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Literature summary extracted from

  • Chang, A.K.; Nixon, P.F.; Duggleby, R.G.
    Effects of deletions at the carboxyl terminus of Zymomonas mobilis pyruvate decarboxylase on the kinetic properties and substrate specificity (2000), Biochemistry, 39, 9430-9437.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.1 expression of wild-type PDC and C-terminal deletion mutants in Escherichia coli Zymomonas mobilis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.1.1 crystal structure Zymomonas mobilis

Protein Variants

EC Number Protein Variants Comment Organism
4.1.1.1 additional information engineering of 15 variants of PDC with several deletions at the C-terminus, properties of the mutants, kinetic data 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 values for several C-terminal deletion mutants, kinetic model of the catalytic cycle Zymomonas mobilis
4.1.1.1 0.68
-
 pyruvate 30°C, wild-type PDC Zymomonas mobilis
4.1.1.1 2.86
-
 2-Ketobutyrate 30°C, wild-type PDC Zymomonas mobilis
4.1.1.1 12.9
-
 2-ketovalerate 30°C, wild-type PDC Zymomonas mobilis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.1.1 Mg2+ cofactor, activates Zymomonas mobilis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.1.1 60800
-
 4 * 60800, wild-type PDC, SDS-PAGE Zymomonas mobilis
4.1.1.1 200000
-
 about, wild-type PDC, gel filtration 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 pyruvate Zymomonas mobilis
-
 acetaldehyde + CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.1 Zymomonas mobilis P06672
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.1 5 C-terminal deletion mutants Zymomonas mobilis

Reaction

EC Number Reaction Comment Organism Reaction ID
4.1.1.1 a 2-oxo carboxylate = an aldehyde + CO2 catalytic mechanism Zymomonas mobilis
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.1.1.1 additional information
-
-
 Zymomonas mobilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.1 2-ketobutyrate lower activity than with pyruvate Zymomonas mobilis ?
-
 ?
4.1.1.1 2-ketovalerate lower activity than with pyruvate Zymomonas mobilis ?
-
 ?
4.1.1.1 pyruvate
-
 Zymomonas mobilis acetaldehyde + CO2
-
 ?
4.1.1.1 pyruvate C-terminal region occludes the active site, enzyme structure, catalytic cycle, active site closure is required for decarboxylation Zymomonas mobilis acetaldehyde + CO2
-
 ?

Subunits

EC Number Subunits Comment Organism
4.1.1.1 homotetramer 4 * 60800, wild-type PDC, SDS-PAGE Zymomonas mobilis

Synonyms

EC Number Synonyms Comment Organism
4.1.1.1 PDC
-
 Zymomonas mobilis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.1.1 30
-
 assay at Zymomonas mobilis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.1.1.1 additional information
-
 additional information values for several C-terminal deletion mutants Zymomonas mobilis
4.1.1.1 9
-
 2-Ketobutyrate 30°C, wild-type PDC Zymomonas mobilis
4.1.1.1 13.7
-
 2-ketovalerate 30°C, wild-type PDC Zymomonas mobilis
4.1.1.1 61.4
-
 2-Ketobutyrate 30°C, wild-type PDC Zymomonas mobilis
4.1.1.1 113
-
 pyruvate 30°C, wild-type PDC Zymomonas mobilis

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.1 thiamine diphosphate cofactor activation Zymomonas mobilis