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Literature summary for 4.1.1.1 extracted from

  • Joseph, E.; Wei, W.; Tittmann, K.; Jordan, F.
     Function of a conserved loop of the beta-domain, not involved in thiamin diphosphate binding, in catalysis and substrate activation in yeast pyruvate decarboxylase (2006), Biochemistry, 45, 13517-13527.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
Pyruvamide a substrate activator surrogate, activates, a flexible loop spanning residues 290 to 304 on the beta-domain of the enzyme, not seen in the absence of pyruvamide, occurs in presence of the activator, residues on the loop affect the enzyme activity, conformational equilibrium between the open and closed conformations of the enzyme identified in the pyruvamide-activated structure Saccharomyces cerevisiae

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
D291A site-directed mutagenesis, the mutant shows altered kinetics with highly reduced kcat compared to the wild-type enzyme Saccharomyces cerevisiae
D291N site-directed mutagenesis, the mutant shows altered kinetics with highly reduced activity compared to the wild-type enzyme Saccharomyces cerevisiae
L111A site-directed mutagenesis, the mutant shows 47% of the wild-type kcat Saccharomyces cerevisiae
L111Q site-directed mutagenesis, the mutant shows 73% of the wild-type kcat Saccharomyces cerevisiae
L111V site-directed mutagenesis, the mutant shows 21% of the wild-type kcat Saccharomyces cerevisiae
additional information construction of mutant pdc-803 with a S296DELTAF297DELTA deletion, the mutant shows highly reduced activity compared to the wild-type enzyme Saccharomyces cerevisiae
N293A site-directed mutagenesis, the mutant shows altered kinetics with highly reduced kcat compared to the wild-type enzyme Saccharomyces cerevisiae
S298A site-directed mutagenesis, the mutant shows altered kinetics with highly reduced kcat compared to the wild-type enzyme Saccharomyces cerevisiae
S300A site-directed mutagenesis, the mutant shows altered kinetics with slightly reduced kcat compared to the wild-type enzyme Saccharomyces cerevisiae
T294A site-directed mutagenesis, the mutant shows altered kinetics with highly reduced kcat compared to the wild-type enzyme Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information pre-steady-state and steady-state kinetics of recombinant wild-type and mutant enzymes, overview Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3) Saccharomyces cerevisiae

Reaction

Reaction Comment Organism Reaction ID
a 2-oxo carboxylate = an aldehyde + CO2 reaction mechanism, overview Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information in the pyruvamide-activated enzyme form, the flexible loop located on the beta-domain can transfer information to the active center thiamine diphosphate located at the interface of the alpha and gamma domains, overview Saccharomyces cerevisiae ?
-
?

Subunits

Subunits Comment Organism
More conformational equilibrium between the open and closed conformations of the enzyme identified in the pyruvamide-activated structure Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
pyruvamide-activated yeast pyruvate decarboxylase
-
Saccharomyces cerevisiae
YPDC
-
Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
31
-
assay at Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.6
-
wild-type enzyme Saccharomyces cerevisiae

pH Range

pH Minimum pH Maximum Comment Organism
5.1 7.5
-
Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate bound to the active site located at the interface of the alpha and gamma domains Saccharomyces cerevisiae