The enzyme has been characterized from bacteria, plants, and fungi. Unlike EC 4.1.1.28, aromatic-L-amino-acid decarboxylase, this enzyme is specific for L-tryptophan.
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SYSTEMATIC NAME
IUBMB Comments
L-tryptophan carboxy-lyase
The enzyme has been characterized from bacteria, plants, and fungi. Unlike EC 4.1.1.28, aromatic-L-amino-acid decarboxylase, this enzyme is specific for L-tryptophan.
enzyme TDC has substrate specificity for Trp, but not for phenolic L-amino acids (Phe and Tyr) and their derivatives, substrate binding site sequence determination
enzyme TDC has substrate specificity for Trp, but not for phenolic L-amino acids (Phe and Tyr) and their derivatives, substrate binding site sequence determination
enzyme TDC has substrate specificity for Trp, but not for phenolic L-amino acids (Phe and Tyr) and their derivatives, substrate binding site sequence determination
the enzyme acts as a decarboxylase that is strictly specific for L-tryptophan and 5-hydroxy-L-tryptophan. No activity of the wild-type enzyme with 1-, 2-, 4-, 5-, 6-, and 7-methyl-L-tryptophan or with L-tyrosine, 3,4-dihydroxy-L-phenylalanine, or L-histidine
the enzyme acts as a decarboxylase that is strictly specific for L-tryptophan and 5-hydroxy-L-tryptophan. No activity of the wild-type enzyme with 1-, 2-, 4-, 5-, 6-, and 7-methyl-L-tryptophan or with L-tyrosine, 3,4-dihydroxy-L-phenylalanine, or L-histidine
the enzyme acts as a decarboxylase that is strictly specific for L-tryptophan and 5-hydroxy-L-tryptophan. No activity of the wild-type enzyme with 1-, 2-, 4-, 5-, 6-, and 7-methyl-L-tryptophan or with L-tyrosine, 3,4-dihydroxy-L-phenylalanine, or L-histidine
plant tryptophan decarboxylase (TDC) converts tryptophan into tryptamine, precursor of indolealkylamine alkaloids. Successive methylation pathway of the tryptamine to N,N,N-trimethyltryptamine produced from the tryptophan decarboxylation, overview
plant tryptophan decarboxylase (TDC) converts tryptophan into tryptamine, precursor of indolealkylamine alkaloids. Successive methylation pathway of the tryptamine to N,N,N-trimethyltryptamine produced from the tryptophan decarboxylation, overview
plant tryptophan decarboxylase (TDC) converts tryptophan into tryptamine, precursor of indolealkylamine alkaloids. Successive methylation pathway of the tryptamine to N,N,N-trimethyltryptamine produced from the tryptophan decarboxylation, overview
site-directed saturation mutagenesis, the mutant shows additional 3,4-dihydroxy-L-phenylalanine (L-DOPA) decarboxylase activity, and G351L shows approximately twelvefold and fivefold increases in Km values for L-tryptophan and 5-hydroxy-L-tryptophan compared to wild-type, as well as increased values for L-tyrosine and L-DOPA (2.44 and 3.4 mM), respectively
the mutation adds L-tyrosine and 3,4-dihydroxy-L-phenylalanine decarboxylase activity while retaining stereospecificity and L-tryptophan decarboxylase activity compared to the wild type enzyme
site-directed saturation mutagenesis, the mutant shows additional 3,4-dihydroxy-L-phenylalanine (L-DOPA) decarboxylase activity, and G351L shows approximately twelvefold and fivefold increases in Km values for L-tryptophan and 5-hydroxy-L-tryptophan compared to wild-type, as well as increased values for L-tyrosine and L-DOPA (2.44 and 3.4 mM), respectively
the mutation adds L-tyrosine and 3,4-dihydroxy-L-phenylalanine decarboxylase activity while retaining stereospecificity and L-tryptophan decarboxylase activity compared to the wild type enzyme
except for G351T, all engineered variants are opened for phenolic substrates compared to wild-type enzyme. Neither of the engineered enzymes turns over L-phenylalanine, L-histidine, or D-amino acids
except for G351T, all engineered variants are opened for phenolic substrates compared to wild-type enzyme. Neither of the engineered enzymes turns over L-phenylalanine, L-histidine, or D-amino acids
except for G351T, all engineered variants are opened for phenolic substrates compared to wild-type enzyme. Neither of the engineered enzymes turns over L-phenylalanine, L-histidine, or D-amino acids
gene tdc, DNA and amino acid sequence determination and analysis, TDC is a homodimer and its polypeptide chain is encoded by a single copy gene without introns, sequence comparisons and phylogenetic tree
Nicotiana tabacum T-201-1 tobacco line transformed with a full-length TDC cDNA gene and expressed under the regulatory control of the cauliflower mosaic virus CaMV 35S promoter
gene tdc, DNA and amino acid sequence determination and analysis, TDC is a homodimer and its polypeptide chain is encoded by a single copy gene without introns, sequence comparisons and phylogenetic tree
gene tdc, DNA and amino acid sequence determination and analysis, TDC is a homodimer and its polypeptide chain is encoded by a single copy gene without introns, sequence comparisons and phylogenetic tree
Nicotiana tabacum T-201-1 tobacco line transformed with a full-length TDC cDNA gene and expressed under the regulatory control of the cauliflower mosaic virus CaMV 35S promoter
Nicotiana tabacum T-201-1 tobacco line transformed with a full-length TDC cDNA gene and expressed under the regulatory control of the cauliflower mosaic virus CaMV 35S promoter
Tryptophan decarboxylase is encoded by two autonomously regulated genes in Camptotheca acuminata which are differentially expressed during development and stress
Increased production of serotonin by suspension and root cultures of Peganum harmala transformed with a tryptophan decarboxylase cDNA clone from Catharanthus roseus