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Literature summary for 4.1.1.1 extracted from

  • Neale, A.D.; Scopes, R.K.; Wettenhall, R.E.H.; Hoogenraad, N.J.
    Pyruvate decarboxylase of Zymomonas mobilis: isolation, properties, and genetic expression in Escherichia coli (1987), J. Bacteriol., 169, 1024-1028.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.1.1.1

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Zymomonas mobilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.3
-
 pyruvate
-
 Zymomonas mobilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
59000
-
 4 * 59000, SDS-PAGE Zymomonas mobilis
240000
-
 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

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 * 59000, SDS-PAGE Zymomonas mobilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6 6.5
-
 Zymomonas mobilis

pH Range

pH Minimum pH Maximum Comment Organism
4.6 8 pH 4.6: about 35% of maximal activity, pH 8.0: about 70% of maximal activity Zymomonas mobilis