Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Yun, H.; Kim, B.
    Enzymatic production of (R)-phenylacetylcarbinol by pyruvate decarboxylase from Zymomonas mobilis (2008), Biotechnol. Bioprocess Eng., 13, 372-376.
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.1 expressed in Escherichia coli strain BL21 Zymomonas mobilis

Protein Variants

EC Number Protein Variants Comment Organism
4.1.1.1 W329M the carboligase activity of the mutant is 2.8% as high as the decarboxylase activity which is about 10fold higher than the wild type enzyme Zymomonas mobilis

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.1.1 benzaldehyde after a 20 h incubation with 30 mM benzaldehyde, the residual activity is 84% of the initial activity, enzyme stability dramatically decreases in the presence of 200 mM benzaldehyde (27% residual activity after 3 h incubation) Zymomonas mobilis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.1.1 Mg2+ required for activity Zymomonas mobilis

Organism

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.1 benzaldehyde + pyruvate
-
 Zymomonas mobilis (1R)-phenylacetylcarbinol + CO2
-
 ir
4.1.1.1 pyruvate
-
 Zymomonas mobilis acetaldehyde + CO2
-
 ir

Synonyms

EC Number Synonyms Comment Organism
4.1.1.1 PDC
-
 Zymomonas mobilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.1.1 5.5
-
 for decarboxylation Zymomonas mobilis
4.1.1.1 6.5
-
 for carboligation Zymomonas mobilis

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.1 thiamine diphosphate
-
 Zymomonas mobilis