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Literature summary extracted from

  • Bringer-Meyer, S.; Schimz, K.L.; Sahm, H.
    Pyruvate decarboxylase from Zymomonas mobilis. Isolation and partial characterization (1986), Arch. Microbiol., 146, 105-110.
No PubMed abstract available

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.1 0.4
-
 pyruvate pH 6.0 Zymomonas mobilis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.1.1 Mg2+ Km: 0.024 mM Zymomonas mobilis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.1.1 56500
-
 4 * 56500, SDS-PAGE Zymomonas mobilis
4.1.1.1 200000
-
 gel filtration Zymomonas mobilis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.1.1 additional information Zymomonas mobilis key enzyme in ethanol formation ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.1 Zymomonas mobilis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.1
-
 Zymomonas mobilis

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.1.1.1 181
-
-
 Zymomonas mobilis

Storage Stability

EC Number Storage Stability Organism
4.1.1.1 -20°C, 50% v/v glycerol, negligible loss of activity Zymomonas mobilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.1 additional information key enzyme in ethanol formation Zymomonas mobilis ?
-
 ?
4.1.1.1 pyruvate
-
 Zymomonas mobilis acetaldehyde + CO2
-
 ?

Subunits

EC Number Subunits Comment Organism
4.1.1.1 tetramer 4 * 56500, SDS-PAGE Zymomonas mobilis