Protoporphyrinogen Oxidase Inhibitor: An Ideal Target for Herbicide Discovery

Bibliographic Details
Title: Protoporphyrinogen Oxidase Inhibitor: An Ideal Target for Herbicide Discovery
Authors: Ge-Fei Hao, Yang Zuo, Sheng-Gang Yang, Guang-Fu Yang
Source: CHIMIA, Vol 65, Iss 12 (2011)
Publisher Information: Swiss Chemical Society, 2011.
Publication Year: 2011
Collection: LCC:Chemistry
Subject Terms: Herbicide, Inhibitor, Molecular design, Protoporphyrinogen oxidase, Qsar, Chemistry, QD1-999
More Details: As the last common enzyme in the biosynthetic pathway leading to heme and chlorophyll, protoporphyrinogen oxidase (PPO; EC 1.3.3.4) is an ideal target for herbicide development. Currently, about 30 PPO inhibitors have been developed as agricultural herbicides. PPO inhibitors have displayed environmentally benign, but advantageous characteristics, including low toxicity, low effective concentration, broad herbicidal spectrum (active against both monocotyledon and dicotyledon weeds), quick onset of action, and long lasting effect. Over the last several years, great achievements have been made in revealing the structural biology of PPO. Five PPO crystal structures, four isolated in enzyme-inhibitor complexes and one in the native form, have been determined, including those from Nicotiana tabacum, Myxococcus Xanthus, Bacillus subtilis, and human. Although PPO inhibitors have been developed for over forty years, we continue to uncover exciting future prospects for novel PPO-inhibiting herbicides. In this review, we have summarized the structures of PPOs from plants, human, and bacteria; the interactions between PPOs and inhibitors; the quantitative structure–activity relationships of PPO inhibitors; and the molecular design of new PPO inhibitors.
Document Type: article
File Description: electronic resource
Language: German
English
French
ISSN: 0009-4293
2673-2424
Relation: https://www.chimia.ch/chimia/article/view/5139; https://doaj.org/toc/0009-4293; https://doaj.org/toc/2673-2424
DOI: 10.2533/chimia.2011.961
Access URL: https://doaj.org/article/aa72f0c259e448c1a5e0b8121ff86b4e
Accession Number: edsdoj.72f0c259e448c1a5e0b8121ff86b4e
Database: Directory of Open Access Journals
More Details
ISSN:00094293
26732424
DOI:10.2533/chimia.2011.961
Published in:CHIMIA
Language:German
English
French