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Literature summary for 4.1.1.1 extracted from

  • Goetz, G.; Iwan, P.; Hauer, B.; Breuer, M.; Pohl, M.
    Continuous production of (R)-phenylacetylcarbinol in an enzyme-membrane reactor using a potent mutant of pyruvate decarboxylase from Zymomonas mobilis (2001), Biotechnol. Bioeng., 74, 317-325.
    View publication on PubMed

Application

Application Comment Organism
synthesis synthesis of (R)-phenylacetylcarbinol from cheap substrates in an aqueous reaction system by W392M mutant PDC, alternative strategy to the current fermentative process free of any unwanted by-product Zymomonas mobilis

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and W392M mutant PDC in Escherichia coli K12 Zymomonas mobilis

Protein Variants

Protein Variants Comment Organism
W392M higher carboligase/(R)-phenylacetylcarbinol-producing activity, more stable and higher resistance towards acetaldehyde than wild-type PDC Zymomonas mobilis

General Stability

General Stability Organism
low stability in the isolated state, less stable than PDC from Zymomonas mobilis Saccharomyces cerevisiae
more stable than PDC from Saccharomyces cerevisiae, stirring deactivates significantly Zymomonas mobilis

Inhibitors

Inhibitors Comment Organism Structure
acetaldehyde inhibits, more resistant than PDC from Zymomonas mobilis, 8 mM, 2h, stable Saccharomyces cerevisiae
acetaldehyde 0.4 mM, inactivates Zymomonas mobilis
benzaldehyde inhibits formation of (R)-1-phenyl-1-hydroxy-propane-2-one Zymomonas mobilis
additional information no product inhibition by (R)-1-phenyl-1-hydroxy-propane-2-one Zymomonas mobilis
PO43-
-
Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetic data, kinetic model Zymomonas mobilis

Organism

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

Reaction

Reaction Comment Organism Reaction ID
a 2-oxo carboxylate = an aldehyde + CO2 catalyzes the carboligation of 2 aldehydes as a side reaction, mechanisms of both reactions Saccharomyces cerevisiae
a 2-oxo carboxylate = an aldehyde + CO2 catalyzes the carboligation of 2 aldehydes as a side reaction, mechanisms of both reactions, thermodynamic data Zymomonas mobilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetaldehyde + acetaldehyde carboligation of 2 aldehydes as a side reaction of PDC Saccharomyces cerevisiae acetoin
-
?
acetaldehyde + acetaldehyde carboligation of 2 aldehydes as a side reaction of PDC Zymomonas mobilis acetoin
-
?
acetaldehyde + benzaldehyde carboligation of 2 aldehydes as a side reaction of PDC, high carboligase activity, more active than PDC from Zymomonas mobilis Saccharomyces cerevisiae (R)-1-phenyl-1-hydroxy-propane-2-one (R)-phenylacetylcarbinol ?
acetaldehyde + benzaldehyde carboligation of 2 aldehydes as a side reaction of PDC, less active than PDC from Saccharomyces cerevisiae Zymomonas mobilis (R)-1-phenyl-1-hydroxy-propane-2-one (R)-phenylacetylcarbinol ?
pyruvate nonoxidative decarboxylation, main reaction Saccharomyces cerevisiae acetaldehyde + CO2
-
?
pyruvate nonoxidative decarboxylation, main reaction Zymomonas mobilis acetaldehyde + CO2
-
?

Synonyms

Synonyms Comment Organism
PDCS.c.
-
Saccharomyces cerevisiae
PDCZ.m.
-
Zymomonas mobilis

Temperature Optimum [°C]

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

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
20 30 only slightly differing catalytic activity in the range, +/-10% relative to 25°C Zymomonas mobilis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
25
-
rapidly inactivated at Saccharomyces cerevisiae
30
-
rapidly inactivated at Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
assay at Saccharomyces cerevisiae
6.5 7 carboligation of acetaldehyde and benzaldehyde, optimal activity in potassium phosphate buffer Zymomonas mobilis