EC Number | Cloned (Comment) | Organism |
---|---|---|
4.1.1.105 | expressed in Escherichia coli KRX cells | Gelatoporia subvermispora |
4.1.1.105 | gene tdc, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain KRX | Gelatoporia subvermispora |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
4.1.1.105 | G351A | site-directed saturation mutagenesis, the mutant shows additional activity with phenolic substrates | Gelatoporia subvermispora |
4.1.1.105 | G351I | site-directed saturation mutagenesis, the mutant shows additional activity with phenolic substrates | Gelatoporia subvermispora |
4.1.1.105 | G351L | 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 | Gelatoporia subvermispora |
4.1.1.105 | G351L | 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 | Gelatoporia subvermispora |
4.1.1.105 | G351S | 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 | Gelatoporia subvermispora |
4.1.1.105 | G351S | site-directed saturation mutagenesis, the mutant shows additional L-tyrosine decarboxylase activity while retaining stereospecificity and L-tryptophan decarboxylase activity | Gelatoporia subvermispora |
4.1.1.105 | G351V | site-directed saturation mutagenesis, the mutant shows additional L-tyrosine decarboxylase activity while retaining stereospecificity and L-tryptophan decarboxylase activity | Gelatoporia subvermispora |
4.1.1.105 | additional information | 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 | Gelatoporia subvermispora |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
4.1.1.105 | additional information | - |
additional information | Michaelis-Menten kinetics | Gelatoporia subvermispora | |
4.1.1.105 | 0.16 | - |
L-tryptophan | recombinant wild-type enzyme, pH 7.5, 37°C | Gelatoporia subvermispora | |
4.1.1.105 | 0.16 | - |
L-tryptophan | wild type enzyme, at pH 7.5 and 37°C | Gelatoporia subvermispora | |
4.1.1.105 | 0.29 | - |
L-tryptophan | mutant enzyme G351S, at pH 7.5 and 37°C | Gelatoporia subvermispora | |
4.1.1.105 | 0.32 | - |
5-hydroxy-L-tryptophan | recombinant wild-type enzyme, pH 7.5, 37°C | Gelatoporia subvermispora | |
4.1.1.105 | 0.32 | - |
5-hydroxy-L-tryptophan | wild type enzyme, at pH 7.5 and 37°C | Gelatoporia subvermispora | |
4.1.1.105 | 0.35 | - |
5-hydroxy-L-tryptophan | mutant enzyme G351S, at pH 7.5 and 37°C | Gelatoporia subvermispora | |
4.1.1.105 | 1.72 | - |
5-hydroxy-L-tryptophan | mutant enzyme G351L, at pH 7.5 and 37°C | Gelatoporia subvermispora | |
4.1.1.105 | 1.72 | - |
5-hydroxy-L-tryptophan | recombinant mutant G351L, pH 7.5, 37°C | Gelatoporia subvermispora | |
4.1.1.105 | 1.94 | - |
L-tryptophan | mutant enzyme G351L, at pH 7.5 and 37°C | Gelatoporia subvermispora | |
4.1.1.105 | 1.94 | - |
L-tryptophan | recombinant mutant G351L, pH 7.5, 37°C | Gelatoporia subvermispora |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.1.1.105 | 5-hydroxy-L-tryptophan | Gelatoporia subvermispora | - |
5-hydroxytryptamine + CO2 | - |
? | |
4.1.1.105 | 5-hydroxy-L-tryptophan | Gelatoporia subvermispora B | - |
5-hydroxytryptamine + CO2 | - |
? | |
4.1.1.105 | L-tryptophan | Gelatoporia subvermispora | - |
tryptamine + CO2 | - |
? | |
4.1.1.105 | L-tryptophan | Gelatoporia subvermispora B | - |
tryptamine + CO2 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.1.1.105 | Gelatoporia subvermispora | - |
- |
- |
4.1.1.105 | Gelatoporia subvermispora | M2RF26 | - |
- |
4.1.1.105 | Gelatoporia subvermispora B | M2RF26 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
4.1.1.105 | His-Trap column chromatography and Superdex 200 gel filtration | Gelatoporia subvermispora |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.1.1.105 | 5-hydroxy-L-tryptophan | - |
Gelatoporia subvermispora | 5-hydroxytryptamine + CO2 | - |
? | |
4.1.1.105 | 5-hydroxy-L-tryptophan | - |
Gelatoporia subvermispora B | 5-hydroxytryptamine + CO2 | - |
? | |
4.1.1.105 | L-tryptophan | - |
Gelatoporia subvermispora | tryptamine + CO2 | - |
? | |
4.1.1.105 | L-tryptophan | - |
Gelatoporia subvermispora B | tryptamine + CO2 | - |
? | |
4.1.1.105 | additional information | the enzyme does not accept L-tyrosine, L-phenylalanine, L-DOPA, or L-histidine, nor does any of the D-configured amino acids lead to a product | Gelatoporia subvermispora | ? | - |
? | |
4.1.1.105 | additional information | 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 | Gelatoporia subvermispora | ? | - |
? | |
4.1.1.105 | additional information | 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 | Gelatoporia subvermispora B | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
4.1.1.105 | ? | x * 57600, calculated from amino acid sequence | Gelatoporia subvermispora |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
4.1.1.105 | (5-hydroxy-)L-tryptophan decarboxylase | - |
Gelatoporia subvermispora |
4.1.1.105 | CsTDC | - |
Gelatoporia subvermispora |
4.1.1.105 | L-Tryptophan decarboxylase | - |
Gelatoporia subvermispora |
4.1.1.105 | TDC | - |
Gelatoporia subvermispora |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
4.1.1.105 | 37 | 45 | - |
Gelatoporia subvermispora |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
4.1.1.105 | 0.16 | - |
5-hydroxy-L-tryptophan | mutant enzyme G351S, at pH 7.5 and 37°C | Gelatoporia subvermispora | |
4.1.1.105 | 0.17 | - |
5-hydroxy-L-tryptophan | recombinant wild-type enzyme, pH 7.5, 37°C | Gelatoporia subvermispora | |
4.1.1.105 | 0.17 | - |
5-hydroxy-L-tryptophan | wild type enzyme, at pH 7.5 and 37°C | Gelatoporia subvermispora | |
4.1.1.105 | 0.26 | - |
5-hydroxy-L-tryptophan | mutant enzyme G351L, at pH 7.5 and 37°C | Gelatoporia subvermispora | |
4.1.1.105 | 0.82 | - |
L-tryptophan | mutant enzyme G351S, at pH 7.5 and 37°C | Gelatoporia subvermispora | |
4.1.1.105 | 1.21 | - |
L-tryptophan | recombinant wild-type enzyme, pH 7.5, 37°C | Gelatoporia subvermispora | |
4.1.1.105 | 1.21 | - |
L-tryptophan | wild type enzyme, at pH 7.5 and 37°C | Gelatoporia subvermispora | |
4.1.1.105 | 1.79 | - |
L-tryptophan | mutant enzyme G351L, at pH 7.5 and 37°C | Gelatoporia subvermispora |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
4.1.1.105 | 7.5 | - |
- |
Gelatoporia subvermispora |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
4.1.1.105 | pyridoxal 5'-phosphate | - |
Gelatoporia subvermispora |
EC Number | General Information | Comment | Organism |
---|---|---|---|
4.1.1.105 | additional information | residue G351 is the key catalytic residue of the enzyme | Gelatoporia subvermispora |