| EC |
2.6.1.79 |
| Accepted name: |
glutamate—prephenate aminotransferase |
| Reaction: |
L-arogenate + 2-oxoglutarate = prephenate + L-glutamate |
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For diagram of phenylalanine and tyrosine biosynthesis, click here |
| Other name(s): |
prephenate transaminase (ambiguous); PAT (ambiguous); L-glutamate:prephenate aminotransferase |
| Systematic name: |
L-arogenate:2-oxoglutarate aminotransferase |
| Comments: |
A pyridoxal-phosphate protein. Aspartate can also act as the amino donor, but more slowly (cf. EC 2.6.1.78, aspartate—prephenate aminotransferase). The enzyme from higher plants shows a marked preference for prephenate as substrate compared to pyruvate, phenylpyruvate or 4-hydroxyphenylpyruvate [1]. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Bonner, C.A. and Jensen, R.A. Novel features of prephenate aminotransferase from cell cultures of Nicotiana silvestris. Arch. Biochem. Biophys. 238 (1985) 237–246. [DOI] [PMID: 3985619] |
| 2. |
Siehl, D.L., Connelly, J.A. and Conn, E.E. Tyrosine biosynthesis in Sorghum bicolor: characteristics of prephenate aminotransferase. Z. Naturforsch. 41 (1986) 79–86. [PMID: 2939644] |
| 3. |
Bonner, C. and Jensen, R. Prephenate aminotransferase. Methods Enzymol. 142 (1987) 479–487. [PMID: 3298985] |
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| [EC 2.6.1.79 created 2005] |
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