Open AccessExceptional characteristics of heterotetrameric (α 2 β 2 ) E1p of the pyruvate dehydrogenase complex from Zymomonas mobilis : expression from an own promoter and a lipoyl domain in E1β
Author(s) -
Neveling Ute,
BringerMeyer Stephanie,
Sahm Hermann
Publication year - 1999
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1999.tb13721.x
Subject(s) - zymomonas mobilis , pyruvate dehydrogenase complex , biochemistry , escherichia coli , pyruvate dehydrogenase phosphatase , biology , dihydrolipoyl transacetylase , protein subunit , microbiology and biotechnology , recombinant dna , dehydrogenase , dna , gene , chemistry , enzyme , ethanol fuel , fermentation
In the pyruvate dehydrogenase complex (PDHC) of Zymomonas mobilis the β subunit of the pyruvate dehydrogenase (E1p) as well as the acetyltransferase (E2p) contain an N‐terminal lipoyl domain. Both lipoyl domains were acetylated in vitro using 2‐ 14 C‐pyruvate as a substrate, demonstrating that both lipoyl domains can accept acetyl groups from the E1 component. As previously shown the structural genes ( pdhA αβ, pdhB, lpd ) encoding the pyruvate dehydrogenase complex of Z. mobilis are located in two distinct gene clusters, pdhA αβ and pdhB ‐ orf2 ‐ lpd (U. Neveling et al. (1998) J. Bacteriol. 180, 1540–1548). Analysis of pdh gene expression using lacZ fusions revealed that the DNA fragments upstream of pdhA α, pdhB and lpd each have promoter activities. These pdh promoter activities were 7–30‐fold higher in Z. mobilis than in Escherichia coli .