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Literature summary for 4.1.1.1 extracted from

  • Miczka, G.; Vernau, J.; Kula, M.R.; Hoffmann, B.; Schomburg, D.
    Purification and primary structure of pyruvate decarboxylase from Zymomonas mobilis (1992), Biotechnol. Appl. Biochem., 15, 192-206.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Zymomonas mobilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.38
-
pyruvate
-
Zymomonas mobilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
59000
-
4 * 59000, SDS-PAGE Zymomonas mobilis
60746
-
4 * 60746, SDS-PAGE Zymomonas mobilis
209000
-
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 glycolytic pathway to ethanol ?
-
?

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
additional information
-
-
Zymomonas mobilis

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
tetramer 4 * 59000, SDS-PAGE Zymomonas mobilis
tetramer 4 * 60746, SDS-PAGE Zymomonas mobilis