Metabolites of the Shikimate Pathway

1974 ◽  
pp. 80-127 ◽  
Author(s):  
Edwin Haslam
Keyword(s):  
1991 ◽  
Vol 266 (17) ◽  
pp. 10893-10898
Author(s):  
C. Kleanthous ◽  
M. Reilly ◽  
A. Cooper ◽  
S. Kelly ◽  
N.C. Price ◽  
...  

Biomolecules ◽  
2021 ◽  
Vol 11 (5) ◽  
pp. 705
Author(s):  
Awdhesh Kumar Mishra ◽  
Kwang-Hyun Baek

Salicylic acid (SA) is an active secondary metabolite that occurs in bacteria, fungi, and plants. SA and its derivatives (collectively called salicylates) are synthesized from chorismate (derived from shikimate pathway). SA is considered an important phytohormone that regulates various aspects of plant growth, environmental stress, and defense responses against pathogens. Besides plants, a large number of bacterial species, such as Pseudomonas, Bacillus, Azospirillum, Salmonella, Achromobacter, Vibrio, Yersinia, and Mycobacteria, have been reported to synthesize salicylates through the NRPS/PKS biosynthetic gene clusters. This bacterial salicylate production is often linked to the biosynthesis of small ferric-ion-chelating molecules, salicyl-derived siderophores (known as catecholate) under iron-limited conditions. Although bacteria possess entirely different biosynthetic pathways from plants, they share one common biosynthetic enzyme, isochorismate synthase, which converts chorismate to isochorismate, a common precursor for synthesizing SA. Additionally, SA in plants and bacteria can undergo several modifications to carry out their specific functions. In this review, we will systematically focus on the plant and bacterial salicylate biosynthesis and its metabolism.


2003 ◽  
Vol 67 (10) ◽  
pp. 2124-2131 ◽  
Author(s):  
Osao ADACHI ◽  
Somboon TANASUPAWAT ◽  
Nozomi YOSHIHARA ◽  
Hirohide TOYAMA ◽  
Kazunobu MATSUSHITA
Keyword(s):  

2003 ◽  
Vol 36 (3) ◽  
pp. 301-317 ◽  
Author(s):  
Lars Voll ◽  
Rainer E. Hausler ◽  
Rolf Hecker ◽  
Andreas Weber ◽  
Gottfried Weissenbock ◽  
...  

2018 ◽  
Vol 16 (06) ◽  
pp. 1850027
Author(s):  
Quanfeng Liu ◽  
Liping Li ◽  
Fei Xu

Shikimate pathway plays an essential role in the biosynthesis of aromatic amino acids in various plants and bacteria, which consists of seven key enzymes and they are all attractive targets for antibacterial agent development due to their absence in humans. The Staphylococcus aureus dehydroquinate synthase (SaDHQS) is involved in the second step of shikimate pathway, which catalyzes the NAD[Formula: see text]-dependent conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate to dehydroquinate via multiple steps. The enzyme active site can be characterized by two spatially separated subpockets 1 and 2, which represent the reaction center of substrate adduct with NAD[Formula: see text] nicotinamide moiety and the assistant binding site of NAD[Formula: see text] adenine moiety, respectively. In silico virtual screening is performed against a biogenic compound library to discover SaDHQS subpocket-specific inhibitors, which were then tested against both antibiotic-sensitive and antibiotic-resistant S. aureus strains by using in vitro susceptibility test. The activity profile of hit compounds has no considerable difference between the antibiotic-sensitive and -resistant strains. The subpocket 1-specific inhibitors exhibit a generally higher activity than subpocket 2-specific inhibitors, and they also hold a strong selectivity between their cognate and noncognate subpockets. Dynamics and energetics analyses reveal that the SaDHQS active site prefers to interact with amphipathic and polar inhibitors by forming multiple hydrogen bonds and van der Waals packing at the complex interfaces of the two subpockets with their cognate inhibitors.


1980 ◽  
Vol 10 (4) ◽  
pp. 845-862 ◽  
Author(s):  
Otto R. Gottlieb

Abstract While different biosynthetic groups of secondary metabolites (micromolecules) rarely accumulate in the same plant species, one such group may replace another in morphologically related taxa. The use of micromolecules as general systematic markers of the plant kingdom thus requires unifying postulates concerning their evolution patterns. Two such postulates — contraction of the shikimate pathway and blocking of oxidative enzymes — are illustrated with the aid of systematic considerations on the genera Aniba (Lauraceae) and Derris-Lonchocarpus (Leguminosae) which involve besides chemistry, morphology, ecology and geography. Extrapolation of the principles applied in these examples to the entire plant kingdom seems possible, an important fact, due to the ecological implications of micromolecules. In this sense, the paper opens the way, rather than simply to a more "natural" classification, to an information retrieval device of ecologically relevant facts about plants.


2020 ◽  
Author(s):  
Divjot Kaur ◽  
Christophe Corre ◽  
Fabrizio Alberti

Isoprenoid quinones are bioactive molecules that include an isoprenoid chain and a quinone head. They are traditionally found to be involved in primary metabolism, where they act as electron transporters, but specialized isoprenoid quinones are also produced by all domains of life. Here, we report the engineering of a baker's yeast strain, Saccharomyces cerevisiae EPYFA3, for the production of isoprenoid quinones. Our yeast strain was developed through overexpression of the shikimate pathway in a well-established recipient strain (S. cerevisiae EPY300) where the mevalonate pathway is overexpressed. As a proof of concept, our new host strain was used to overproduce the endogenous isoprenoid quinone coenzyme Q6, resulting in a final four-fold production increase. EPYFA3 represents a valuable platform for the heterologous production of high value isoprenoid quinones. EPYFA3 will also facilitate the elucidation of isoprenoid quinone biosynthetic pathways.


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