A Genome-Centric Approach Reveals a Novel Glycosyltransferase from the GA A07 Strain of Responsible for Catalyzing 15--Glycosylation of Ganoderic Acid A.

Strain GA A07 was identified as an intestinal bacterium of zebrafish, which has high efficiency to biotransform the triterpenoid, ganoderic acid A (GAA), into GAA-15--β-glucoside. To date, only two known enzymes (BsUGT398 and BsUGT489) of ATCC 6633 strain can biotransform GAA. It is thus worthwhile to identify the responsible genes of strain GA A07 by whole genome sequencing.

catena-Poly[[diaqua-[(4-tolyl-sulfan-yl)acetato-κO]cadmium(II)]-μ-4,4'-bipyridine-κN:N'].

The title complex, [Cd(C(9)H(9)O(2)S)(2)(C(10)H(8)N(2))(H(2)O)(2)](n), has a linear chain structure. The central Cd(II) ion is in a slightly disorted octa-hedral environment, coordinated by two aqua ligands, two (4-tolyl-sulfan-yl)acetate ligands and two bridging 4,4'-bipyridine ligands. The Cd(II) ion lies on a twofold rotation axis.