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4.1.1.53 |
| Description |
Phenylalanine decarboxylase. |
| Alternative names |
L-phenylalanine decarboxylase. |
| Catalyzed reaction |
L-phenylalanine = phenylethylamine + CO(2). |
| Cofactor |
Pyridoxal-phosphate. |
| Comments |
-!- Also acts on tyrosine and other aromatic amino acids. |
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Enzymes with this activity are enlisted under EC 4.1.1.28 (aromatic amino acid decarboxylase)
Phenylacetaldehyde synthase from petunia is a specialized aromatic amino acid decarboxylase that is capable of stoichiometrically coupling the decarboxylation of Phe with the further conversion of phenylethylamine to phenylacetaldehyde. |
| Organisms |
-Bacteria -Plants -Metazoa -Human |
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| Links |
Enzyme (activities) 4.1.1.53
BRENDA (activities) 4.1.1.53
KEGG (pathways) 4.1.1.53
PLPMDB (PLP mutants) 4.1.1.53
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| References |
Kaminaga, Y.; Schnepp, J.;Peel G, Kish CM;Ben-Nissan G,Weiss D, Orlova I,Lavie O, Rhodes D, Wood K, Porterfield DM, Cooper AJ, Schloss JV, Pichersky E, Vainstein A, Dudareva N.
(2006) Plant phenylacetaldehyde synthase is a bifunctional homotetrameric enzyme that catalyzes phenylalanine decarboxylation and oxidation J. Biol. Chem. 281 23357-66. David, J. C.; Dairman, W.; Udenfriend, S. (1974) On the importance of decarboxylation in the metabolism of phenylalanine, tyrosine, and tryptophan Arch Biochem Biophys 160 561-8.. |
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| last changed |
2008/01/30 19:17 |
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