Abstract
Pyruvate decarboxylases (E.C. 4.1.1.1) from various organisms have been studied for many years, mainly with respect to the mechanism of the non-oxidative decarboxylation reaction. Although the C−C-bond-forming properties of these enzymes are known and have been applied for many years in biotransformations for the synthesis of chiral α-hydroxy ketones, only little is known about the factors influencing the carboligase side-reaction.
The present review surveys recent efforts in the study of site-directed mutagenesis on PDCs, which are discussed against a background of the structural and kinetical investigations. It also includes recent studies on tailoring the PDCs of Zymomonas mobilis for the syntheses of (R)-phenylacetyl carbinol (PAC), a pre-step in the synthesis of l-ephedrine, by protein design techniques.
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Abbreviations
- ADH:
-
alcohol dehydrogenase
- CD:
-
circular dichroism
- 3D:
-
three-dimensional
- HEThDP:
-
2-(hydroxyethyl)thiamine diphosphate
- Mes:
-
4-morpholineethanesulfonsäure
- nh :
-
Hill-coefficient
- PAC:
-
phenylacetyl carbinol
- PDC:
-
pyruvate decarboxylase
- PDCS.c. :
-
PDC from Saccharomyces cerevisiae
- PDCS.u. :
-
PDC from Saccharomyces uvarum
- PDCZZ.m. :
-
PDC from Zymomonas mobilis
- S0.5 :
-
substrate concentration necessary for half-maximal velocity
- ThDP:
-
thiamine diphosphate
- v/S:
-
velocity vs substrate concentration
- Vmax :
-
maximal velocity
- wt:
-
wild-type
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Dedicated to Professor Dr. Maria-Regina Kula on the occasion of her 60th birthday
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Pohl, M. (1997). Protein design on pyruvate decarboxylase (PDC) by site-directed mutagenesis. In: New Enzymes for Organic Synthesis. Advances in Biochemical Engineering/Biotechnology, vol 58. Springer, Berlin, Heidelberg. https://doi.org/10.1007/BFb0103301
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