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Literature summary extracted from

  • Koga, J.; Adachi, T.; Hidaka, H.
    Purification and characterization of indolepyruvate decarboxylase: A novel enzyme for indole-3-acetic acid biosynthesis in Enterobacter cloacae (1992), J. Biol. Chem., 267, 15823-15828.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.74
-
 Enterobacter cloacae

General Stability

EC Number General Stability Organism
4.1.1.74 less stable at a high potassium phosphate concentration Enterobacter cloacae
4.1.1.74 slightly stabilized in presence of 5 mM MgCl2 Enterobacter cloacae
4.1.1.74 stabilized by addition of 1 mM thiamine diphosphate Enterobacter cloacae

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.1.74 2-oxoglutaric acid
-
 Enterobacter cloacae
4.1.1.74 3-phenylpyruvic acid competitive against indole-3-acetic acid Enterobacter cloacae
4.1.1.74 Pyruvic acid
-
 Enterobacter cloacae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.74 0.015
-
 3-(Indol-3-yl)pyruvate
-
 Enterobacter cloacae
4.1.1.74 2.5
-
 Pyruvic acid
-
 Enterobacter cloacae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.1.74 Mg2+ 5 mM, 10fold increase in activity. 39fold increase in activity in presence of 0.1 mM thiamine diphosphate and 5 mM Mg2+. One of the roles of Mg2+ is to facilitate the binding of thiamin diphosphate to the enzyme by formation of a thiamine diphosphate complex Enterobacter cloacae

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.1.74 60000
-
 4 * 60000, SDS-PAGE Enterobacter cloacae
4.1.1.74 240000
-
 gel filtration Enterobacter cloacae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.1.74 3-(Indol-3-yl)pyruvate Enterobacter cloacae key enzyme for indole-3-acetic acid biosynthesis ?
-
 ?

Organic Solvent Stability

EC Number Organic Solvent Comment Organism
4.1.1.74 Ethanol rather stable in ethanol Enterobacter cloacae
4.1.1.74 Ethyl acetate rather stable in ethyl acetate Enterobacter cloacae

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.74 Enterobacter cloacae
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.74 recombinant enzyme from Escherichia coli cells Enterobacter cloacae

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.1.1.74 additional information
-
-
 Enterobacter cloacae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.74 3-(Indol-3-yl)pyruvate
-
 Enterobacter cloacae Indole-3-acetaldehyde + CO2
-
 ?
4.1.1.74 3-(Indol-3-yl)pyruvate key enzyme for indole-3-acetic acid biosynthesis Enterobacter cloacae ?
-
 ?
4.1.1.74 pyruvic acid decarboxylation at 19% of the indole-3-acetic acid decarboxylation Enterobacter cloacae acetaldehyde + CO2
-
 ?

Subunits

EC Number Subunits Comment Organism
4.1.1.74 tetramer 4 * 60000, SDS-PAGE Enterobacter cloacae

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.1.1.74 30
-
 24 h, in presence of 1 mM thiamine diphosphate and 5 mM MgCl2, stable Enterobacter cloacae
4.1.1.74 50
-
 30 min, in presence of 1 mM thiamine diphosphate and 5 mM MgCl2, stable Enterobacter cloacae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.1.74 6.4 6.6
-
 Enterobacter cloacae

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.74 thiamine diphosphate 0.1 mM, 8fold increase in activity. 39fold increase in activity in presence of 0.1 mM thiamine diphosphate and 5 mM Mg2+ Enterobacter cloacae