2.6.1.79	739351	Deciphering the role of aspartate and prephenate aminotransferase activities in plastid nitrogen metabolism	Plant Physiol.	164	92-104	2014	Nicotiana benthamiana	https://pubmed.ncbi.nlm.nih.gov/24296073/	
2.6.1.79	722267	Identification of a plant gene encoding glutamate/aspartate-prephenate aminotransferase: the last homeless enzyme of aromatic amino acids biosynthesis	FEBS Lett.	584	4357-4360	2010	Arabidopsis thaliana	https://pubmed.ncbi.nlm.nih.gov/20883697/	
2.6.1.79	657635	Novel features of prephenate aminotransferase from cell cultures of Nicotiana silvestris	Arch. Biochem. Biophys.	238	237-246	1985	Nicotiana sylvestris	https://pubmed.ncbi.nlm.nih.gov/3985619/	
2.6.1.79	659858	Prephenate aminotransferase	Methods Enzymol.	142	479-487	1987	[Brevibacterium] flavum	https://pubmed.ncbi.nlm.nih.gov/3298985/	
2.6.1.79	659858	Prephenate aminotransferase	Methods Enzymol.	142	479-487	1987	Nicotiana sylvestris	https://pubmed.ncbi.nlm.nih.gov/3298985/	
2.6.1.79	659858	Prephenate aminotransferase	Methods Enzymol.	142	479-487	1987	Magnolia sp.	https://pubmed.ncbi.nlm.nih.gov/3298985/	
2.6.1.79	659858	Prephenate aminotransferase	Methods Enzymol.	142	479-487	1987	Sorghum sp.	https://pubmed.ncbi.nlm.nih.gov/3298985/	
2.6.1.79	659858	Prephenate aminotransferase	Methods Enzymol.	142	479-487	1987	Spinacia oleracea	https://pubmed.ncbi.nlm.nih.gov/3298985/	
2.6.1.79	659858	Prephenate aminotransferase	Methods Enzymol.	142	479-487	1987	Lemna sp.	https://pubmed.ncbi.nlm.nih.gov/3298985/	
2.6.1.79	659858	Prephenate aminotransferase	Methods Enzymol.	142	479-487	1987	Hemerocallis hybrid cultivar	https://pubmed.ncbi.nlm.nih.gov/3298985/	
2.6.1.79	659858	Prephenate aminotransferase	Methods Enzymol.	142	479-487	1987	Corynebacterium glutamicum	https://pubmed.ncbi.nlm.nih.gov/3298985/	
2.6.1.79	759965	Structural basis for substrate recognition and inhibition of prephenate aminotransferase from Arabidopsis	Plant J.	94	304-314	2018	Arabidopsis thaliana	https://pubmed.ncbi.nlm.nih.gov/29405514/	
2.6.1.79	738632	Three different classes of aminotransferases evolved prephenate aminotransferase functionality in arogenate-competent microorganisms	J. Biol. Chem.	289	3198-3208	2014	Sinorhizobium meliloti	https://pubmed.ncbi.nlm.nih.gov/24302739/	
2.6.1.79	738632	Three different classes of aminotransferases evolved prephenate aminotransferase functionality in arogenate-competent microorganisms	J. Biol. Chem.	289	3198-3208	2014	Synechocystis sp.	https://pubmed.ncbi.nlm.nih.gov/24302739/	
2.6.1.79	738632	Three different classes of aminotransferases evolved prephenate aminotransferase functionality in arogenate-competent microorganisms	J. Biol. Chem.	289	3198-3208	2014	Streptomyces avermitilis	https://pubmed.ncbi.nlm.nih.gov/24302739/	
2.6.1.79	738632	Three different classes of aminotransferases evolved prephenate aminotransferase functionality in arogenate-competent microorganisms	J. Biol. Chem.	289	3198-3208	2014	Streptomyces avermitilis DSM 46492	https://pubmed.ncbi.nlm.nih.gov/24302739/	
2.6.1.79	660563	Tyrosine biosynthesis in Sorghum bicolor: characteristics of prephenate aminotransferase	Z. Naturforsch. C	41	79-86	1986	Sorghum bicolor x Sorghum sudanesis	https://pubmed.ncbi.nlm.nih.gov/2939644/	
2.6.1.79	759178	Tyrosine metabolism	 identification of a key residue in the acquisition of prephenate aminotransferase activity by 1beta aspartate aminotransferase	FEBS J.	286	2118-2134	2019	Arabidopsis thaliana	https://pubmed.ncbi.nlm.nih.gov/30771275/	
2.6.1.79	759178	Tyrosine metabolism	 identification of a key residue in the acquisition of prephenate aminotransferase activity by 1beta aspartate aminotransferase	FEBS J.	286	2118-2134	2019	Sinorhizobium meliloti	https://pubmed.ncbi.nlm.nih.gov/30771275/