3-dehydroquinate synthase
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The enzyme 3-dehydroquinate synthase (EC 4.2.3.4) catalyzes the chemical reaction
- [[3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate]] 3-dehydroquinate+ phosphate
The protein uses NAD+ to catalyze the reaction.[2][3] This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids.
3-Dehydroquinate synthase belongs to the family of lyases, to be specific those carbon-oxygen lyases acting on phosphates. This enzyme participates in phenylalanine, tyrosine, and tryptophan biosynthesis. It employs one cofactor, cobalt (Co2+).
Background
The
Function
3-Dehydroquinate synthase utilizes a complex multi-step mechanism that includes alcohol oxidation, phosphate β-elimination, carbonyl reduction, ring opening, and intramolecular aldol condensation.[5] Dehydroquinate synthase requires
Applications
3-Dehydroquinate synthase catalyzes the second step in the shikimate pathway, which is essential for the production of aromatic amino acids in bacteria, plants, and fungi, but not mammals. This makes it an ideal target for new antimicrobial agents, anti-parasitic agents, and herbicides.[1] Other enzymes in the shikimate pathway have already been targeted and put to use as herbicides.
Nomenclature
The systematic name of this enzyme class is 3-deoxy-D-arabino-hept-2-ulosonate-7-phosphate phosphate-lyase (cyclizing; 3-dehydroquinate-forming). Other names in common use include 5-dehydroquinate synthase, 5-dehydroquinic acid synthetase, dehydroquinate synthase, 3-dehydroquinate synthetase, 3-deoxy-arabino-heptulosonate-7-phosphate phosphate-lyase, (cyclizing), and 3-deoxy-arabino-heptulonate-7-phosphate phosphate-lyase (cyclizing).
References
Further reading
- Rotenberg SL, Sprinson DB (December 1970). "Mechanism and stereochemistry of 5-dehydroquinate synthetase". Proceedings of the National Academy of Sciences of the United States of America. 67 (4): 1669–72. PMID 5275368.
- Srinivasan PR, Rothschild J, Sprinson DB (October 1963). "The enzymic conversion of 3-deoxy-d-arabino-heptulosonic acid 7-phosphate to 5-dehydroquinate". The Journal of Biological Chemistry. 238 (10): 3176–82. PMID 14085358.
- Bender SL, Mehdi S, Knowles JR (September 1989). "Dehydroquinate synthase: the role of divalent metal cations and of nicotinamide adenine dinucleotide in catalysis". Biochemistry. 28 (19): 7555–60. PMID 2514789.
- Carpenter EP, Hawkins AR, Frost JW, Brown KA (July 1998). "Structure of dehydroquinate synthase reveals an active site capable of multistep catalysis". Nature. 394 (6690): 299–302. S2CID 4423190.
