Characterization of the PduS Cobalamin Reductase of
            <i>Salmonella</i>
            <i>enterica</i>
            and Its Role in the Pdu Microcompartment

Cheng, Sibo; Bobik, Thomas A.

doi:10.1128/jb.00575-10

Cited by 49 publications

(72 citation statements)

References 68 publications

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“…Thus, supplying the enzymes of the Pdu MCP with NAD ϩ /NADH is thought to require both internal recycling and transport across the protein shell via specific pores. Studies with the Pdu system also showed that all of the enzymes needed for adenosylcobalamin (Ado-B 12 ) recycling were components of purified MCPs, and it was therefore proposed that cobalamin recycling can also occur internally within the Pdu MCP (80).…”

Section: Figmentioning

confidence: 99%

“…2D electrophoresis followed by proteomics analyses identified 14 different polypeptide components (PduABB=CDEGHJKOPTU). Subsequent studies determined that 4 additional proteins (PduMNQS) are tightly associated with the Pdu MCP and that the PduV protein might be associated with the outer surface of the shell (48,58,79,80,84). Of the 19 polypeptides that are components of the Pdu MCP, 8 (PduABB=JKNTU) are likely shell components, PduM and PduV are of uncertain function, and 9 polypeptides are subunits of six enzymes: B 12 -dependent diol dehydratase (DDH) (PduCDE), DDH reactivase (PduGH), propionaldehyde dehydrogenase (PduP), 1-propanol dehydrogenase (PduQ), cobalamin reductase (PduS), and adenosyltransferase (ATR) (PduO) (6,28,79,80,83,89,(104)(105)(106)(107).…”

Section: Purification Composition and Enzymology Of The Pdu Mcpmentioning

confidence: 99%

“…7). The PduGH, PduS, and PduO enzymes are encoded by the pdu operon, and all these enzymes are associated with the Pdu MCP, suggesting that DDH reactivation and OH-B 12 recycling occur within the MCP lumen (80,104,105). The PduS and PduO enzymes are also used for the assimilation of exogenous OH-B 12 and are redundant with a set of constitutively expressed enzymes for this process (128)(129)(130).…”

Section: Enzymes For Reactivation Of Diol Dehydratase and B 12 Recyclingmentioning

confidence: 99%

“…Reactivation begins with the PduGH reactivase, which converts the inactive [OH-B 12 -DDH] to free OH-B 12 and apoenzyme (120,(122)(123)(124)(125)(126)(127). Subsequently, Ado-B 12 spontaneously reassociates with apo-DDH to form an active holoenzyme, and the OH-B 12 is recycled back to Ado-B 12 by cobalamin reductase (PduS) and adenosyltransferase (PduO) (80,104,105) (Fig. 7).…”

Section: Enzymes For Reactivation Of Diol Dehydratase and B 12 Recyclingmentioning

confidence: 99%

“…The shells of the Pdu MCP are built primarily from BMC domain proteins and also include a BMV pentamer that forms the vertices (6). A variety of studies indicate that the Pdu MCPs are used to optimize growth on 1,2-PD by sequestering a toxic/volatile pathway intermediate (propionaldehyde) (6,22,58,79,80,(82)(83)(84).…”

Section: 2-propanediol Degradation and The Pdu Mcpmentioning

confidence: 99%

See 4 more Smart Citations

Diverse Bacterial Microcompartment Organelles

Chowdhury

Sinha

Chun

et al. 2014

Microbiol Mol Biol Rev

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214

278

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SUMMARY Bacterial microcompartments (MCPs) are sophisticated protein-based organelles used to optimize metabolic pathways. They consist of metabolic enzymes encapsulated within a protein shell, which creates an ideal environment for catalysis and facilitates the channeling of toxic/volatile intermediates to downstream enzymes. The metabolic processes that require MCPs are diverse and widely distributed and play important roles in global carbon fixation and bacterial pathogenesis. The protein shells of MCPs are thought to selectively control the movement of enzyme cofactors, substrates, and products (including toxic or volatile intermediates) between the MCP interior and the cytoplasm of the cell using both passive electrostatic/steric and dynamic gated mechanisms. Evidence suggests that specialized shell proteins conduct electrons between the cytoplasm and the lumen of the MCP and/or help rebuild damaged iron-sulfur centers in the encapsulated enzymes. The MCP shell is elaborated through a family of small proteins whose structural core is known as a bacterial microcompartment (BMC) domain. BMC domain proteins oligomerize into flat, hexagonally shaped tiles, which assemble into extended protein sheets that form the facets of the shell. Shape complementarity along the edges allows different types of BMC domain proteins to form mixed sheets, while sequence variation provides functional diversification. Recent studies have also revealed targeting sequences that mediate protein encapsulation within MCPs, scaffolding proteins that organize lumen enzymes and the use of private cofactor pools (NAD/H and coenzyme A [HS-CoA]) to facilitate cofactor homeostasis. Although much remains to be learned, our growing understanding of MCPs is providing a basis for bioengineering of protein-based containers for the production of chemicals/pharmaceuticals and for use as molecular delivery vehicles.

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Section: Figmentioning

confidence: 99%

Section: Purification Composition and Enzymology Of The Pdu Mcpmentioning

confidence: 99%

Section: Enzymes For Reactivation Of Diol Dehydratase and B 12 Recyclingmentioning

confidence: 99%

Section: Enzymes For Reactivation Of Diol Dehydratase and B 12 Recyclingmentioning

confidence: 99%

Section: 2-propanediol Degradation and The Pdu Mcpmentioning

confidence: 99%

See 3 more Smart Citations

Diverse Bacterial Microcompartment Organelles

Chowdhury

Sinha

Chun

et al. 2014

Microbiol Mol Biol Rev

Self Cite

214

278

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Synthetic Biology in Metabolic Engineering: From Complex Biochemical Pathways to Compartmentalized Metabolic Processes - a Vitamin Connection

Deery

Frank

Lawrence

et al. 2014

Encyclopedia of Molecular Cell Biology and Molecular Medicine

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Cobalamin Biosynthesis and Insertion

Mattes

Deery

Warren

et al. 2017

Encyclopedia of Inorganic and Bioinorganic Chemistry

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Metal‐containing cyclic tetrapyrroles are widely distributed in nature, and together comprise the family of compounds frequently referred to as “the pigments of life,” namely cobamides (Cba, contain cobalt), chlorophylls (contain magnesium), hemes (contain iron), and factor F 430 (contains nickel). In comparison to these other modified tetrapyrroles, the B 12 architecture is slightly different. The chemistry of the cobalt ion is key to the function of the molecule as either a coenzyme or cofactor. Other differences include a contraction of the tetrapyrrole mainframe, which allows for tighter binding of the metal, and the presence of a lower nucleotide loop that provides an extra ligand for the metal. The biosynthesis of adenosylcobalamin requires the concerted effort of around 30 enzyme‐mediated steps tethered with the cellular provision of a range of cofactors and cobalt. The biosynthesis can be divided into two major sections, the first being the synthesis of the tetrapyrrole‐derived corrin ring and the second involving the synthesis and attachment of the lower nucleotide loop. In the last decade, much has been learned about how the vitamin form is converted to its biologically active coenzymic form, providing mechanistic answers into the events that overcome steep thermodynamic barriers in the formation of the covalent, organometallic bond between the cobalt ion of the ring and the 5′‐deoxyadenosyl upper ligand. Exciting recent discoveries regarding the biosynthesis of the lower ligand base 5,6‐dimethylbenzimidazole in aerobes and anaerobes have filled long‐standing gaps of knowledge, providing a solid platform for the analysis of what is likely to be a membrane‐anchored multienzyme complex.

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Characterization of the PduS Cobalamin Reductase of Salmonella enterica and Its Role in the Pdu Microcompartment

Cited by 49 publications

References 68 publications

Diverse Bacterial Microcompartment Organelles

Diverse Bacterial Microcompartment Organelles

Synthetic Biology in Metabolic Engineering: From Complex Biochemical Pathways to Compartmentalized Metabolic Processes - a Vitamin Connection

Cobalamin Biosynthesis and Insertion

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