Literature summary for 2.6.1.79 extracted from

Siehl, D.L.; Connelly, J.A.; Conn, E.E.
Tyrosine biosynthesis in Sorghum bicolor: characteristics of prephenate aminotransferase (1986), Z. Naturforsch. C, 41, 79-86.

Search for more literature for 2.6.1.79

General Stability

General Stability	Organism
pyridoxal 5'-phosphate, EDTA, and glycerol stabilize, required for activity assay	Sorghum bicolor x Sorghum sudanesis

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.07	-	prephenate	pH 8.0	Sorghum bicolor x Sorghum sudanesis
0.8	-	L-arogenate	pH 8.0	Sorghum bicolor x Sorghum sudanesis
1.07	-	L-glutamate	pH 8.0	Sorghum bicolor x Sorghum sudanesis

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
prephenate + L-glutamate	Sorghum bicolor x Sorghum sudanesis	important step in biosynthesis of L-tyrosine and L-phenylalanine	L-arogenate + 2-oxoglutarate	-	r

Organism

Organism	UniProt	Comment	Textmining
Sorghum bicolor x Sorghum sudanesis	-	hybrid	-

Purification (Commentary)

Purification (Comment)	Organism
partially by ion exchange chromatography	Sorghum bicolor x Sorghum sudanesis

Source Tissue

Source Tissue	Comment	Organism	Textmining
shoot	etiolated, 4-days-old	Sorghum bicolor x Sorghum sudanesis	-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
additional information	-	substrate specificity	Sorghum bicolor x Sorghum sudanesis
additional information	-	partially purified enzyme, activity of prephenate aminotransferase as a function of the concentration of prephenate and glutamate	Sorghum bicolor x Sorghum sudanesis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
4-hydroxyphenylpyruvate + L-glutamate	10% of the activity with prephenate at 1.0 mM substrate concentration	Sorghum bicolor x Sorghum sudanesis	L-tyrosine + 2-oxoglutarate	-	r
oxaloacetate + L-glutamate	78% of the activity with prephenate at 1.0 mM substrate concentration	Sorghum bicolor x Sorghum sudanesis	L-aspartate + 2-oxoglutarate	-	r
prephenate + L-aspartate	20% of the activity with L-glutamate	Sorghum bicolor x Sorghum sudanesis	L-arogenate + oxaloacetate	-	r
prephenate + L-glutamate	important step in biosynthesis of L-tyrosine and L-phenylalanine	Sorghum bicolor x Sorghum sudanesis	L-arogenate + 2-oxoglutarate	-	r
prephenate + L-glutamate	enzyme shows high affinity and specificity for prephenate, similar reaction rate in both reaction directions	Sorghum bicolor x Sorghum sudanesis	L-arogenate + 2-oxoglutarate	-	r
pyruvate + L-glutamate	10% of the activity with prephenate at 1.0 mM substrate concentration	Sorghum bicolor x Sorghum sudanesis	L-alanine + 2-oxoglutarate	-	r

Synonyms

Synonyms	Comment	Organism
prephenate aminotransferase	-	Sorghum bicolor x Sorghum sudanesis
prephenate: glutamate aminotransferase	-	Sorghum bicolor x Sorghum sudanesis

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
70	-	-	Sorghum bicolor x Sorghum sudanesis

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
70	-	95% remaining activity after 17 min	Sorghum bicolor x Sorghum sudanesis

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8	-	-	Sorghum bicolor x Sorghum sudanesis

pH Range

pH Minimum	pH Maximum	Comment	Organism
6	10.5	no activity below pH 6.0 and above pH 10.5	Sorghum bicolor x Sorghum sudanesis

Cofactor

Cofactor	Comment	Organism	Structure
pyridoxal 5'-phosphate	-	Sorghum bicolor x Sorghum sudanesis

pI Value

Organism	Comment	pI Value Maximum	pI Value
Sorghum bicolor x Sorghum sudanesis	isoelectric focusing	-	5.2

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Release 2023.1 (January 2023)