prephenate dehydrogenase

Gene: (Saccharomyces Cerevisiae) TYR1{{cite journal | vauthors = Mannhaupt G, Stucka R, Pilz U, Schwarzlose C, Feldmann H | year = 1989 | title = Characterization of the Prephenate Dehydrogenase-encoding Gene, TYR1, from Saccharomyces Cerevisiae | journal = Gene | volume = 85 | issue = 2| pages = 303–11 | doi=10.1016/0378-1119(89)90422-8| pmid = 2697638 }}

Shikimate pathway: Arogenate/Prephenate (ADH/PDH). Although in the shikimate pathway arogenate and prephenate dehydrogenase catalyze different reactions, they can at times be used interchangeably."EC 1.3.1.13." EC 1.3.1.13. IUBMB Enzyme Nomenclature, 1972. Web. 24 Apr. 2014.

• TyrA (tyrosine A: within the tyrosine pathway)"Prephenate Dehydrogenase - TyrA - Bacillus Subtilis (strain 168)."Prephenate Dehydrogenase - TyrA - Bacillus Subtilis (strain 168). UniProt, 13 Nov. 2013. Web. 24 Apr. 2014.
• Prephenate dehydrogenase"EC 1.3.1.13." EC 1.3.1.13. IUBMB Enzyme Nomenclature, 1972. Web. 24 Apr. 2014.
• Prephenate (Nicotinamide adenine dinucleotide phosphate) dehydrogenase"EC 1.3.1.13." EC 1.3.1.13. IUBMB Enzyme Nomenclature, 1972. Web. 24 Apr. 2014.
• Prephenate dehydrogenase (NADP)"EC 1.3.1.13." EC 1.3.1.13. IUBMB Enzyme Nomenclature, 1972. Web. 24 Apr. 2014.
• NADP+ oxidoreductase"EC 1.3.1.13." EC 1.3.1.13. IUBMB Enzyme Nomenclature, 1972. Web. 24 Apr. 2014.

This enzyme so far has been found in sixteen different organisms; twelve different kinds of bacteria (mostly cyanobacteria) and four different kinds of plants (mostly different kinds of beans)."EC 1.3.1.13 - Prephenate Dehydrogenase (NADP+)." Information on Prephenate Dehydrogenase. BRENDA, n.d. Web. 24 Apr. 2014.

Bacteria organisms (examples): Acenitobacter calcoaceticus, Fischerella sp., Flavobacterium so., Comamonas testosteroni, and nostoc sp.

Plant organisms: phaseolus coccineus, phaseolus vulgaris, vicia faba, vigna radiata

Present in the shikimate pathway, in the pathway to synthesize tyrosine (a non-essential amino acid in both plants and animals). It catalyzes the oxidative decarboxylation reaction of prephenate to 4-hydroxyphenylpyruvate."InterPro." Bifunctional Chorismate Mutase/prephenate Dehydrogenase T-protein (IPR008244). InterPro, n.d. Web. 24 Apr. 2014.

File:Prephenate dehydrogenase reaction.png

In enzymology, a prephenate dehydrogenase ({{EC number|1.3.1.12}}) is an enzyme that catalyzes the chemical reaction

: prephenate + NAD⁺ $\backslash rightleftharpoons$ 4-hydroxyphenylpyruvate + CO₂ + NADH

Thus, the two substrates of this enzyme are prephenate and NAD⁺, whereas its 3 products are 4-hydroxyphenylpyruvate, CO₂, and NADH.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is prephenate:NAD+ oxidoreductase (decarboxylating). Other names in common use include hydroxyphenylpyruvate synthase, and chorismate mutase---prephenate dehydrogenase. This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis and novobiocin biosynthesis.

Also found in haemophilus influenzae, synechocystis (bacteria), and aquifex aeolicus (plant).

However, in haemophilus influenzae, prephenate dehydrogenase is fused with the enzyme chorismate mutase. This fusion is not found in plants or animals.{{cite journal |vauthors=Chiu HJ, Abdubek P, Astakhova T, Axelrod HL, Carlton D, Clayton T, Das D, Deller MC, Duan L, Feuerhelm J, Grant JC, Grzechnik A, Han GW, Jaroszewski L, Jin KK, Klock HE, Knuth MW, Kozbial P, Krishna SS, Kumar A, Marciano D, McMullan D, Miller MD, Morse AT, Nigoghossian E, Okach L, Reyes R, Tien HJ, Trame CB, van den Bedem H, Weekes D, Xu Q, Hodgson KO, Wooley J, Elsliger MA, Deacon AM, Godzik A, Lesley SA, Wilson IA | pmid=20944228 |title=The Structure of Haemophilus Influenzae Prephenate Dehydrogenase Suggests Unique Features of Bifunctional TyrA Enzymes | doi=10.1107/S1744309110021688 | volume=66 | issue=Pt 10 | date=Oct 2010 | journal=Acta Crystallogr F | pages=1317–25 | pmc=2954222}}

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes {{PDB link|2G5C}} and {{PDB link|2PV7}}.

{{reflist}}

{{CH-CH oxidoreductases}}

{{Enzymes}}

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Category:Enzymes of known structure

Category:EC 1.3.1

Category:NADH-dependent enzymes