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Author
- Enghild, Jan J1
- Garcia-Ferrer, Irene1
- Gomis-Rüth, F Xavier1
- Guevara, Tibisay1
- Hara, Satoshi1
- Hisabori, Toru1
- Kalix, Leon1
- Lange, Theo1
- Lukassen, Marie V1
- Meinjohanns, Ernst1
- Nielsen, Tania A1
- Pimenta Lange, Maria João1
- Risør, Michael W1
- Rossen, Litten1
- Sanggaard, Kristian W1
- Scavenius, Carsten1
- Szperlinski, Manuela1
- Thomsen, Line R1
- Thøgersen, Ida B1
- Yoshida, Keisuke1
Keyword
- Arabidopsis2
- anabolism1
- catabolism1
- chloroplast1
- cucumber1
- cysteine proteases1
- development1
- digestion1
- dioxygenase1
- enzyme mechanism1
- enzyme structure1
- gibberellins1
- metabolism1
- oxidase1
- papain1
- phytohormone1
- plant biochemistry1
- plant carnivory1
- plant molecular biology1
- proteinase1
- recombinant protein expression1
- redox regulation1
- Venus flytrap1
Plant Biology
3 Results
- Plant BiologyOpen Access
Cucumber gibberellin 1-oxidase/desaturase initiates novel gibberellin catabolic pathways
Journal of Biological ChemistryVol. 295Issue 25p8442–8448Published online: April 27, 2020- Maria João Pimenta Lange
- Manuela Szperlinski
- Leon Kalix
- Theo Lange
Cited in Scopus: 2Bioactive gibberellins (GAs) are central regulators of plant growth and development, including seed development. GA homeostasis is achieved via complex biosynthetic and catabolic pathways, whose exact activities remain to be elucidated. Here, we isolated two cDNAs from mature or imbibed cucumber seeds with high sequence similarity to known GA 3-oxidases. We found that one enzyme (designated here CsGA3ox5) has GA 3-oxidation activity. However, the second enzyme (designated CsGA1ox/ds) performed multiple reactions, including 1β-oxidation and 9,11-desaturation of GAs, but was lacking the 3-oxidation activity. - Plant BiologyOpen Access
Enzymatic and Structural Characterization of the Major Endopeptidase in the Venus Flytrap Digestion Fluid
Journal of Biological ChemistryVol. 291Issue 5p2271–2287Published online: December 1, 2015- Michael W. Risør
- Line R. Thomsen
- Kristian W. Sanggaard
- Tania A. Nielsen
- Ida B. Thøgersen
- Marie V. Lukassen
- and others
Cited in Scopus: 14Carnivorous plants primarily use aspartic proteases during digestion of captured prey. In contrast, the major endopeptidases in the digestive fluid of the Venus flytrap (Dionaea muscipula) are cysteine proteases (dionain-1 to -4). Here, we present the crystal structure of mature dionain-1 in covalent complex with inhibitor E-64 at 1.5 Å resolution. The enzyme exhibits an overall protein fold reminiscent of other plant cysteine proteases. The inactive glycosylated pro-form undergoes autoprocessing and self-activation, optimally at the physiologically relevant pH value of 3.6, at which the protective effect of the pro-domain is lost. - Plant Biology BioenergeticsOpen Access
Thioredoxin Selectivity for Thiol-based Redox Regulation of Target Proteins in Chloroplasts
Journal of Biological ChemistryVol. 290Issue 23p14278–14288Published online: April 15, 2015- Keisuke Yoshida
- Satoshi Hara
- Toru Hisabori
Cited in Scopus: 68Redox regulation based on the thioredoxin (Trx) system is believed to ensure light-responsive control of various functions in chloroplasts. Five Trx subtypes have been reported to reside in chloroplasts, but their functional diversity in the redox regulation of Trx target proteins remains poorly clarified. To directly address this issue, we studied the Trx-dependent redox shifts of several chloroplast thiol-modulated enzymes in vitro and in vivo. In vitro assays using a series of Arabidopsis recombinant proteins provided new insights into Trx selectivity for the redox regulation as well as the underpinning for previous suggestions.