Institut für Mikrobiologie, Lehrstuhl für Angewandte und Ökologische Mikrobiologie, Friedrich-Schiller-Universität Jena, Jena, Germany.
FEMS Microbiol Lett. 2011 May;318(2):131-6. doi: 10.1111/j.1574-6968.2011.02251.x. Epub 2011 Mar 11.
The anaerobic phenyl methyl ether cleavage in acetogenic bacteria is mediated by multicomponent enzyme systems designated O-demethylases. Depending on the growth substrate, different O-demethylases are induced in Acetobacterium dehalogenans. A vanillate- and a veratrol-O-demethylase of this organism have been described earlier. The methyltransferase I (MT I), a component of this enzyme system, catalyzes the ether cleavage and the transfer of the methyl group to a super-reduced corrinoid bound to a protein. The MT I of the vanillate- and veratrol-O-demethylase (MT I(van) and MT I(ver)) were found to be zinc-containing enzymes. By site-directed mutagenesis, putative zinc ligands were identified, from which the following unique zinc-binding motifs were derived: E-X(14)-E-X(20)-H for MT I(van) and D-X(27)-C-X(39)-C for MT I(ver).
产乙酸细菌中的厌氧苯甲醚裂解是由多组分酶系统介导的，这些酶系统被指定为 O-脱甲基酶。根据生长底物的不同，产乙酸不动杆菌中诱导了不同的 O-脱甲基酶。该菌的香草酸盐和藜芦醇 O-脱甲基酶先前已有描述。该酶系统的甲基转移酶 I（MT I）是其组成部分，催化醚裂解和甲基基团转移到与蛋白质结合的超还原钴胺素上。香草酸盐和藜芦醇 O-脱甲基酶（MT I（van）和 MT I（ver））的 MT I 被发现是含锌酶。通过定点诱变，鉴定出假定的锌配体，从中推导出以下独特的锌结合基序：MT I（van）的 E-X（14）-E-X（20）-H 和 MT I（ver）的 D-X（27）-C-X（39）-C。
