Phenylalanine ammonia lyase
| Phenylalanine ammonia lyase | ||
|---|---|---|
| other names |
|
|
| Enzyme classification | ||
| EC, category | 4.3.1.24 , lyase | |
| Response type | Elimination of ammonia | |
| Substrate | Phenylalanine | |
| Products | trans -cinnamate + NH 3 | |
| Occurrence | ||
| Parent taxon | plants | |
The phenylalanine ammonia-lyase (PAL) is an enzyme which primarily in eukaryotes and bacteria occurs. PAL converts the amino acid phenylalanine to cinnamic acid with the release of ammonia (NH 3 ) . This is the first step in the biosynthesis of the phenylpropanoids . PAL is one of two enzymes with the amino acid dehydroalanine .
Since phenylalanine is a product of the primary metabolism of the plant and is removed from the primary metabolism by the formation of cinnamic acid, the biosynthesis of PAL and its activity is subject to the control of z. B. Light (via the phytochrome system) and other factors. For example, the PAL is activated when the plant is injured, probably to stimulate the synthesis of secondary plant substances.
The enzyme is mostly encoded by three or four genes; H. Several paralogous isoforms exist in many plants .
Individual evidence
- ↑ Information on EC 4.3.1.5 - phenylalanine ammonia-lyase. In: BRENDA. July 2019, accessed December 31, 2019 .
- ↑ UniProtKB results. In: UniProtKB. Accessed December 31, 2019 .
- ↑ Swiss Institute of Bioinformatics (SIB): PROSITE documentation PDOC00424. Phenylalanine and histidine ammonia-lyases. Retrieved August 12, 2011 .
- ↑ The Seed: Info: The archive link was automatically inserted and not yet checked. Please check the original and archive link according to the instructions and then remove this notice.
