The Stereocontrolled Biosynthesis of Mirror-Symmetric 2,4-Diaminobutyric Acid Homopolymers Is Critically Governed by Adenylation Activations

Yamanaka, Kazuya; Fukumoto, Hibiki; Takehara, Munenori; Hamano, Yoshimitsu; Oikawa, Tadao

doi:10.1021/acschembio.0c00321

Cited by 11 publications

(37 citation statements)

References 30 publications

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“…1A ). Similar architectures can be found only in Pls-related β-poly- l -diaminopropionic acid (β-PDAP) synthetase, γ-poly- l -diaminobutanoic acid (γ-PLDAB) synthetase, and γ-poly-d-diaminobutanoic acid (γ-PDDAB) synthetase ( 12 – 14 ). β-PDAP, γ-PLDAB, and γ-PDDAB are cationic isopeptides structurally similar to ε-PL ( Fig.…”

Section: Resultsmentioning

confidence: 54%

“…β-PDAP and γ-PLDAB are coproduced with ε-PL in different Streptomyces strains, with higher antifungal activities and lower antibacterial activities than ε-PL ( 12 , 13 , 15 ). γ-PDDAB is produced by Streptoalloteichus hindustanus with strong antiviral activity and only weak antibacterial activities ( 14 , 16 ). The Corynebacterium protein is more similar to Pls (sequence identity of 51%) than to the other three synthetases (32%, 33%, and 31%, respectively), and similar to the Streptomyces Pls gene, the Corynebacterium gene forms an operon with a peptidase gene, which is a different gene context than for the other three synthetases ( Fig.…”

Section: Resultsmentioning

confidence: 99%

“…Arrows of the same color indicate homologous genes. Genes are as follows: pls , ε-polylysine synthetase ( 17 ); pldII , ε-PL-degrading enzyme II ( 17 ); pldA , γ-poly- l -diaminobutanoic acid synthetase; dat , diaminobutyrate-2-oxoglutarate transaminase; ask , aspartate kinase ( 14 ); pddA , γ-poly- d -diaminobutanoic acid synthetase ( 14 ); and pdabs , β-poly- l -diaminopropionic acid synthetase ( 15 ).…”

Section: Resultsmentioning

confidence: 99%

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Distribution of ε-Poly- l -Lysine Synthetases in Coryneform Bacteria Isolated from Cheese and Human Skin

Jiang

Radko

Gren

et al. 2021

Appl Environ Microbiol

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ε-poly-L-lysine is a potent antimicrobial produced through fermentation of Streptomyces and used in many Asian countries as a food preservative. It is synthesized and excreted by a special NRPS-like enzyme called Pls. Here we discovered a gene from cheese bacterium Corynebacterium variabile that showed high similarity to the Pls from Streptomyces in terms of domain architecture and gene context. By cloning it into Streptomyces coelicolor with a Streptomyces albulus Pls promoter, we confirmed that its product is indeed ε-poly-L-lysine. A comprehensive sequence analysis suggests that Pls genes are widely spread among coryneform actinobacteria isolated from cheese and human skin; 14 out of 15 Brevibacterium isolates and 10 out of 12 Corynebacterium isolates contain it in their genomes. This finding raises the possibility that ε-poly-L-lysine as a bioactive secondary metabolite might be produced and play a role in the cheese and skin ecosystems. IMPORTANCE Every year, microbial contamination causes billions of tons of food wasted and millions of cases of illness. ε-poly-L-lysine has potent, wide spectrum of inhibitory activity and is heat stable and biodegradable. It has been approved for food preservation by an increasing number of countries. ε-poly-L-lysine is produced from the soil bacteria Streptomyces, also a producer of various antibiotic drugs and toxins, and not considered to be a naturally-occurring food component. The frequent finding of pls in cheese and skin bacteria suggests that ε-poly-L-lysine may naturally exist in cheese and on our skin, and ε-poly-L-lysine producers are not limited to filamentous actinobacteria.

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Section: Resultsmentioning

confidence: 54%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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Distribution of ε-Poly- l -Lysine Synthetases in Coryneform Bacteria Isolated from Cheese and Human Skin

Jiang

Radko

Gren

et al. 2021

Appl Environ Microbiol

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“…1B). Similar architectures can only be found in Pls related β-poly-Ldiaminopropionic acid (β-PDAP) synthetase, γ-poly-L-diaminobutanoic acid (γ-PLDAB) synthetase and γ-poly-D-diaminobutanoic acid (γ-PDDAB) synthetase (11)(12)(13). β-PDAP, γ-PLDAB and γ-PDDAB are cationic isopeptides structurally similar to ε-PL ( Fig.…”

mentioning

confidence: 73%

“…β-PDAP and γ-PLDAB are co-produced with ε-PL in different Streptomyces strains with higher antifungal activities and lower antibacterial activities than ε-PL (11,12,14). γ-PDDAB is produced by Streptoalloteichus hindustanus with strong antiviral activity and only weak antibacterial activities (13,15). The Corynebacterium protein is more similar to Pls (sequence identity of 51%) than to the other three synthetases (32%, 33%, and 31%, respectively).…”

mentioning

confidence: 99%

Distribution of Epsilon-Polylysine Synthetases in Coryneform Bacteria Isolated from Cheese and Human Skin

Jiang

Radko

Gren

et al. 2020

Preprint

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Epsilon-polylysine (ε-PL) is an antimicrobial commercially produced by Streptomyces fermentation and widely used in Asian countries for food preservation. Here we discovered a gene from cheese bacterium Corynebacterium variabile that showed high similarity to the ε-PL synthetase from Streptomyces in terms of enzymatic domain architecture and gene context. By cloning it into Streptomyces coelicolor with a Streptomyces albulus ε-PL synthetase promoter, we confirmed that its product is indeed ε-PL. A comprehensive sequence analysis suggests that ε-PL synthetases are widely spread among coryneform bacteria isolated from cheese and human skin; 14 out of 15 Brevibacterium isolates and 10 out of 12 Corynebacterium isolates contain Pls gene. This discovery raises the possibility that ε-PL as a bioactive secondary metabolite might be produced and play a role in the cheese and skin ecosystems.IMPORTANCEEvery year, microbial contamination causes billions of tons of food wasted and millions of cases of foodborne illness. ε-PL is an excellent food preservative as it is potent, wide spectrum and is heat stable and biodegradable. It has not been accepted by all countries (e.g those in the EU) partially because it was not a natural composition of food but rather originated from the soil bacteria Streptomyces, a famous producer of various antibiotic drugs and toxins. The unexpected finding of ε-PL synthetases in cheese and skin bacteria suggests that ε-PL may naturally exist in cheese and on our skin.

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Advances in the adenylation domain: discovery of diverse non-ribosomal peptides

Zhang

Yao

et al. 2023

Appl Microbiol Biotechnol

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The Stereocontrolled Biosynthesis of Mirror-Symmetric 2,4-Diaminobutyric Acid Homopolymers Is Critically Governed by Adenylation Activations

Cited by 11 publications

References 30 publications

Distribution of ε-Poly- l -Lysine Synthetases in Coryneform Bacteria Isolated from Cheese and Human Skin

Distribution of ε-Poly- l -Lysine Synthetases in Coryneform Bacteria Isolated from Cheese and Human Skin

Distribution of Epsilon-Polylysine Synthetases in Coryneform Bacteria Isolated from Cheese and Human Skin

Advances in the adenylation domain: discovery of diverse non-ribosomal peptides

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