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MetaCyc Pathway: tyrosine biosynthesis III

Enzyme View:

This view shows enzymes only for those organisms listed below, in the list of taxa known to possess the pathway. If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.

Superclasses: Biosynthesis Amino Acids Biosynthesis Individual Amino Acids Biosynthesis Tyrosine Biosynthesis

Some taxa known to possess this pathway include ? : Actinoplanes missouriensis , Zea mays

Expected Taxonomic Range: Bacteria , Embryophyta , Fungi

Summary:
General Background

The three aromatic amino acids, L-tryptophan, L-tyrosine, and L-phenylalanine, derived from the common precursor chorismate, are constituents of proteins, and precursors of many plant secondary metabolites. Two steps are required for conversion of prephenate to L-tyrosine: a dehydrogenation/decarboxylation and a transamination. Two possible routes for this conversion are known. In the route described in tyrosine biosynthesis I the decarboxylation occurs first, resulting in the intermediate 4-hydroxyphenylpyruvate, followed by a transamination to L-tyrosine. In the second route, described here, transamination occurs first, resulting in formation of L-arogenate, which is subsequently decarboxylated to L-tyrosine.

While the first route has been confirmed in many microorganisms, including E.coli and yeast, some other bacteria, including cyanobacteria, as well as many plants, employ the arogenate route [Stenmark74, Bonner87]. The two routes have been reported to co-exist in many microorganisms. In addition, the 4-hydroxyphenylpyruvate route cannot be completely ruled out for plants based on these facts:

1) early studies detected prephenate dehydrogenase activity in mung bean shoots [Gamborg66].

2) the Arabidopsis arogenate dehydrogenase TyrAAT2 presents a weak prephenate dehydrogenase activity [Rippert02], even though the high Km for prephenate and low specific activity of prephenate dehydrogenase reaction indicates the reaction is unlikely physiologically significant.

Two types of arogenate dehydrogenase are known, that utilze either NADP+ or NAD+. These two types are described by the pathways tyrosine biosynthesis II and tyrosine biosynthesis III, respectively.

About This Pathway

The two key reactions in this pathway are catalyzed by the enzymes prephenate aminotransferase and arogenate dehydrogenase, respectively.

Arogenate is the branch-point and the immediate precursor for the synthesis of both tyrosine and phenylalanine. Arogenate dehydrogenase is the key enzyme channeling arogenate towards tyrosine synthesis. Its activity is strongly feedback inhibited by tyrosine.

The Arabidopsis arogenate dehydrogenase [Rippert02], as well as the enzyme from the cyanobacterium Synechocystis sp. PCC 6803 [Bonner04], are strictly NADP-dependent (see tyrosine biosynthesis II). The enzymes from maize [Byng81] and the actinobacterium Actinoplanes missouriensis [Hund89] are strictly NAD-dependent.

Variants: tyrosine biosynthesis I , tyrosine biosynthesis II , tyrosine biosynthesis IV

Credits:
Created 09-Jan-2009 by Caspi R , SRI International


References

Bonner04: Bonner CA, Jensen RA, Gander JE, Keyhani NO (2004). "A core catalytic domain of the TyrA protein family: arogenate dehydrogenase from Synechocystis." Biochem J 382(Pt 1);279-91. PMID: 15171683

Bonner87: Bonner C, Jensen R (1987). "Prephenate aminotransferase." Methods Enzymol 142;479-87. PMID: 3298985

Byng81: Byng, Graham, Whitaker, Robert, Flick, Christopher, Jensen, Roy A. "Enzymology of L-tyrosine biosynthesis in corn." Phytochemistry (1981) vol. 20 (6):1289-1292.

Gamborg66: Gamborg OL, Keeley FW (1966). "Aromatic metabolism in plants. I. A study of the prephenate dehydrogenase from bean plants." Biochim Biophys Acta 115(1);65-72. PMID: 4379953

Hund89: Hund HK, Bar G, Lingens F (1989). "Purification and properties of arogenate dehydrogenase from Actinoplanes missouriensis." Z Naturforsch [C] 44(9-10);797-801. PMID: 2590341

Rippert02: Rippert P, Matringe M (2002). "Purification and kinetic analysis of the two recombinant arogenate dehydrogenase isoforms of Arabidopsis thaliana." Eur J Biochem 269(19);4753-61. PMID: 12354106

Stenmark74: Stenmark SL, Pierson DL, Jensen RA, Glover GI (1974). "Blue-green bacteria synthesise L-tyrosine by the pretyrosine pathway." Nature 247(439);290-2. PMID: 4206476

Other References Related to Enzymes, Genes, Subpathways, and Substrates of this Pathway

Baldwin81: Baldwin GS, Davidson BE (1981). "A kinetic and structural comparison of chorismate mutase/prephenate dehydratase from mutant strains of Escherichia coli K 12 defective in the PheA gene." Arch Biochem Biophys 1981;211(1);66-75. PMID: 7030214

Baldwin83: Baldwin GS, Davidson BE (1983). "Kinetic studies on the mechanism of chorismate mutase/prephenate dehydratase from Escherichia coli K12." Biochim Biophys Acta 1983;742(2);374-83. PMID: 6337635

Bonner85: Bonner CA, Jensen RA (1985). "Novel features of prephenate aminotransferase from cell cultures of Nicotiana silvestris." Arch Biochem Biophys 238(1);237-46. PMID: 3985619

Chook94: Chook YM, Gray JV, Ke H, Lipscomb WN (1994). "The monofunctional chorismate mutase from Bacillus subtilis. Structure determination of chorismate mutase and its complexes with a transition state analog and prephenate, and implications for the mechanism of the enzymatic reaction." J Mol Biol 1994;240(5);476-500. PMID: 8046752

Connelly86: Connelly JA, Conn EE (1986). "Tyrosine biosynthesis in Sorghum bicolor: isolation and regulatory properties of arogenate dehydrogenase." Z Naturforsch C 41(1-2);69-78. PMID: 2939643

Dopheide72: Dopheide TA, Crewther P, Davidson BE (1972). "Chorismate mutase-prephenate dehydratase from Escherichia coli K-12. II. Kinetic properties." J Biol Chem 247(14);4447-52. PMID: 4261395

Duggleby78: Duggleby RG, Sneddon MK, Morrison JF (1978). "Chorismate mutase-prephenate dehydratase from Escherichia coli: active sites of a bifunctional enzyme." Biochemistry 1978;17(8);1548-54. PMID: 348236

Eberhard96: Eberhard J, Ehrler TT, Epple P, Felix G, Raesecke HR, Amrhein N, Schmid J (1996). "Cytosolic and plastidic chorismate mutase isozymes from Arabidopsis thaliana: molecular characterization and enzymatic properties." Plant J 10(5);815-21. PMID: 8953244

Editors93: Editors: Abraham L. Sonenshein, James A. Hoch, Richard Losick (1993). "Bacillus subtilis and Other Gram-Positive Bacteria: Biochemistry, Physiology, and Molecular Genetics." American Society For Microbiology, Washington, DC 20005.

Gaines82: Gaines C G, Byng G S, Whitaker R J, Jensen R A (1982). "L-tyrosine regulation and biosynthesis via arogenate dehydrogenase in suspension-cultured cells of Nicotiana silvestris Speg. et Comes." Planta 156(3);233-240.

Gething77: Gething MJ, Davidson BE (1977). "Chorismate mutase/prephenate dehydratase from Escherichia coli K12. Effects of chemical modification on the enzymic activities and allosteric inhibition." Eur J Biochem 1977;78(1);111-7. PMID: 334530

Gething77a: Gething MJ, Davidson BE (1977). "Chorismate mutase/prephenate dehydratase from Escherichia coli K12. Modification with 5,5'-dithio-bis(2-nitrobenzoic acid)." Eur J Biochem 1977;78(1);103-10. PMID: 334529

Gray90: Gray JV, Golinelli-Pimpaneau B, Knowles JR (1990). "Monofunctional chorismate mutase from Bacillus subtilis: purification of the protein, molecular cloning of the gene, and overexpression of the gene product in Escherichia coli." Biochemistry 1990;29(2);376-83. PMID: 2105742

Haunso97: Haunso S, Carlsen J, Sheikh S (1997). "The new ischemic syndromes. Remodelling of the heart is due to a biochemical and not haemodynamic mechanism?." Basic Res Cardiol 1997;92 Suppl 2;60-1. PMID: 9457377

Holding10: Holding DR, Meeley RB, Hazebroek J, Selinger D, Gruis F, Jung R, Larkins BA (2010). "Identification and characterization of the maize arogenate dehydrogenase gene family." J Exp Bot 61(13);3663-73. PMID: 20558569

Hudson83: Hudson GS, Howlett GJ, Davidson BE (1983). "The binding of tyrosine and NAD+ to chorismate mutase/prephenate dehydrogenase from Escherichia coli K12 and the effects of these ligands on the activity and self-association of the enzyme. Analysis in terms of a model." J Biol Chem 1983;258(5);3114-20. PMID: 6338013

Kane71: Kane JF, Stenmark SL, Calhoun DH, Jensen RA (1971). "Metabolic interlock. The role of the subordinate type of enzyme in the regulation of a complex pathway." J Biol Chem 1971;246(13);4308-16. PMID: 4996881

Koch72: Koch GL, Shaw DC, Gibson F (1972). "Studies on the relationship between the active sites of chorismate mutase-prephenate dehydrogenase from Escherichia coli or Aerobacter aerogenes." Biochim Biophys Acta 1972;258(3);719-30. PMID: 4552899

Lassila05: Lassila JK, Keeffe JR, Oelschlaeger P, Mayo SL (2005). "Computationally designed variants of Escherichia coli chorismate mutase show altered catalytic activity." Protein Eng Des Sel 18(4);161-3. PMID: 15820980

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

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Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Fri Dec 19, 2014, biocyc11.