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Glutamate-prephenate aminotransferase
Identifiers
EC no.	2.6.1.79
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Search PMC articles PubMed articles NCBI proteins

In enzymology, glutamate-prephenate aminotransferase (EC 2.6.1.79, also known as prephenate transaminase, PAT, and L-glutamate:prephenate aminotransferase) is an enzyme that catalyzes the chemical reaction

L-arogenate + 2-oxoglutarate $\rightleftharpoons$ prephenate + L-glutamate

Thus, the two substrates of this enzyme are L-arogenate and 2-oxoglutarate, whereas its two products are prephenate and L-glutamate. However, in most plant species utilizing this enzyme, the left side of the reaction is strongly favored. Therefore, glutamate is used as the amino donor to convert prephenate into arogenate.

Background

This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-arogenate:2-oxoglutarate aminotransferase. Other names in common use include prephenate transaminase (ambiguous), PAT (ambiguous), and L-glutamate:prephenate aminotransferase. It operates in the phenylalanine and tyrosine biosynthesis pathway. The gene which encodes this enzyme has recently been identified in various plant species and microorganisms, meaning that all genes in the pathway have now been identified and accounted for. This pathway occurs in many different plant species. As phenylalanine is an essential amino acid, humans (and other animals) have lost the ability to produce it and must therefore obtain it from their diet. As such, the activity of this enzyme in various plant species affects the survival of animals as well. In these animals, tyrosine is synthesized from phenylalanine via the enzyme phenylalanine hydroxylase, whereas plants have their own method of tyrosine synthesis.

Function

Glutamate-Prephanate Aminotransferase catalyzes the reaction shown below

The enzyme catalyzes the reaction above, an important step in the synthesis of phenylalanine, tyrosine, and tryptophan. From left to right, the species involved are L-arogenate, 2-oxoglutarate, prephenate, and L-glutamate.

,

and its primary purpose is to convert prephenate into arogenate via transamination, using glutamate as the amino donor. As stated previously, the left side of the reaction is strongly favored. This is a necessary process for any organism which needs to convert arogenate into phenylalanine or tyrosine, as arogenate is an intermediate in the reactions which synthesize these amino acids, an alternative route to that involving phenylpyruvate and hydroxyphenylpyruvate. In the absence of glutamate, aspartate can act as the amino donor in the reaction without the need for a different enzyme, but this reaction proceeds more slowly. The details of the activity of this enzyme are still somewhat of a mystery.

Structure

Little is known about the structure of glutamate-prephenate aminotransferase. However, some data indicates that the enzyme may have an α₂-β₂ subunit structure.

References

• Bonner CA, Jensen RA (1985). "Novel features of prephenate aminotransferase from cell cultures of Nicotiana silvestris". Arch. Biochem. Biophys. 238 (1): 237–46. doi:10.1016/0003-9861(85)90161-4. PMID 3985619.

• Siehl DL, Connelly JA, Conn EE (1986). "Tyrosine biosynthesis in Sorghum bicolor: characteristics of prephenate aminotransferase". Z. Naturforsch. [C]. 41 (1–2): 79–86. doi:10.1515/znc-1986-1-213. PMID 2939644.{{cite journal}}: CS1 maint: multiple names: authors list (link)
• Bonner C, Jensen R (1987). Prephenate aminotransferase. Methods Enzymol. Vol. 142. pp. 479–87. doi:10.1016/S0076-6879(87)42059-4. ISBN 978-0-12-182042-8. PMID 3298985.
• "Orthology: K15849." KEGG. KEGG. Web. <http://www.kegg.jp/dbget-bin/www_bget?K158492.6.1.79 R07276>.
• FEBS Lett. 2010 Oct 22;584(20):4357-60. doi: 10.1016/j.febslet.2010.09.037. Epub 2010 Sep 29.
• Maeda, Hiroshi, Heejin Yoo, and Natalia Dudareva. "Prephenate aminotransferase directs plant phenylalanine biosynthesis via arogenate." Nature Chemical Biology. 7 (2010): 19-21.
• De-Eknamkul, W, and BE Ellis. "Purification and characterization of prephenate aminotransferase from Anchusa officinalis cell cultures." PubMed. 1988 Nov 15;267(1): 87-94.
• Dal Cin et al. The Plant Cell, Vol. 23: 2738–2753, July 2011, www.plantcell.org 2011 American Society of Plant Biologists.
• Graindorge. "Three Different Classes of Aminotransferases Evolved Prephenate Aminotransferase Functionality in Arogenate-competent Microorganisms." The Journal of Biological Chemistry. 2014 Feb 7; 289: 3198-3208.

Category:EC 2.6.1

Category:Enzymes of unknown structure