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Literature summary for 1.2.4.1 extracted from

  • Kaczowka, S.J.; Reuter, C.J.; Talarico, L.A.; Maupin-Furlow, J.A.
    Recombinant production of Zymomonas mobilis pyruvate decarboxylase in the haloarchaeon Haloferax volcanii (2005), Archaea, 1, 327-334.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
biotechnology active expression of enzyme from non-halophilic Zymomonas mobilis in the haloarchaeon Haloferax volcanii with no difference in the secondary structure. Post-transcriptional mechanisms in the stationary phase appear to limit the amount of recombinant protein expressed Zymomonas mobilis

Inhibitors

Inhibitors Comment Organism Structure
KCl at 2 M, 50% residual activity of enzyme expressed in Escherichia coli Zymomonas mobilis
NaCl at 2 M, 50% residual activity of enzyme expressed in Escherichia coli Zymomonas mobilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
60000
-
4 * 60000, SDS-PAGE Zymomonas mobilis
240000
-
gel filtration, recombinant protein from Escherichia coli and from Haloferax volcanii Zymomonas mobilis

Organism

Organism UniProt Comment Textmining
Zymomonas mobilis
-
recombinant expression in Haloferax volcanii
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme both expressed in Escherichia coli and Haloferax volcanii Zymomonas mobilis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
55
-
recombinant enzyme from Haloferax volcanii Zymomonas mobilis
91
-
recombinant enzyme from Escherichia coli Zymomonas mobilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pyruvate + CoA + NAD+
-
Zymomonas mobilis acetyl-CoA + CO2 + NADH
-
?

Subunits

Subunits Comment Organism
tetramer 4 * 60000, SDS-PAGE Zymomonas mobilis

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Zymomonas mobilis