3-Deoxy-D-arabinoheptulosonate 7-phosphate (DAHP) synthase (EC 2.5.1.54) is the first enzyme in a series of metabolic reactions known as the shikimate pathway, which is responsible for the biosynthesis of the amino acids phenylalanine, tyrosine, and tryptophan. (wikipedia.org)
These isoenzymes require a divalent metal ion and most of them are feedback regulated by the respective end product.This thesis describes studies on crystal structures of the tyrosine regulated DAHP synthase from Saccharomyces cerevisiae and a variety of its complexes. (uni-goettingen.de)
A complex of DAHP synthase, manganese(II) and tyrosine reveals the effector binding pocket of this enzyme family. (uni-goettingen.de)
By comparing the active and the inhibited structures of the enzyme the inhibition mechanism of the tyrosine sensitive DAHP synthase could be understood. (uni-goettingen.de)
DHQS2
Dehydroquinate synthase (DHQS) is a nicotinamide adenine dinucleotide (NAD)-dependent enzyme that converts 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) into 3-dehydroquinate (DHQ). (nih.gov)
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway for. (systemsbiology.net)
Isoenzymes1
In Escherichia coli, a species of bacteria, DAHP synthase is found as three isoenzymes, each of which sensitive to one of the amino acids produced in the shikimate pathway. (wikipedia.org)
1.541
In enzymology, a DAHP synthase (EC 2.5.1.54) is an enzyme that catalyzes the chemical reaction phosphoenolpyruvate + D-erythrose 4-phosphate + H2O ⇌ {\displaystyle \rightleftharpoons } 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate The three substrates of this enzyme are phosphoenolpyruvate, D-erythrose 4-phosphate, and H2O, whereas its two products are 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate and phosphate. (wikipedia.org)
Dehydroquinate1
Catalysis of the reaction: 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate. (systemsbiology.net)
Shikimate pathway2
Thus the amount of carbon entering the shikimate pathway can be controlled by inhibiting DAHP synthase from catalyzing the reaction that forms DAHP. (wikipedia.org)
The first common step in biosynthesis for these amino acids follows the shikimate pathway and the initial reaction, the condensation of erythrose-4-phosphate (E4P) and phosphoenolpyruvate (PEP) is catalyzed by the enzyme family of 3-Deoxy-arabino-heptulosonate-7-phosphate synthases (DAHP synthases). (uni-goettingen.de)
Metal ions are required in order for DAHP synthase to catalyze reactions. (wikipedia.org)
In DAHP synthase, it has been shown that binding site contains patterns of cysteine and histidine residues bound to metal ions in a Cys-X-X-His fashion. (wikipedia.org)
Reaction3
Forms of this enzyme differ between organisms, but can be considered DAHP synthase based upon the reaction that is catalyzed by this enzyme. (wikipedia.org)
The primary function of DAHP synthase is to catalyze the reaction of phosphoenolpyruvate and D-erythrose 4-phosphate to DAHP and phosphate. (wikipedia.org)
The reaction catalyzed by DAHP synthase is shown below. (wikipedia.org)
Bacteria1
Feedback inhibition and transcriptional control are both mechanisms of regulating carbon in bacteria, but the only mechanism of regulation found in DAHP synthase found in plants is transcriptional control. (wikipedia.org)
Substrate1
Anhand der Doppelkomplex-Struktur der DAHP Synthase mit Mangan(II), PEP und dem E4P-Analogon Glycerol-3-Phosphat (G3P) wurden die Bindungstaschen der zwei Substrate innerhalb des aktiven Zentrums bestimmt. (uni-goettingen.de)
Enzyme2
It was also determined that the enzyme is inhibited by inorganic phosphate through noncompetitive inhibition with respect to both substrates and inhibited by DAHP through competitive inhibition with respect to phosphoenolpyruvate and noncompetitive inhibition with respect to D-erythrose 4-phosphate. (wikipedia.org)
It has been shown that, in general, DAHP synthases require a bivalent metal ion cofactor in order for the enzyme to function properly. (wikipedia.org)
Phosphate2
The binding pockets for both substrates could be determined on the basis of the double complex of the DAHP synthase with manganese, PEP and the E4P analogue glyceraldehyde-3-phosphate (G3P). (uni-goettingen.de)
Studies have suggested that one metal ion bonds to each monomer of DAHP synthase. (wikipedia.org)
Compounds1
Compounds (3-4, 6-8, 14-15) were evaluated for their cytotoxic activity against HepG2, MCF-7, SW1116 and HeLa cells and compound 6 and 14 showed moderate cytotoxic activity against HeLa cells with IC50 49.61 ± 2.91 and 28.38 ± 1.57 µM, respectively. (bvsalud.org)
Activity1
In plants, as the plants progressed through the growth cycle, the activity of DAHP synthase changed. (wikipedia.org)
Image3
To the right is an image of DAHP synthase that shows the quaternary structure of DAHP synthase. (wikipedia.org)
This image shows that DAHP synthase consists of two tightly bound dimers. (wikipedia.org)
Below the first image to the right is an image of DAHP synthase that also shows quaternary structure, however this image is in a cartoon view. (wikipedia.org)
Structure1
The quaternary structure of DAHP synthase consists of two tightly bound dimers, which means that DAHP synthase is a tetramer. (wikipedia.org)
Type1
Four previously undescribed diketopiperazine-type alkaloids including one oxepin-containing diketopiperazine-type alkaloid, oxepinamide L (1), three 4-quinazolinone alkaloids, puniceloids E-G (10-12), together with 12 known analogues, protuboxepin D (2), oxepinamides D-G, J-K and I (3-9), puniceloids B-D (13-15) and protubonine B (16), were isolated from the culture of the marine-derived fungus Aspergillus puniceus FAHY0085. (bvsalud.org)