2.6.1.79	additional information	the substrate specificity of the enzyme in bacteria is less high than in plants	?	-	?	89	
2.6.1.79	additional information	substrate specificity, no activity with 4-hydroxyphenylpyruvate, phenylpyruvate, and indolepyruvate using cosubstrate L-glutamate, no activity with 4-hydroxyphenylpyruvate, phenylpyruvate, and pyruvate using cosubstrate L-aspartate	?	-	?	89	
2.6.1.79	prephenate + L-glutamate	prephenate is the preferred substrate, optimal at low concentrations of about 1 mM	L-arogenate + 2-oxoglutarate	L-arogenate is cyclohexadienylic acid	r	375251	
2.6.1.79	prephenate + L-glutamate	prephenate is the preferred substrate	L-arogenate + 2-oxoglutarate	L-arogenate is cyclohexadienylic acid	r	375251	
2.6.1.79	prephenate + L-glutamate	optimal prephenate concentration is 0.5-1.0 mM	L-arogenate + 2-oxoglutarate	-	r	375251	
2.6.1.79	additional information	no substrates: 4-hydroxyphenylpyruvate, phenylpyruvate	?	-	?	89	
2.6.1.79	additional information	no activity with oxaloacetate, 2-ketoglutarate, or pyruvate with L-glutamate	?	-	?	89	
2.6.1.79	prephenate + L-glutamate	important step in biosynthesis of L-tyrosine and L-phenylalanine	L-arogenate + 2-oxoglutarate	-	r	375251	
2.6.1.79	prephenate + L-glutamate	enzyme shows high affinity and specificity for prephenate, similar reaction rate in both reaction directions	L-arogenate + 2-oxoglutarate	-	r	375251	
2.6.1.79	prephenate + L-aspartate	about 50% of the activity with L-glutamate	L-arogenate + oxaloacetate	-	r	375250