Abstract
The pduP gene encodes a propionaldehyde dehydrogenase (PduP) was investigated for the role in 3-hydroxypropionic acid (3-HP) glycerol metabolism in Klebsiella pneumoniae. The enzyme assay showed that cell extracts from a pduP mutant strain lacked measurable dehydrogenase activity. Additionally, the mutant strain accumulated the cytotoxic intermediate metabolite 3-hydroxypropionaldehyde (3-HPA), causing both cell death and a lower final 3-HP titer. Ectopic expression of pduP restored normal cell growth to mutant. The enzymatic property of recombinant protein from Escherichia coli was examined, exhibiting a broad substrate specificity, being active on 3-HPA. The present work is thus the first to demonstrate the role of PduP in glycerol metabolism and biosynthesis of 3-HP.
Copyright © 2011 Elsevier Ltd. All rights reserved.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Aldehydes / metabolism*
-
Amino Acid Sequence
-
Bacterial Proteins / chemistry
-
Bacterial Proteins / isolation & purification
-
Bacterial Proteins / metabolism*
-
Biosynthetic Pathways* / drug effects
-
Escherichia coli / drug effects
-
Escherichia coli / metabolism
-
Gene Deletion
-
Klebsiella pneumoniae / drug effects
-
Klebsiella pneumoniae / enzymology*
-
Klebsiella pneumoniae / growth & development
-
Lactic Acid / analogs & derivatives*
-
Lactic Acid / biosynthesis
-
Microbial Viability / drug effects
-
Molecular Sequence Data
-
Oxidoreductases / chemistry
-
Oxidoreductases / isolation & purification
-
Oxidoreductases / metabolism*
-
Sequence Analysis, Protein
-
Sirolimus / pharmacology
-
Substrate Specificity / drug effects
Substances
-
Aldehydes
-
Bacterial Proteins
-
Lactic Acid
-
propionaldehyde
-
hydracrylic acid
-
Oxidoreductases
-
Sirolimus