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Literature summary for 4.1.1.105 extracted from

  • Kalb, D.; Gressler, J.; Hoffmeister, D.
    Active-site engineering expands the substrate profile of the basidiomycete L-tryptophan decarboxylase CsTDC (2016), ChemBioChem, 17, 132-136 .
    View publication on PubMed
Search for more literature for 4.1.1.105

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli KRX cells Gelatoporia subvermispora
gene tdc, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain KRX Gelatoporia subvermispora

Protein Variants

Protein Variants Comment Organism
G351A site-directed saturation mutagenesis, the mutant shows additional activity with phenolic substrates Gelatoporia subvermispora
G351I site-directed saturation mutagenesis, the mutant shows additional activity with phenolic substrates Gelatoporia subvermispora
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
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
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
G351S site-directed saturation mutagenesis, the mutant shows additional L-tyrosine decarboxylase activity while retaining stereospecificity and L-tryptophan decarboxylase activity Gelatoporia subvermispora
G351V site-directed saturation mutagenesis, the mutant shows additional L-tyrosine decarboxylase activity while retaining stereospecificity and L-tryptophan decarboxylase activity Gelatoporia subvermispora
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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten kinetics Gelatoporia subvermispora
0.16
-
 L-tryptophan recombinant wild-type enzyme, pH 7.5, 37°C Gelatoporia subvermispora
0.16
-
 L-tryptophan wild type enzyme, at pH 7.5 and 37°C Gelatoporia subvermispora
0.29
-
 L-tryptophan mutant enzyme G351S, at pH 7.5 and 37°C Gelatoporia subvermispora
0.32
-
 5-hydroxy-L-tryptophan recombinant wild-type enzyme, pH 7.5, 37°C Gelatoporia subvermispora
0.32
-
 5-hydroxy-L-tryptophan wild type enzyme, at pH 7.5 and 37°C Gelatoporia subvermispora
0.35
-
 5-hydroxy-L-tryptophan mutant enzyme G351S, at pH 7.5 and 37°C Gelatoporia subvermispora
1.72
-
 5-hydroxy-L-tryptophan mutant enzyme G351L, at pH 7.5 and 37°C Gelatoporia subvermispora
1.72
-
 5-hydroxy-L-tryptophan recombinant mutant G351L, pH 7.5, 37°C Gelatoporia subvermispora
1.94
-
 L-tryptophan mutant enzyme G351L, at pH 7.5 and 37°C Gelatoporia subvermispora
1.94
-
 L-tryptophan recombinant mutant G351L, pH 7.5, 37°C Gelatoporia subvermispora

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5-hydroxy-L-tryptophan Gelatoporia subvermispora
-
 5-hydroxytryptamine + CO2
-
 ?
5-hydroxy-L-tryptophan Gelatoporia subvermispora B
-
 5-hydroxytryptamine + CO2
-
 ?
L-tryptophan Gelatoporia subvermispora
-
 tryptamine + CO2
-
 ?
L-tryptophan Gelatoporia subvermispora B
-
 tryptamine + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Gelatoporia subvermispora
-
-
-
Gelatoporia subvermispora M2RF26
-
-
Gelatoporia subvermispora B M2RF26
-
-

Purification (Commentary)

Purification (Comment) Organism
His-Trap column chromatography and Superdex 200 gel filtration Gelatoporia subvermispora

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5-hydroxy-L-tryptophan
-
 Gelatoporia subvermispora 5-hydroxytryptamine + CO2
-
 ?
5-hydroxy-L-tryptophan
-
 Gelatoporia subvermispora B 5-hydroxytryptamine + CO2
-
 ?
L-tryptophan
-
 Gelatoporia subvermispora tryptamine + CO2
-
 ?
L-tryptophan
-
 Gelatoporia subvermispora B tryptamine + CO2
-
 ?
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 ?
-
 ?
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 ?
-
 ?
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 ?
-
 ?

Subunits

Subunits Comment Organism
? x * 57600, calculated from amino acid sequence Gelatoporia subvermispora

Synonyms

Synonyms Comment Organism
(5-hydroxy-)L-tryptophan decarboxylase
-
 Gelatoporia subvermispora
CsTDC
-
 Gelatoporia subvermispora
L-Tryptophan decarboxylase
-
 Gelatoporia subvermispora
TDC
-
 Gelatoporia subvermispora

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37 45
-
 Gelatoporia subvermispora

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.16
-
 5-hydroxy-L-tryptophan mutant enzyme G351S, at pH 7.5 and 37°C Gelatoporia subvermispora
0.17
-
 5-hydroxy-L-tryptophan recombinant wild-type enzyme, pH 7.5, 37°C Gelatoporia subvermispora
0.17
-
 5-hydroxy-L-tryptophan wild type enzyme, at pH 7.5 and 37°C Gelatoporia subvermispora
0.26
-
 5-hydroxy-L-tryptophan mutant enzyme G351L, at pH 7.5 and 37°C Gelatoporia subvermispora
0.82
-
 L-tryptophan mutant enzyme G351S, at pH 7.5 and 37°C Gelatoporia subvermispora
1.21
-
 L-tryptophan recombinant wild-type enzyme, pH 7.5, 37°C Gelatoporia subvermispora
1.21
-
 L-tryptophan wild type enzyme, at pH 7.5 and 37°C Gelatoporia subvermispora
1.79
-
 L-tryptophan mutant enzyme G351L, at pH 7.5 and 37°C Gelatoporia subvermispora

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
 Gelatoporia subvermispora

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
 Gelatoporia subvermispora

General Information

General Information Comment Organism
additional information residue G351 is the key catalytic residue of the enzyme Gelatoporia subvermispora