Enzymes
| UniProtKB help_outline | 1 proteins |
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| GO Molecular Function help_outline |
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- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,176 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-phenylalanine Identifier CHEBI:58095 Charge 0 Formula C9H11NO2 InChIKeyhelp_outline COLNVLDHVKWLRT-QMMMGPOBSA-N SMILEShelp_outline [NH3+][C@@H](Cc1ccccc1)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 72 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 2-phenylethylamine Identifier CHEBI:225237 (Beilstein: 3539103) help_outline Charge 1 Formula C8H12N InChIKeyhelp_outline BHHGXPLMPWCGHP-UHFFFAOYSA-O SMILEShelp_outline [NH3+]CCc1ccccc1 2D coordinates Mol file for the small molecule Search links Involved in 7 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline CO2 Identifier CHEBI:16526 (Beilstein: 1900390; CAS: 124-38-9) help_outline Charge 0 Formula CO2 InChIKeyhelp_outline CURLTUGMZLYLDI-UHFFFAOYSA-N SMILEShelp_outline O=C=O 2D coordinates Mol file for the small molecule Search links Involved in 980 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:19717 | RHEA:19718 | RHEA:19719 | RHEA:19720 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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The possible role of thyroid aromatic amino acid decarboxylase in thyroxine biosynthesis.
Schulz A.R., Oliner L.
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Tomato aromatic amino acid decarboxylases participate in synthesis of the flavor volatiles 2-phenylethanol and 2-phenylacetaldehyde.
Tieman D., Taylor M., Schauer N., Fernie A.R., Hanson A.D., Klee H.J.
An important phenylalanine-derived volatile compound produced by plants is 2-phenylethanol. It is a major contributor to flavor in many foods, including fresh fruits, such as tomato, and an insect-attracting scent in roses and many other flowers. Despite the centrality of 2-phenylethanol to flavor ... >> More
An important phenylalanine-derived volatile compound produced by plants is 2-phenylethanol. It is a major contributor to flavor in many foods, including fresh fruits, such as tomato, and an insect-attracting scent in roses and many other flowers. Despite the centrality of 2-phenylethanol to flavor and fragrance, the plant genes responsible for its synthesis have not been identified. Here, we describe a biosynthetic pathway for 2-phenylethanol and other phenylalanine-derived volatiles in tomato fruits and a small family of decarboxylases (LeAADC1A, LeAADC1B, and LeAADC2) that can mediate that pathway's first step. These enzymes each catalyze conversion of phenylalanine to phenethylamine and tyrosine to tyramine. Although tyrosine is the preferred substrate in vitro, phenylalanine levels in tomato fruits far exceed those of tyrosine, indicating that phenylalanine is a physiological substrate. Consistent with this view, overexpression of either LeAADC1A or LeAADC2 in transgenic tomato plants resulted in fruits with up to 10-fold increased emissions of the products of the pathway, including 2-phenylacetaldehyde, 2-phenylethanol, and 1-nitro-2-phenylethane. Further, antisense reduction of LeAADC2 significantly reduced emissions of these volatiles. Besides establishing a biosynthetic route, these results show that it is possible to change phenylalanine-based flavor and aroma volatiles in plants by manipulating expression of a single gene. << Less
Proc Natl Acad Sci U S A 103:8287-8292(2006) [PubMed] [EuropePMC]
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Aromatic L-amino acid decarboxylase.
LOVENBERG W., WEISSBACH H., UDENFRIEND S.