1,2-dioxygenases from Rhodococcus rhodnii strain 135 and Rhodococcus rhodochrous strain 89: comparison with analogous enzymes of the ordinary and modified ortho-cleavage pathways.

作者信息

Solyanikova I P, Golovlev E L, Lisnyak O V, Golovleva L A

机构信息

Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Pushchino, Moscow Region, 142292, Russia.

出版信息

Biochemistry (Mosc). 1999 Jul;64(7):824-31.

Abstract

Catechol 1,2-dioxygenases of the ordinary ortho-cleavage pathway have been isolated from strains Rhodococcus rhodnii 135 and Rhodococcus rhodochrous 89 grown on phenol as the sole source of carbon and energy. The activities of the catechol 1,2-dioxygenases with 3- and 4-methylpyrocatechols were 1.3-1.5 times higher than those with pyrocatechol. The rate of oxidation of 3-chloropyrocatechol catalyzed by both enzymes was 20% of the rate of oxidation of unsubstituted pyrocatechol. The enzymes are homodimers composed of 37-kD subunits.

摘要

普通邻位裂解途径的儿茶酚1,2 -双加氧酶已从以苯酚作为唯一碳源和能源生长的红球菌属红球菌135菌株和红球菌属红平红球菌89菌株中分离出来。儿茶酚1,2 -双加氧酶对3 -和4 -甲基邻苯二酚的活性比对邻苯二酚的活性高1.3 - 1.5倍。两种酶催化3 -氯邻苯二酚的氧化速率是未取代邻苯二酚氧化速率的20%。这些酶是由37-kD亚基组成的同型二聚体。

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