Detection and localization of a new enzyme catalyzing the β‐aryl ether cleavage in the soil bacterium (Pseudomonas paucimobilis SYK‐6)

FEBS Letters

Yamasaki, Makari¹  Katayama, Yoshihiro²  Morohoshi, Noriyuki²  Masai, Eiji²  Nishikawa, Seiji²  Haraguchi, Takafusa² 

[1] University of Tokyo, Bunkyo-ku, Tokyo Japan;Lab. Wood Chemistry, Faculty of Agriculture, Tokyo Noko University, Fuchu, Tokyo, Japan

关键词: Lignin metabolism;    Arylglycerol-β-aryl ether linkage;    Aryl ether cleaving enzyme;    β-;    Cell-free lysate;    Membrane enzyme;    (Pseudomonas paucimobilis SYK-6);    DDVA;    2;    2′-dihydroxy-3;    3′-dimethoxy-5;    5′-dicarboxybiphenyl;    MEGA-8;    octanoyl-N-methylglucamide;    MEGA-9;    nonanoyl-N-glucamide;    CHAPS;    3-[(3-cholamidopropyl)dimethylammonio] - 1 - propanesulfonate;    HAPSO;    3-[(3-cholamidopropyl)dimethylammonio]-2-hydroxypropanesulfonate;    NADH;    reduced nicotinamide adenine dinucleotide;    NAD;    nicotinamide adenine dinucleotide;    DTT;    dithiothreitol;   

DOI  :  10.1016/0014-5793(89)80656-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 of Pseudomonas paucimobilis SYK-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 by P. paucimobilis SYK-6.

【 授权许可】

Unknown