各种微生物的儿茶酚 1,2-双加氧酶对 3-甲基儿茶酚的外二醇裂解作用。
Extradiol cleavage of 3-methylcatechol by catechol 1,2-dioxygenase from various microorganisms.
机构信息
Corporate Research Laboratories, EXXON Research and Engineering Company, Linden, New Jersey 07036.
出版信息
Appl Environ Microbiol. 1977 Mar;33(3):725-7. doi: 10.1128/aem.33.3.725-727.1977.
Abstract
The isofunctional enzymes of catechol 1,2-dioxygenase from species of Acinetobacter, Pseudomonas, Nocardia, Alcaligenes, and Corynebacterium oxidize 3-methylcatechol according to both the intradiol and extradiol cleavage patterns. However, the enzyme preparations from Brevibacterium and Arthrobacter have only the intradiol cleavage activity. Comparison of substrate specificity among these isofunctional dioxygenases shows striking differences in the oxidation of 3-methylcatechol, 4-methylcatechol and pyrogallol.
摘要
来自不动杆菌属、假单胞菌属、诺卡氏菌属、产碱杆菌属和棒状杆菌属的儿茶酚 1,2-双加氧酶的同功酶可根据邻位二醇和对位二醇裂解模式氧化 3-甲基儿茶酚。然而，来自短杆菌属和节杆菌属的酶制剂仅具有邻位二醇裂解活性。这些同功的双加氧酶的底物特异性比较表明，它们在氧化 3-甲基儿茶酚、4-甲基儿茶酚和焦儿茶酚方面存在显著差异。
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