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Literature summary for 4.1.1.74 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
Search for more literature for 4.1.1.74

Cloned(Commentary)

Cloned (Comment) Organism
-
 Enterobacter cloacae

General Stability

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

Inhibitors

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

KM Value [mM]

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

Metals/Ions

Metals/Ions Comment Organism Structure
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]

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

Natural Substrates/ Products (Substrates)

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

Organic Solvent Stability

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

Organism

Organism UniProt Comment Textmining
Enterobacter cloacae
-
-
-

Purification (Commentary)

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

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Subunits

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

Temperature Stability [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.4 6.6
-
 Enterobacter cloacae

Cofactor

Cofactor Comment Organism Structure
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