Structures of cepafungins I, II and III.

Terui, Yoshihiro; Nishikawa, Junko; Hinoo, Hiroshi; Kato, Toshiyuki; Shoji, Jun

doi:10.7164/antibiotics.43.788

Cited by 38 publications

(25 citation statements)

References 7 publications

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“…CB-3. 42 The Lys-Xxx-Mal motif is found in syringolin, which is a virulence factor of host plants produced by Pseudomonas syringae pv. syringae B301D-R. 43 All three compounds have lactam ring structures between the amino group of a Lys residue and the C-terminal carboxyl group.…”

Section: Deduced Functions Of Novel Pks/nrps Produced By Pseudomonas mentioning

confidence: 99%

Comprehensive Analysis of Distinctive Polyketide and Nonribosomal Peptide Structural Motifs Encoded in Microbial Genomes

Minowa

Araki

Kanehisa

2007

Journal of Molecular Biology

140

132

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Section: Deduced Functions Of Novel Pks/nrps Produced By Pseudomonas mentioning

confidence: 99%

Comprehensive Analysis of Distinctive Polyketide and Nonribosomal Peptide Structural Motifs Encoded in Microbial Genomes

Minowa

Araki

Kanehisa

2007

Journal of Molecular Biology

140

132

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“…The determination of SylA's structure revealed its similarity to the glidobactins (similar to cepafungins), a family of agents from soil bacteria with anti-tumor and antifungal activity isolated more than twenty years ago [62,63]. Like SylA, glidobactin A (GlbA) contains a 12-membered macrolactam ring with its characteristic α,β-unsaturated carbonyl group (Figure 1).…”

Section: Syrbactins In Animal Pathogensmentioning

confidence: 99%

The role of bacterial phytotoxins in inhibiting the eukaryotic proteasome

Dudler

2014

Trends in Microbiology

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The ubiquitin-26S proteasome degradation system (UPS) plays a pivotal role in almost all aspects of plant life, including defending against pathogens. Although the proteasome is important for plant immunity, it has been found to be also exploited by pathogens using effectors to increase their virulence. Recent work on the XopJ effector and syringolin A/syrbactins has highlighted host proteasome inhibition as a virulence strategy of pathogens. This review will focus on these recent developments. AbstractThe ubiquitin-26S proteasome degradation system (UPS) plays a pivotal role in almost all aspects of plant life, including defending against pathogens. While the proteasome is important for plant immunity, it has been found to also be exploited by pathogens using effectors to increase their virulence. Recent work on the XopJ effector and syringolin A/syrbactins has highlighted host proteasome inhibition as a virulence strategy of pathogens. This review will focus on these recent developments. The ubiquitin-26S proteasome degradation system (UPS) and plant immunityBesides the lysosome, the UPS is the main protein degradation system of eukaryotic cells that not only destructs misfolded proteins but is also involved in many cellular processes by degrading proteins regulating such processes [1,2]. Proteins destined for destruction by the proteasome become polyubiquitinated by a reaction cascade involving three enzymes designated E1, E2, and E3. Ubiquitin is activated in an ATP-dependent way by E1 and transferred to E2, from which it is normally directly transferred to a lysine residue of the target protein by E3, which, by selecting target proteins, confers specificity to the UPS [3].Polyubiquitination is achieved by multiple rounds in which further ubiquitin units are conjugated to an internal lysine residue of ubiquitin. Polyubiquitinated proteins are substrates for the proteasome, which is composed of two 19S regulatory particles (RP) capping a 20S core particle (CP). The RPs recognize polyubiquitinated proteins, which become deubiquitinated and unfolded in an ATP-dependent reaction, and regulate access of unfolded substrates to the proteolytic channel of the CP. The channel is formed by four stacked sevenmembered rings. The two identical outer rings consist of seven different α-subunits, whereas 3 the two identical inner rings consist of seven different β-subunits, three of which have proteolytic activities: the β1 subunit exhibits a caspase-like activity (CL), cleaving protein substrates after acidic residues, while the β2 and β5 subunits have trypsin-like (TL) and chymotrypsin-like (ChTL) activities cleaving after basic and hydrophobic residues, respectively. In all three catalytic subunits, the active site residue is the N-terminal threonineThe UPS is involved in the signaling pathways of nearly all plant hormones, including salicylic acid (SA), jasmonic acid (JA), and ethylene (ET), hormones of particular importance for plant defense against pathogens [5]. SA plays a prominent role in defense reactio...

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“…5c) are structurally highly similar to the glidobactins, exemplified by cepafungin II which is even identical to glidobactin A [65][66]. Similar to glidobactins, cepafungins proved to be highly active in cellular assays but further studies have not yet been performed with this compound class.…”

Section: Syrbactinsmentioning

confidence: 95%

Macrocyclic Proteasome Inhibitors

Krahn¹,

Ottmann²,

Kaiser³

2011

CMC

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Proteasome inhibitors have proven to be effective anticancer agents. Despite the success of the first on the market proteasome inhibitor bortezomib in chemotherapy, alternative clinically useful proteasome inhibitors are still urgently needed as bortezomib therapy causes severe side effects and is limited by arising drug resistance. Experience from previous proteasome inhibitor studies has thereby demonstrated that the identification of proteasome inhibitor structures with suitable pharmacological properties is a key factor for a successful development of clinically useful proteasome inhibitors. Macrocycles often show distinct and in comparison to linear small molecules superior pharmacological properties. Consequently, macrocyclic proteasome inhibitors might represent promising small molecules for drug development. Here, we want to highlight the current state of the art of macrocyclic proteasome inhibitor research. To this end, we give an overview and critically discuss currently known classes of macrocyclic proteasome inhibitors.

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Structures of cepafungins I, II and III.

Cited by 38 publications

References 7 publications

Comprehensive Analysis of Distinctive Polyketide and Nonribosomal Peptide Structural Motifs Encoded in Microbial Genomes

Comprehensive Analysis of Distinctive Polyketide and Nonribosomal Peptide Structural Motifs Encoded in Microbial Genomes

The role of bacterial phytotoxins in inhibiting the eukaryotic proteasome

Macrocyclic Proteasome Inhibitors

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