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2 Bibliography  














Shikimate pathway






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From Wikipedia, the free encyclopedia
 


The shikimate pathway (shikimic acid pathway) is a seven-step metabolic pathway used by bacteria, archaea, fungi, algae, some protozoans, and plants for the biosynthesisoffolates and aromatic amino acids (tryptophan, phenylalanine, and tyrosine). This pathway is not found in mammals.

The seven enzymes involved in the shikimate pathway are DAHP synthase, 3-dehydroquinate synthase, 3-dehydroquinate dehydratase, shikimate dehydrogenase, shikimate kinase, EPSP synthase, and chorismate synthase. The pathway starts with two substrates, phosphoenol pyruvate and erythrose-4-phosphate, and ends with chorismate (chrorismic acid), a substrate for the three aromatic amino acids. The fifth enzyme involved is the shikimate kinase, an enzyme that catalyzes the ATP-dependent phosphorylationofshikimate to form shikimate 3-phosphate (shown in the figure below).[1] Shikimate 3-phosphate is then coupled with phosphoenol pyruvate to give 5-enolpyruvylshikimate-3-phosphate via the enzyme 5-enolpyruvylshikimate-3-phosphate (EPSP) synthase. Glyphosate, the herbicidal ingredient in Roundup, is a competitive inhibitor of EPSP synthase, acting as a transition state analog that binds more tightly to the EPSPS-S3P complex than PEP and inhibits the shikimate pathway.

Then 5-enolpyruvylshikimate-3-phosphate is transformed into chorismate by a chorismate synthase.

Prephenic acid is then synthesized by a Claisen rearrangementofchorismatebychorismate mutase.[2][3]

Prephenate is oxidatively decarboxylated with retention of the hydroxyl group to give p-hydroxyphenylpyruvate, which is transaminated using glutamate as the nitrogen source to give tyrosine and α-ketoglutarate.

References[edit]

  1. ^ Herrmann, K. M.; Weaver, L. M. (1999). "The Shikimate Pathway". Annual Review of Plant Physiology and Plant Molecular Biology. 50: 473–503. doi:10.1146/annurev.arplant.50.1.473. PMID 15012217.
  • ^ Helmut Goerisch (1978). "On the mechanism of the chorismate mutase reaction". Biochemistry. 17 (18): 3700–3705. doi:10.1021/bi00611a004. PMID 100134.
  • ^ Peter Kast; Yadu B. Tewari; Olaf Wiest; Donald Hilvert; Kendall N. Houk; Robert N. Goldberg (1997). "Thermodynamics of the Conversion of Chorismate to Prephenate: Experimental Results and Theoretical Predictions". J. Phys. Chem. B. 101 (50): 10976–10982. doi:10.1021/jp972501l.
  • Bibliography[edit]


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