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Literature summary for 4.1.1.1 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
Search for more literature for 4.1.1.1

KM Value [mM]

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

Metals/Ions

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Zymomonas mobilis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Zymomonas mobilis

Specific Activity [micromol/min/mg]

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

Storage Stability

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

Substrates and Products (Substrate)

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

Subunits

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