Minges, Alexander ORCID: 0000-0001-7760-2753 and Groth, Georg (2017). Small-molecule inhibition of pyruvate phosphate dikinase targeting the nucleotide binding site. PLoS One, 12 (7). SAN FRANCISCO: PUBLIC LIBRARY SCIENCE. ISSN 1932-6203

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Abstract

Pyruvate phosphate dikinase (PPDK) is an essential enzyme of C4 photosynthesis in plants, catalyzing the ATP-driven conversion of pyruvate to phosphoenolpyruvate ( PEP). It is further used by some bacteria and unicellular protists in the reverse, ATP-forming direction. Many weed species use C4 photosynthesis in contrast to world's major crops, which are C3 plants. Hence inhibitors of PPDK may be used as C4-specific herbicides. By screening a library of 80 commercially available kinase inhibitors, we identified compounds derived from bisindolylmaleimide (bisindolylmaleimide IV, IC50 = 0.76 +/- 0.13 mu M) and indirubin (indirubin3'- monoxime, IC50 = 4.2 +/- 0.9 mu M) that showed high inhibitory potency towards PPDK and are among the most effective PPDK inhibitors described today. Physiological studies on leaf tissues of a C4 model plant confirmed in vivo inhibition of C4-driven photosynthesis by these substances. Moreover, comparative docking studies of non-inhibitory bisindolylmaleimide derivatives suggest that the selectivity towards PPDK may be increased by addition of functional groups to the core structure.

Item Type: Journal Article
Creators:
CreatorsEmailORCIDORCID Put Code
Minges, AlexanderUNSPECIFIEDorcid.org/0000-0001-7760-2753UNSPECIFIED
Groth, GeorgUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
URN: urn:nbn:de:hbz:38-225045
DOI: 10.1371/journal.pone.0181139
Journal or Publication Title: PLoS One
Volume: 12
Number: 7
Date: 2017
Publisher: PUBLIC LIBRARY SCIENCE
Place of Publication: SAN FRANCISCO
ISSN: 1932-6203
Language: English
Faculty: Unspecified
Divisions: Unspecified
Subjects: no entry
Uncontrolled Keywords:
KeywordsLanguage
PROTEIN-KINASE-C; SWIVELING-DOMAIN MECHANISM; BUNDLE SHEATH-CELLS; ORTHOPHOSPHATE DIKINASE; C-4 PHOTOSYNTHESIS; REVERSIBLE PHOSPHORYLATION; INACTIVATION; ACTIVATION; DESIGN; CANCERMultiple languages
Multidisciplinary SciencesMultiple languages
Refereed: Yes
URI: http://kups.ub.uni-koeln.de/id/eprint/22504

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