| Entry |
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| Name |
tyrosine decarboxylase;
L-tyrosine decarboxylase;
L-(-)-tyrosine apodecarboxylase;
L-tyrosine carboxy-lyase
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| Class |
Lyases;
Carbon-carbon lyases;
Carboxy-lyases
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| Sysname |
L-tyrosine carboxy-lyase (tyramine-forming)
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| Reaction(IUBMB) |
L-tyrosine = tyramine + CO2 [RN: R00736]
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| Reaction(KEGG) |
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| Substrate |
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| Product |
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| Comment |
A pyridoxal-phosphate protein. The bacterial enzyme also acts on 3-hydroxytyrosine and, more slowly, on 3-hydroxyphenylalanine.
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| History |
EC 4.1.1.25 created 1961
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| Pathway |
| ec00950 | Isoquinoline alkaloid biosynthesis |
| ec01110 | Biosynthesis of secondary metabolites |
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| Orthology |
| K18933 | tyrosine decarboxylase / aspartate 1-decarboxylase |
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| Genes |
» show all
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| Reference |
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| Authors |
McGILVERY RW, COHEN PP |
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| Title |
The decarboxylation of L-phenylalanine by Streptococcus faecalis R. |
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| Journal |
J Biol Chem 174:813-6 (1948) |
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| Other DBs |
| ExplorEnz - The Enzyme Database: | 4.1.1.25 |
| ExPASy - ENZYME nomenclature database: | 4.1.1.25 |
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| LinkDB |
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