PduP is a coenzyme-a-acylating propionaldehyde dehydrogenase associated with the polyhedral bodies involved in B12-dependent 1,2-propanediol degradation by Salmonella enterica serovar Typhimurium LT2

@article{Leal2003PduPIA,
  title={PduP is a coenzyme-a-acylating propionaldehyde dehydrogenase associated with the polyhedral bodies involved in B12-dependent 1,2-propanediol degradation by Salmonella enterica serovar Typhimurium LT2},
  author={Nicole A. Leal and Gregory D. Havemann and Thomas A. Bobik},
  journal={Archives of Microbiology},
  year={2003},
  volume={180},
  pages={353-361}
}
Salmonella enterica forms polyhedral bodies involved in coenzyme-B12-dependent 1,2-propanediol degradation. [...] Key Result A PCR-based method was used to construct a precise nonpolar deletion of the gene pduP. The resulting pduP deletion strain grew poorly on 1,2-propanediol minimal medium and expressed 105-fold less propionaldehyde dehydrogenase activity (0.011 μmol min−1 mg−1) than did wild-type S. enterica grown under similar conditions (1.15 μmol min−1 mg−1).Expand
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PduL is an evolutionary distinct phosphotransacylase involved in B12-dependent 1,2-propanediol degradation by Salmonella enterica serovar Typhimurium LT2 and is associated with the propanediol utilization microcompartments
TLDR
It is shown that the pduL gene encodes an evolutionarily distinct PTAC used for 1,2-PD degradation that is unrelated in amino acid sequence to known PTAC enzymes and that PduL homologues are distributed among at least 49 bacterial species, but are absent from the Archaea and Eukarya. Expand
PduL Is an Evolutionarily Distinct Phosphotransacylase Involved in B12-Dependent 1,2-Propanediol Degradation by Salmonella enterica Serovar Typhimurium LT2
TLDR
It is shown that the pduL gene encodes an evolutionarily distinct PTAC used for 1,2-PD degradation, and that PduL homologues are distributed among at least 49 bacterial species but are absent from the Archaea and Eukarya. Expand
Microcompartments for B12-Dependent 1,2-Propanediol Degradation Provide Protection from DNA and Cellular Damage by a Reactive Metabolic Intermediate
TLDR
High-pressure liquid chromatography analyses of culture medium were used to show that the major products of aerobic 1,2-PD degradation are propionaldehyde, propionate, and 1-propanol, and it is proposed that a primary function of the MCPs involved in 1,1- PD degradation is the mitigation of toxicity and DNA damage by propional dehyde. Expand
Coenzyme A-acylating propionaldehyde dehydrogenase (PduP) from Lactobacillus reuteri: kinetic characterization and molecular modeling.
TLDR
In silico docking of the coenzyme A and NAD(+), respectively, showed a common binding site consisting of amino acids Thr145, Ile275, Cys277 and Ser417, which through site-directed mutagenesis to alanine and kinetic studies, were confirmed as essential for the catalytic activity of PduP. Expand
The PduQ Enzyme Is an Alcohol Dehydrogenase Used to Recycle NAD+ Internally within the Pdu Microcompartment of Salmonella enterica
TLDR
It is shown that the PduQ protein of S. enterica is an iron-dependent alcohol dehydrogenase used for 1,2-PD catabolism and the first report of internal recycling as a mechanism for cofactor homeostasis within a bacterial MCP. Expand
The PduM Protein Is a Structural Component of the Microcompartments Involved in Coenzyme B12-Dependent 1,2-Propanediol Degradation by Salmonella enterica
TLDR
It is shown that the protein PduM is required for the assembly and function of the Pdu MCP, and may represent a new class of MCP structural proteins that are unrelated in sequence to proteins of known function. Expand
Characterization of the PduS Cobalamin Reductase of Salmonellaenterica and Its Role in the Pdu Microcompartment
TLDR
Genetic studies showed that a pduS deletion decreased the growth rate of Salmonella on 1,2-PD, supporting a role in cobalamin reduction in vivo, and studies demonstrated that the PduS protein is a component of the P DU microcompartments (MCPs) used for 1, 2-PD degradation and that it interacts with thePduO adenosyltransferase, which catalyzes the terminal step of AdoCbl synthesis. Expand
Exploring Lactobacillus reuteri DSM20016 as a biocatalyst for transformation of longer chain 1,2-diols: Limits with microcompartment
TLDR
Recombinant Escherichia coli BL21(DE3) cells harboring the GDH variant converted diols with up to C6 carbon chain length to their respective aldehydes, suggesting that the protein shell of the microcompartment in L. reuteri posed a barrier to the passage of longer chain substrate. Expand
Biochemical evidence that the pduS gene encodes a bifunctional cobalamin reductase.
TLDR
Results indicate that the PduS enzyme represents a new class of cobalamin reductase, which is likely to be important physiologically, since cob(I)alamin is extremely reactive and would need to be protected from unproductive by-reactions. Expand
The PduL Phosphotransacylase Is Used To Recycle Coenzyme A within the Pdu Microcompartment
TLDR
The results support a model in which a steady supply of coenzyme A is provided to MCP lumen enzymes by internal recycling by PduL as well as by the movement of cofenzyme A across the shell by an unknown mechanism. Expand
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References

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PduA Is a Shell Protein of Polyhedral Organelles Involved in Coenzyme B12-Dependent Degradation of 1,2-Propanediol in Salmonella enterica Serovar Typhimurium LT2
TLDR
The results suggest that the polyhedral organelles formed by S. enterica during growth on 1,2-propanediol are not involved in the concentration of 1, 2-pro panediol or coenzyme B(12), but are consistent with the hypothesis that these organlles moderate aldehyde production to minimize toxicity. Expand
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TLDR
The polyhedral organelles involved in B(12)-dependent 1,2-PD degradation by S. enterica were purified by a combination of detergent extraction and differential and density gradient centrifugation and contained four enzymes, indicating that the primary catalytic function of the S. entersica organelle function to minimize aldehyde toxicity during growth on 1, 2-PD. Expand
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The propanediol utilization (pdu) operon of Salmonella enterica serovar Typhimurium LT2 includes genes necessary for formation of polyhedral organelles involved in coenzyme B(12)-dependent 1, 2-propanediol degradation.
TLDR
Genetic tests demonstrate that genes of the pdu operon are required for polyhedral body formation, and immunoelectron microscopy shows that AdoCbl-dependent diol dehydratase is associated with these polyhedra, the first evidence for a B(12)-dependent enzyme associated with a polyhedral bodies. Expand
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TLDR
It is shown that the pduO gene encodes a protein with ATP:cob(I)alamin adenosyltransferase activity, apparently the conversion of inactive cobalamins to AdoCbl for 1,2-propanediol degradation, and that PduO is a bifunctional enzyme. Expand
Glutathione is required for maximal transcription of the cobalamin biosynthetic and 1,2-propanediol utilization (cob/pdu) regulon and for the catabolism of ethanolamine, 1,2-propanediol, and propionate in Salmonella typhimurium LT2
TLDR
Nutritional analysis and DNA sequencing confirmed that a strain defective in expression of the cob/pdu regulon in response to 1,2-PDL lacked a functional gshA gene, and possible roles for GSH in ethanolamine, 1, 2- PDL, and propionate catabolism are proposed and discussed. Expand
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TLDR
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TLDR
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TLDR
Evidence is presented that aerobically grown cells have a different metabolic pathway for utilizing 1,2-propanediol, and this metabolic pathway was also suggested in some other genera of Enterobacteriaceae which were able to grow anaerobically on 1, 2-pro panediol. Expand
The Alternative Electron Acceptor Tetrathionate Supports B12-Dependent Anaerobic Growth ofSalmonella enterica Serovar Typhimurium on Ethanolamine or 1,2-Propanediol
TLDR
The paradox of cobalamin de novo by Salmonella enterica serovar Typhimurium strain LT2 and the absence of this ability in Escherichia coli is resolved by the electron acceptor tetrathionate, which allowsSalmonella to grow anaerobically on ethanolamine or 1,2-propanediol by using endogenously synthesized B12. Expand
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