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Results 1 - 10 of 31

EC Number	Substrates	Commentary Substrates	Products	Commentary (Products)	Reversibility
2.6.1.79	more	the substrate specificity of the enzyme in bacteria is less high than in plants	?	-	?
2.6.1.79	more	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	?	-	?
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
2.6.1.79	prephenate + L-glutamate	prephenate is the preferred substrate	L-arogenate + 2-oxoglutarate	L-arogenate is cyclohexadienylic acid	r
2.6.1.79	prephenate + L-glutamate	optimal prephenate concentration is 0.5-1.0 mM	L-arogenate + 2-oxoglutarate	-	r
2.6.1.79	more	no substrates: 4-hydroxyphenylpyruvate, phenylpyruvate	?	-	?
2.6.1.79	more	no activity with oxaloacetate, 2-ketoglutarate, or pyruvate with L-glutamate	?	-	?
2.6.1.79	prephenate + L-glutamate	important step in biosynthesis of L-tyrosine and L-phenylalanine	L-arogenate + 2-oxoglutarate	-	r
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
2.6.1.79	prephenate + L-aspartate	about 50% of the activity with L-glutamate	L-arogenate + oxaloacetate	-	r

Results 1 - 10 of 31