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Literature summary extracted from

  • Candy, J.M.; Duggleby, R.G.
    Structure and properties of pyruvate decarboxylase and site-directed mutagenesis of the Zymomonas mobilis enzyme (1998), Biochim. Biophys. Acta, 1385, 323-338.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
4.1.1.1 D440E active, but unlike the wild type enzyme, exhibits a lag phase in product formation which can be reduced by preincubation with 5 mM thiamine diphosphate. Mutant N467D shows decreased affinity for thiamine diphosphate Zymomonas mobilis

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.1.1 3-hydroxypyruvate
-
Zymomonas mobilis
4.1.1.1 phosphate
-
Ipomoea batatas
4.1.1.1 phosphate
-
Sarcina ventriculi
4.1.1.1 phosphate
-
Zea mays
4.1.1.1 phosphate
-
Zymomonas mobilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.1 additional information
-
additional information
-
Zymomonas mobilis
4.1.1.1 0.5
-
pyruvate
-
Zea mays
4.1.1.1 0.5
-
pyruvate
-
Zymomonas mobilis
4.1.1.1 0.52
-
pyruvate wild type enzyme and mutant enzyme E449D Zymomonas mobilis
4.1.1.1 0.71
-
pyruvate mutant enzyme H114Q Zymomonas mobilis
4.1.1.1 0.86
-
pyruvate mutant enzyme W487L Zymomonas mobilis
4.1.1.1 0.95
-
pyruvate mutant enzyme D440E and mutant enzyme N467D Zymomonas mobilis
4.1.1.1 0.97
-
pyruvate mutant enzyme F496I Zymomonas mobilis
4.1.1.1 1.06
-
pyruvate mutant enzyme F496H Zymomonas mobilis
4.1.1.1 1.33
-
pyruvate mutant enzyme V111A Zymomonas mobilis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.1.1 Mg2+
-
Saccharomyces cerevisiae
4.1.1.1 Mg2+
-
Zea mays
4.1.1.1 Mg2+
-
Zymomonas mobilis
4.1.1.1 Mg2+
-
Ipomoea batatas
4.1.1.1 Mg2+
-
Saccharomyces uvarum
4.1.1.1 additional information
-
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 Pisum sativum the enzyme catalyzes the penultimate step in alcohol fermentation ?
-
?
4.1.1.1 additional information Zymomonas mobilis the enzyme catalyzes the penultimate step in alcohol fermentation ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.1 Acetobacter sp.
-
-
-
4.1.1.1 Aspergillus sp.
-
-
-
4.1.1.1 Canavalia ensiformis
-
-
-
4.1.1.1 Citrus sp.
-
-
-
4.1.1.1 Clostridium botulinum
-
-
-
4.1.1.1 Erwinia amylovora
-
-
-
4.1.1.1 Hanseniaspora uvarum
-
-
-
4.1.1.1 Ipomoea batatas
-
-
-
4.1.1.1 Kluyveromyces sp.
-
-
-
4.1.1.1 Neurospora crassa
-
-
-
4.1.1.1 Pastinaca sativa
-
-
-
4.1.1.1 Pisum sativum
-
cv. Miko
-
4.1.1.1 Saccharomyces cerevisiae
-
-
-
4.1.1.1 Saccharomyces pastorianus
-
-
-
4.1.1.1 Saccharomyces uvarum
-
-
-
4.1.1.1 Sarcina ventriculi
-
-
-
4.1.1.1 Schizosaccharomyces pombe
-
-
-
4.1.1.1 Zea mays
-
-
-
4.1.1.1 Zymomonas mobilis
-
wild type and mutant enzymes E50D, E50Q, V111A, H113Q, H114Q, D440N, D440T, D440G, D440E, E449D, N467Q, N467D, W487L, F496I, F496H
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.1 2-Oxobutanoate
-
Zymomonas mobilis ?
-
?
4.1.1.1 2-Oxopentanoate
-
Zymomonas mobilis ?
-
?
4.1.1.1 3-Fluoropyruvate decarboxylation is followed by release of F- Saccharomyces cerevisiae acetate + F- + CO2
-
?
4.1.1.1 3-Fluoropyruvate decarboxylation is followed by release of F- Zymomonas mobilis acetate + F- + CO2
-
?
4.1.1.1 3-Hydroxypyruvate
-
Zymomonas mobilis Glycolaldehyde + CO2
-
?
4.1.1.1 additional information the enzyme catalyzes the penultimate step in alcohol fermentation Pisum sativum ?
-
?
4.1.1.1 additional information the enzyme catalyzes the penultimate step in alcohol fermentation Zymomonas mobilis ?
-
?
4.1.1.1 pyruvate
-
Saccharomyces pastorianus acetaldehyde + CO2
-
?
4.1.1.1 pyruvate
-
Saccharomyces cerevisiae acetaldehyde + CO2
-
?
4.1.1.1 pyruvate
-
Neurospora crassa acetaldehyde + CO2
-
?
4.1.1.1 pyruvate
-
Pisum sativum acetaldehyde + CO2
-
?
4.1.1.1 pyruvate
-
Zea mays acetaldehyde + CO2
-
?
4.1.1.1 pyruvate
-
Schizosaccharomyces pombe acetaldehyde + CO2
-
?
4.1.1.1 pyruvate
-
Zymomonas mobilis acetaldehyde + CO2
-
?
4.1.1.1 pyruvate
-
Citrus sp. acetaldehyde + CO2
-
?
4.1.1.1 pyruvate
-
Acetobacter sp. acetaldehyde + CO2
-
?
4.1.1.1 pyruvate
-
Aspergillus sp. acetaldehyde + CO2
-
?
4.1.1.1 pyruvate
-
Canavalia ensiformis acetaldehyde + CO2
-
?
4.1.1.1 pyruvate
-
Clostridium botulinum acetaldehyde + CO2
-
?
4.1.1.1 pyruvate
-
Ipomoea batatas acetaldehyde + CO2
-
?
4.1.1.1 pyruvate
-
Saccharomyces uvarum acetaldehyde + CO2
-
?
4.1.1.1 pyruvate
-
Pastinaca sativa acetaldehyde + CO2
-
?
4.1.1.1 pyruvate
-
Kluyveromyces sp. acetaldehyde + CO2
-
?
4.1.1.1 pyruvate
-
Hanseniaspora uvarum acetaldehyde + CO2
-
?
4.1.1.1 pyruvate
-
Sarcina ventriculi acetaldehyde + CO2
-
?
4.1.1.1 pyruvate
-
Erwinia amylovora acetaldehyde + CO2
-
?

Subunits

EC Number Subunits Comment Organism
4.1.1.1 More
-
Saccharomyces pastorianus
4.1.1.1 More
-
Saccharomyces cerevisiae
4.1.1.1 More
-
Neurospora crassa
4.1.1.1 More
-
Zea mays
4.1.1.1 More
-
Sarcina ventriculi
4.1.1.1 More phosphate stabilizes the tetramer by shifting the dimer-tetramer equilibrium to higher pH values, without altering the conformation of the tetramer Zymomonas mobilis