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ala_decarboxylase |
Description |
Alanine decarboxylase (4.1.1.-) |
Catalyzed reaction |
L-alanine = ethylamine + CO(2). |
Cofactor |
Pyridoxal-phosphate. |
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A very specialized decarboxylase described in Camellia sinensis (tea plant) and apparently required to provide ethylamine for the production of the non-proteinogenic amino acid L-theanine. Theanine is found primarily in particular plant (Camellia and strictly relatetd species) and in some fungi (Xerocomus badius). |
Organisms |
-Plants |
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Family |
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Links |
Enzyme (activities) ala_decarboxylase
BRENDA (activities) ala_decarboxylase
KEGG (pathways) ala_decarboxylase
PLPMDB (PLP mutants) ala_decarboxylase
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References |
Bai P, Wei K, Wang L, Zhang F, Ruan L, Li H, Wu L, Cheng H
(2019) Identification of a Novel Gene Encoding the Specialized Alanine Decarboxylase in Tea (Camellia sinensis) Plants Molecules 24 E540. Deng WW, Ogita S, Ashihara H
(2010) Distribution and biosynthesis of theanine in Theaceae plants Plant Physiol Biochem 48 70-2. Crocomo, OJ; Fowden L
(1970) Amino acid decarboxylases of higher plants: The formation of ethylamine Phytochemistry 9 537-540. Articles on ala.decarboxylase |
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last changed |
2019/03/22 09:14 |
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