Project/Area Number |
05660105
|
Research Category |
Grant-in-Aid for General Scientific Research (C)
|
Allocation Type | Single-year Grants |
Research Field |
応用微生物学・応用生物化学
|
Research Institution | Osaka Prefecture University |
Principal Investigator |
WADANO Akira OSAKA PREFECTURE UNIVERSITY,APPLIED BIOLOGICAL CHEMISTRY,ASSOCIATE PROFESSOR, 農学部, 講師 (40081575)
|
Project Period (FY) |
1993 – 1994
|
Project Status |
Completed (Fiscal Year 1994)
|
Budget Amount *help |
¥1,800,000 (Direct Cost: ¥1,800,000)
Fiscal Year 1994: ¥900,000 (Direct Cost: ¥900,000)
Fiscal Year 1993: ¥900,000 (Direct Cost: ¥900,000)
|
Keywords | Hysteresis / RuBisCO / Fallover / Cloning / Photosynthesis / Carbon fixation |
Research Abstract |
When the illumination is enough under the atomospheric conditions, photosynthesis in higher plants is rate-limited in CO_2 fixation. This causes lowering of reaction efficiency of ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO) which is a enzyme of carbon fixation. This enzyme has only lower activity than other enzymes with 1/100 to 1/1000 activity and low affinity against substrate. On the present study, I focused to the hysteresis with this enzyme and identified lysine residue which was related to fallover phenomena. On the other hand bacterial RuBisCO showed the inverse hysteresis so that the enzyme was converted to arginine or proline instead of lysine. These phenomena were affected by dithiothreitol ; lower was the concentration, higher the activity. From these results It suggested that the change of stereo-structure, which resulted in lysine residue, held the structure by the formation of disulfide bond and that the hysteresis was appeared.
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