DETECTION AND LOCALIZATION OF A NEW ENZYME CATALYZING THE BETA-ARYL ETHER CLEAVAGE IN THE SOIL BACTERIUM (PSEUDOMONAS-PAUCIMOBILIS SYK-6)
DETECTION AND LOCALIZATION OF A NEW ENZYME CATALYZING THE BETA-ARYL ETHER CLEAVAGE IN THE SOIL BACTERIUM (PSEUDOMONAS-PAUCIMOBILIS SYK-6)
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DOI：
10.1016/0014-5793(89)80656-8
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发表时间：
1989-06-05
期刊：
影响因子：
3.5
通讯作者：
HARAGUCHI, T
中科院分区：
文献类型：
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作者：
MASAI, E;KATAYAMA, Y;HARAGUCHI, T
芳基甘油-β-芳基醚键的断裂是木质素生物降解过程中最重要的过程。我们测定了少见假单胞菌SYK-6细胞膜中β-芳基醚键的裂解酶的活性。该酶与细胞膜紧密结合，催化化合物II的独特的还原裂解，但不催化化合物I的裂解。该酶活性被NADH刺激。在此基础上，我们提出了β-芳基醚BYP的特定细胞同化模型。幽门螺杆菌SYK-6。
Cleavage of the arylglycerol‐β‐aryl ether linkage is the most important process in the biological degradation of lignin. We determined the activity of the enzyme cleaving the β‐aryl ether linkage in membranes ofPseudomonas paucimobilisSYK‐6. This enzyme was tightly associated with the cellular membrane and catalyzed the unique and reductive cleavage of compound II but not cleavage of compound I. This enzymatic activity was stimulated by addition of NADH. On the basis of this evidence, we present a model of the specific cellular assimilation of β‐aryl ether byP. paucimobilisSYK‐6.