Record Details

Comparison of pyruvate decarboxylases from Saccharomyces cerevisiae and Komagataella pastoris (Pichia pastoris)

DSpace at IIT Bombay

View Archive Info
 
 
Field Value
 
Title Comparison of pyruvate decarboxylases from Saccharomyces cerevisiae and Komagataella pastoris (Pichia pastoris)
 
Creator AGARWAL, PK
UPPADA, V
NORONHA, SB
 
Subject Pyruvate decarboxylase
S. cerevisiae
K. pastoris
Decarboxylation
Carboligation
Phenyl acetyl carbinol
SITE-DIRECTED MUTAGENESIS
SUBSTRATE ACTIVATION
ZYMOMONAS-MOBILIS
KLUYVEROMYCES-LACTIS
CRYSTAL-STRUCTURE
STRUCTURAL GENES
BREWERS-YEAST
EXPRESSION
ENZYME
GENOME
 
Description Pyruvate decarboxylases (PDCs) are a class of enzymes which carry out the non-oxidative decarboxylation of pyruvate to acetaldehyde. These enzymes are also capable of carboligation reactions and can generate chiral intermediates of substantial pharmaceutical interest. Typically, the decarboxylation and carboligation processes are carried out using whole cell systems. However, fermentative organisms such as Saccharomyces cerevisiae are known to contain several PDC isozymes; the precise suitability and role of each of these isozymes in these processes is not well understood. S. cerevisiae has three catalytic isozymes of pyruvate decarboxylase (ScPDCs). Of these, ScPDC1 has been investigated in detail by various groups with the other two catalytic isozymes, ScPDC5 and ScPDC6 being less well characterized. Pyruvate decarboxylase activity can also be detected in the cell lysates of Komagataella pastoris, a Crabtree-negative yeast, and consequently it is of interest to investigate whether this enzyme has different kinetic properties. This is also the first report of the expression and functional characterization of pyruvate decarboxylase from K. pastoris (PpPDC). This investigation helps in understanding the roles of the three isozymes at different phases of S. cerevisiae fermentation as well as their relevance for ethanol and carboligation reactions. The kinetic and physical properties of the four isozymes were determined using similar conditions of expression and characterization. ScPDC5 has comparable decarboxylation efficiency to that of ScPDC1; however, the former has the highest rate of reaction, and thus can be used for industrial production of ethanol. ScPDC6 has the least decarboxylation efficiency of all three isozymes of S. cerevisiae. PpPDC in comparison to all isozymes of S. cerevisiae is less efficient at decarboxylation. All the enzymes exhibit allostery, indicating that they are substrate activated.
 
Publisher SPRINGER
 
Date 2014-10-17T05:59:59Z
2014-10-17T05:59:59Z
2013
 
Type Article
 
Identifier APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, 97(21)9439-9449
0175-7598
1432-0614
http://dx.doi.org/10.1007/s00253-013-4758-4
http://dspace.library.iitb.ac.in/jspui/handle/100/16129
 
Language en