Purification and characterization of a tuliposide-converting enzyme from bulbs of Tulipa gesneriana.
An enzyme that catalyzes the stoichiometric conversion of 6-tuliposide into tulipalin was purified and characterized from bulbs of Tulipa gesneriana. The enzyme appeared to be a dimer, the relative molecular mass (Mr) of each subunit being 34,900; it had maximum activity and stability at neutral pH and moderate temperature. The enzyme preferentially acted on such glucose esters as 6-tuliposides, and to a lesser extent on p-nitrophenylacetate.
Kato
Yasuo
Y
Biotechnology Research Center, Faculty of Engineering, Toyama Prefectural University, Japan. ykato@pu-toyama.ac.jp
Shoji
Kazuaki
K
Ubukata
Makoto
M
Shigetomi
Kengo
K
Sato
Yukio
Y
Nakajima
Noriyuki
N
Ogita
Shinjiro
S
D000890:Anti-Infective Agents / Q000378:metabolism; D055162:Biocatalysis; D006027:Glycosides / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D018520:Plant Shoots / Q000201:enzymology* / Q000378:metabolism; D012978:Sodium Oxybate / Q000031:analogs & derivatives* / Q000378:metabolism; D013696:Temperature; D031447:Tulipa / Q000201:enzymology* / Q000378:metabolism
D000890:Anti-Infective Agents; D006027:Glycosides; C046169:6-tuliposide A; D012978:Sodium Oxybate