A common structure of substrate shared by lignostilbenedioxygenase isozymes from Sphingomonas paucimobilis TMY1009.
A common structure of substrates of lignostilbenedioxygenases was investigated using synthesized stilbenes. Cell-free extracts of Sphingomonas paucimobilis TMY1009 degraded only trans-4-hydroxystilbene and trans-4-hydroxy-3-methoxystilbene. Other stilbenes that had no 4-hydroxyl group and had a cis structure were not substrates for lignostilbenedioxygenases. These results indicate that a 4-hydroxyl group and trans-structure is necessary for the common structure for substrates of lignostilbenedioxygenases.
Kamoda
Shigehiro
S
The University Forest in Hokkaido, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Yayoi 1-1-1, Bunkyo-ku, Tokyo 113-8657, Japan. kamo@uf.a.u-tokyo.ac.jp
Terada
Tamami
T
Saburi
Yoshimasa
Y
D002457:Cell Extracts; D002851:Chromatography, High Pressure Liquid; D049308:Dioxygenases; D007527:Isoenzymes / Q000737:chemistry* / Q000378:metabolism; D008024:Ligands; D010105:Oxygenases / Q000737:chemistry* / Q000378:metabolism; D020578:Sphingomonas / Q000201:enzymology*; D013237:Stereoisomerism; D013267:Stilbenes / Q000737:chemistry / Q000378:metabolism; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D002457:Cell Extracts; D007527:Isoenzymes; D008024:Ligands; D013267:Stilbenes; C064297:4-hydroxystilbene; D010105:Oxygenases; D049308:Dioxygenases; C069684:lignostilbene-alpha,beta-dioxygenase