scholarly journals Biosynthetic Pathway of Insect Juvenile Hormone III in Cell Suspension Cultures of the Sedge Cyperus iria

2001 ◽  
Vol 127 (2) ◽  
pp. 584-593 ◽  
Author(s):  
Jacqueline C. Bede ◽  
Peter E.A. Teal ◽  
Walter G. Goodman ◽  
Stephen S. Tobe
Biologia ◽  
2009 ◽  
Vol 64 (2) ◽  
Author(s):  
Fuyuan Jing ◽  
Ling Zhang ◽  
Meiya Li ◽  
Yueli Tang ◽  
Yuliang Wang ◽  
...  

AbstractArtemisinin, a sesquiterpene lactone endoperoxide derived from Artemisia annua L., is the most effective antimalarial drug. In an effort to increase the artemisinin production, abscisic acid (ABA) with different concentrations (1, 10 and 100 µM) was tested by treating A. annua plants. As a result, the artemisinin content in ABA-treated plants was significantly increased. Especially, artemisinin content in plants treated by 10 µM ABA was 65% higher than that in the control plants, up to an average of 1.84% dry weight. Gene expression analysis showed that in both the ABA-treated plants and cell suspension cultures, HMGR, FPS, CYP71AV1 and CPR, the important genes in the artemisinin biosynthetic pathway, were significantly induced. While only a slight increase of ADS expression was observed in ABA-treated plants, no expression of ADS was detected in cell suspension cultures. This study suggests that there is probably a crosstalk between the ABA signaling pathway and artemisinin biosynthetic pathway and that CYP71AV1, which was induced most significantly, may play a key regulatory role in the artemisinin biosynthetic pathway.


1991 ◽  
Vol 46 (5-6) ◽  
pp. 371-376 ◽  
Author(s):  
Elisabeth Häusler ◽  
Maike Petersen ◽  
August W. Alfermann

Cell suspension cultures of Coleus blumei Benth. producing high amounts of rosmarinic acid were used to study the biosynthetic pathway of this caffeic acid ester. One of the involved enzymes, the hydroxyphenylpyruvate reductase (HPPR), is characterized in this paper. HPPR catalyzes the NAD (P)H dependent reduction of p-hydroxyphenylpyruvate to p-hydroxyphenyllactate. The enzyme developed maximal activity at an incubation temperature of 37 °C and at a pH of 6.5 to 7.0. The reaction proceeded linearly for an incubation time of 60 min and up to a protein concentration of 0.2 mg per assay. As electron donor HPPR accepted NADH and NADPH with Km-values of 190 µm and 95 µm respectively. The enzyme reduced differently substituted hydroxyphenylpyruvates but not β-phenylpyruvate. The apparent Km-values for the various substrates were at 10 µM for p-hydroxyphenylpyruvate, at 130 µm for 3,4-dihydroxyphenylpyruvate and at 250 µM for 3-methoxy-4-hydroxyphenylpyruvate. HPPR was competitively inhibited by rosmarinic acid and pyruvate with Ki-values of 210 µM and 200 µM respectively. Caffeic acid, p-coumaric acid and cinnamic acid did not affect the enzyme activity but p-coumaroyl-CoA inhibited HPPR


1984 ◽  
Vol 25 (5) ◽  
pp. 573-576 ◽  
Author(s):  
Shinichi Uesato ◽  
Shinichi Ueda ◽  
Koji Kobayashi ◽  
Masao Miyauchi ◽  
Hiroyuki Inouye

Sign in / Sign up

Export Citation Format

Share Document