Literature summary for 4.1.1.1 extracted from

Kutter, S.; Weiss, M.S.; Wille, G.; Golbik, R.; Spinka, M.; Koenig, S.
Covalently bound substrate at the regulatory site of yeast pyruvate decarboxylases triggers allosteric enzyme activation (2009), J. Biol. Chem., 284, 12136-12144.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging drop vapor diffusion method, using 18 mM citrate/2 mM MES, pH 6.3, 2 mM dithiothreitol, 2 mM thiamine diphosphate, 2 mM MgSO4, 22.5% (w/v) PEG 2000/PEG 6000 (1:1 ratio)	Saccharomyces cerevisiae
hanging drop vapor diffusion method, using 20 mM citrate buffer, pH 6.1, 1 mM dithiothreitol, 5 mM thiamine diphosphate, 5 mM MgSO4, 20% (w/v) PEG 2000/PEG 6000 (1:1 ratio)	Kluyveromyces lactis

Protein Variants

Protein Variants	Comment	Organism
D28A	the mutant is almost catalytically inactive	Kluyveromyces lactis
D28A	the mutant is almost catalytically inactive	Saccharomyces cerevisiae
E477Q	the mutant is almost catalytically inactive	Kluyveromyces lactis
E477Q	the mutant is almost catalytically inactive	Saccharomyces cerevisiae

Organism

Organism	UniProt	Comment	Textmining
Kluyveromyces lactis	-	-	-
Saccharomyces cerevisiae	P06169	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Kluyveromyces lactis
-	Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
pyruvate	-	Kluyveromyces lactis	acetaldehyde + CO2	-	?
pyruvate	-	Saccharomyces cerevisiae	acetaldehyde + CO2	-	?

Synonyms

Synonyms	Comment	Organism
PDC	-	Kluyveromyces lactis
PDC	-	Saccharomyces cerevisiae

Cofactor

Cofactor	Comment	Organism	Structure
thiamine diphosphate	-	Kluyveromyces lactis
thiamine diphosphate	-	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)