EC number:4.1.1.53
| ID: | 4.1.1.53 |
|---|---|
| Description: | Phenylalanine decarboxylase. |
| Alternative Name: |
L-phenylalanine decarboxylase. L-phenylalanine carboxy-lyase. |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 4.1.1.53 |
| BRENDA Enzyme Link: | BRENDA 4.1.1.53 |
| KEGG Enzyme Link: | KEGG4.1.1.53 |
| BioCyc Enzyme Link: | BioCyc 4.1.1.53 |
| ExPASy Enzyme Link: | ExPASy4.1.1.53 |
| EC2PDB Enzyme Link: | EC2PDB 4.1.1.53 |
| ExplorEnz Enzyme Link: | ExplorEnz 4.1.1.53 |
| PRIAM enzyme-specific profiles Link: | PRIAM 4.1.1.53 |
| IntEnz Enzyme Link: | IntEnz 4.1.1.53 |
| MEDLINE Enzyme Link: | MEDLINE 4.1.1.53 |
| RHEA:19717 | H(+) + L-phenylalanine = 2-phenylethylamine + CO2 |
| RULE(radius=1) | [*:1]=[C;H0;+0:2](-[OH;+0:3])-[CH;+0:4](-[*:5])-[*:6].[H+;H0:7]>>[*:5]-[CH2;+0:4]-[*:6].[*:1]=[C;H0;+0:2]=[O;H0;+0:3] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| The possible role of thyroid aromatic amino acid decarboxylase in thyroxine biosynthesis. | Schulz AR, Oliner L | 1967 Apr 15 | 6034195 |
| Aromatic L-amino acid decarboxylase. | LOVENBERG W, WEISSBACH H, UDENFRIEND S | 1962 Jan | 14466899 |
| Tomato aromatic amino acid decarboxylases participate in synthesis of the flavor volatiles 2-phenylethanol and 2-phenylacetaldehyde. | Tieman D, Taylor M, Schauer N, Fernie AR, Hanson AD, Klee HJ | 2006 May 23 | 16698923 |