Substrate Trapping in the Siderophore Tailoring Enzyme PvdQ

Clevenger, Kenneth D.; Mascarenhas, Romila; Catlin, Daniel S.; Wu, Rui; Kelleher, Neil L.; Drake, Eric J.; Gulick, Andrew M.; Liu, Dali; Fast, Walter

doi:10.1021/acschembio.7b00031

Cited by 6 publications

(2 citation statements)

References 26 publications

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“…In the periplasm, the acylation of ferribactin is removed by the Ntn-type hydrolase PvdQ 25 45 . This now established function was first proposed by Visca et al .…”

Section: Periplasmic Completion Of Pyoverdine Synthesismentioning

confidence: 99%

The biosynthesis of pyoverdines

Ringel¹,

Brüser²

2018

Microb Cell

119

134

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Pyoverdines are fluorescent siderophores of pseudomonads that play important roles for growth under iron-limiting conditions. The production of pyoverdines by fluorescent pseudomonads permits their colonization of hosts ranging from humans to plants. Prominent examples include pathogenic or non-pathogenic species such as Pseudomonas aeruginosa, P. putida, P. syringae, or P. fluorescens. Many distinct pyoverdines have been identified, all of which have a dihydroxyquinoline fluorophore in common, derived from oxidative cyclizations of non-ribosomal peptides. These serve as precursor of pyoverdines and are commonly known as ferribactins. Ferribactins of distinct species or even strains often differ in their sequence, resulting in a large variety of pyoverdines. However, synthesis of all ferribactins begins with an L-Glu/D-Tyr/L-Dab sequence, and the fluorophore is generated from the D-Tyr/L-Dab residues. In addition, the initial L-Glu residue is modified to various acids and amides that are responsible for the range of distinguishable pyoverdines in individual strains. While ferribactin synthesis is a cytoplasmic process, the maturation to the fluorescent pyoverdine as well as the tailoring of the initial glutamate are exclusively periplasmic processes that have been a mystery until recently. Here we review the current knowledge of pyoverdine biosynthesis with a focus on the recent advancements regarding the periplasmic maturation and tailoring reactions.

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“…In the periplasm, the acylation of ferribactin is removed by the Ntn-type hydrolase PvdQ 25 45 . This now established function was first proposed by Visca et al .…”

Section: Periplasmic Completion Of Pyoverdine Synthesismentioning

confidence: 99%

The biosynthesis of pyoverdines

Ringel¹,

Brüser²

2018

Microb Cell

119

134

View full text Add to dashboard Cite

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“…Recently, the structure of PvdQ bound to the acyl pyoverdine precursor was determined through the use of a circularly permuted enzyme that enabled the production of a processed but catalytically inactive form of the enzyme. 234 …”

Section: Pseudomonas Aeruginosamentioning

confidence: 99%

Nonribosomal peptide synthetase biosynthetic clusters of ESKAPE pathogens

Gulick

2017

Nat. Prod. Rep.

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Overview Natural products are important secondary metabolites produced by bacterial and fungal species that play important roles in cellular growth and signaling, nutrient acquisition, intra- and interspecies communication, and virulence. A subset of natural products is produced by nonribosomal peptide synthetases (NRPSs), a family of large, modular enzymes that function in an assembly line fashion. Because of the pharmaceutical activity of many NRPS products, much effort has gone into the exploration of their biosynthetic pathways and the diverse products they make. Many interesting NRPS pathways have been identified and characterized from both terrestrial and marine bacterial sources. Recently, several NRPS pathways in human commensal bacterial species have been identified that produce molecules with antibiotic activity, suggesting another source of interesting NRPS pathways may be the commensal and pathogenic bacteria that live on the human body. The ESKAPE pathogens (Enterococcus faecium, Staphylococcus aureus, Klebsiella pneumoniae, Acinetobacter baumannii, Pseudomonas aeruginosa, and Enterobacter spp.) have been identified as a significant cause of human bacterial infections that are frequently multidrug resistant. The emerging resistance profile of these organisms has prompted calls from multiple international agencies to identify novel antibacterial targets and develop new approaches to treat infections from ESKAPE pathogens. Each of these species contains several NRPS biosynthetic gene clusters. While some have been well characterized and produce known natural products with important biological roles in microbial physiology, others have yet to be investigated. This review catalogs the NRPS pathways of ESKAPE pathogens. The exploration of novel NRPS products may lead to a better understanding of the chemical communication used by human pathogens and potentially to the discovery of novel therapeutic approaches.

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The complete genome of the antifungal bacterium Pseudomonas sp. strain MS82

Lin

et al. 2019

J Plant Dis Prot

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Substrate Trapping in the Siderophore Tailoring Enzyme PvdQ

Cited by 6 publications

References 26 publications

The biosynthesis of pyoverdines

The biosynthesis of pyoverdines

Nonribosomal peptide synthetase biosynthetic clusters of ESKAPE pathogens

The complete genome of the antifungal bacterium Pseudomonas sp. strain MS82

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