Literature summary for 4.1.1.1 extracted from

Wang, J.; Golbik, R.; Seliger, B.; Spinka, M.; Tittmann, K.; Hubner, G.; Jordan, F.
Consequences of a modified putative substrate-activation site on catalysis by yeast pyruvate decarboxylase (2001), Biochemistry, 40, 1755-1763.

Search for more literature for 4.1.1.1

Activating Compound

Activating Compound	Comment	Organism	Structure
additional information	not activated by the substrate pyruvate	Zymomonas mobilis
Pyruvamide	artificial activator	Saccharomyces cerevisiae
pyruvate	hysteretic substrate activation, Cys-221 binds pyruvate to transmit the information to H-92, E-91, W-412, G-413 and finally to the active center thiamine diphosphate	Saccharomyces cerevisiae

Protein Variants

Protein Variants	Comment	Organism
C221A/C222A	active double mutant without substrate activation, effect of modified substrate-activation site on catalysis, kinetic properties	Saccharomyces cerevisiae
C221S	mutant with abolished activation and reduced Hill coefficient	Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	kinetic data	Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
pyruvate	Saccharomyces cerevisiae	-	acetaldehyde + CO2	-	ir

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	-	-
Zymomonas mobilis	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
wild-type PDC and C221A/C222A double mutant	Saccharomyces cerevisiae

Reaction

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

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
45	50	pH 6, 25°C, wild-type PDC	Saccharomyces cerevisiae
120	-	-	Zymomonas mobilis
515	-	pH 6, 25°C, C221A/C222A double mutant PDC	Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
pyruvate	-	Saccharomyces cerevisiae	acetaldehyde + CO2	-	ir
pyruvate	catalytic mechanism	Saccharomyces cerevisiae	acetaldehyde + CO2	-	ir
pyruvate	H113 is involved in substrate binding and mediates the opening and closing of the active site by ion pairing with the carboxyl group of pyruvate	Zymomonas mobilis	acetaldehyde + CO2	-	?

Synonyms

Synonyms	Comment	Organism
YPDC	-	Saccharomyces cerevisiae
ZmPDC	-	Zymomonas mobilis

Temperature Optimum [°C]

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

Temperature Range [°C]

Temperature Minimum [°C]	Temperature Maximum [°C]	Comment	Organism
4	30	enzyme is 6times more active at 30°C than at 4°C	Saccharomyces cerevisiae

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
2.5	-	pyruvate	pH 6, 4°C, C221A/C222A double mutant PDC	Saccharomyces cerevisiae
10	-	pyruvate	pH 6, 4°C, wild-type PDC	Saccharomyces cerevisiae
15	-	pyruvate	pH 6, 30°C, C221A/C222A double mutant PDC	Saccharomyces cerevisiae
120	-	pyruvate	-	Zymomonas mobilis

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
6	-	assay at	Saccharomyces cerevisiae

Cofactor

Cofactor	Comment	Organism	Structure
thiamine diphosphate	requirement, mode of active site binding	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)