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Detection and localization of a new enzyme catalyzing the β‐aryl ether cleavage in the soil bacterium ( Pseudomonas paucimobilis SYK‐6)
Author(s) -
Masai Eiji,
Katayama Yoshihiro,
Nishikawa Seiji,
Yamasaki Makari,
Morohoshi Noriyuki,
Haraguchi Takafusa
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80656-8
Subject(s) - sphingomonas paucimobilis , syk , chemistry , ether , aryl , enzyme , ether cleavage , cleavage (geology) , biochemistry , stereochemistry , bacteria , organic chemistry , biology , tyrosine kinase , paleontology , signal transduction , genetics , alkyl , fracture (geology)
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.