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Literature summary for 4.1.1.105 extracted from

  • Bueki, K.; Vinh, D.; Horvath, I.
    Partial purification and some properties of tryptophan decarboxylase from a Bacillus strain (1985), Acta Microbiol. Hung., 32, 65-73 .
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.3
-
L-tryptophan at pH 7.0 and 37Ā°C Bacillus sp. (in: Bacteria)

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
150000
-
gel filtration Bacillus sp. (in: Bacteria)

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-tryptophan Bacillus sp. (in: Bacteria)
-
tryptamine + CO2
-
?

Organism

Organism UniProt Comment Textmining
Bacillus sp. (in: Bacteria)
-
-
-

Purification (Commentary)

Purification (Comment) Organism
DEAE-cellulose column chromatography, and Superdex 200 gel filtration Bacillus sp. (in: Bacteria)

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-tryptophan
-
Bacillus sp. (in: Bacteria) tryptamine + CO2
-
?

Synonyms

Synonyms Comment Organism
Tryptophan decarboxylase
-
Bacillus sp. (in: Bacteria)

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
Bacillus sp. (in: Bacteria)

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate required for maximum activity Bacillus sp. (in: Bacteria)