Publication: Isopentenyl diphosphate isomerase in rubber latex
1
Issued Date
1996-01-01
Resource Type
ISSN
00319422
Other identifier(s)
2-s2.0-0030295319
Rights
Mahidol University
Rights Holder(s)
SCOPUS
Bibliographic Citation
Phytochemistry. Vol.43, No.4 (1996), 769-772
Suggested Citation
Tanetoshi Koyama, Dhirayos Wititsuwannakul, Kasem Asawatreratanakul, Rapepun Wititsuwannakul, Norimasa Ohya, Yasuyuki Tanaka, Kyozo Ogura Isopentenyl diphosphate isomerase in rubber latex. Phytochemistry. Vol.43, No.4 (1996), 769-772. doi:10.1016/0031-9422(96)00374-3 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/17525
Research Projects
Organizational Units
Authors
Journal Issue
Thesis
Title
Isopentenyl diphosphate isomerase in rubber latex
Abstract
Isopentenyl diphosphate isomerase (EC 5.3.3.2), which catalyses the reversible isomerization of isopentenyl diphosphate to dimethylallyl diphosphate, is presumed to be involved in rubber biosynthesis, but no direct evidence has been given for its occurrence in rubber latex. This enzyme activity was found in the C-serum powder prepared by lyophilization of centrifuged rubber latex of Hevea brasiliensis. Characterization of partially purified enzyme showed a K(m) value of 71 μM for isopentenyl diphosphate, a pH optimum of 7 and an optimum temperature at 37°. Divalent cations (Mg2+or Mn2+) and dithiothreitol are required for maximum enzymic activity. Sulphhydryl reagents such as iodoacelamide, p-chloromercuribenzoale and N- ethylmaleimide are effective inhibitors.