Draft Genome Sequence of Actinoplanes utahensis NRRL 12052, a Microorganism Involved in Industrial Production of Pharmaceutical Intermediates

Velasco-Bucheli, Rodrigo; Cerro, Carlos del; Hormigo, Daniel; Acebal, Carmen; Arroyo, Miguel; Garcı́a, José Luis; Mata, Isabel de la

doi:10.1128/genomea.01411-14

Cited by 4 publications

(5 citation statements)

References 17 publications

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“…The presence of the putative ahla gene was detected in the draft genome of Actinoplanes utahensis NRRL 12052 [ 23 ]. This gene, as well as the aac gene, which encodes for the aculeacin A acylase from A. utahensis ( Au AAC) [ 24 ], was located within contig 8 and related to nonribosomal peptide synthetases (NRPS) and siderophores biosynthesis based on antiSMASH analysis [ 25 ].…”

Section: Resultsmentioning

confidence: 99%

“…Bacterial strains, plasmids, and oligonucleotides used are listed in Table 3 . Actinoplanes utahensis NRRL 12052 was used as the DNA source [ 23 ], Escherichia coli DH5α was used as the host for subcloning experiments [ 64 ], and Rhodococcus sp. T104 KACC 21099 was used as the host for gene expression [ 38 ].…”

Section: Methodsmentioning

confidence: 99%

“…The hypothetical ahla gene (GenBank accession no. NZ_JRTT01000008.1), including its signal peptide coding sequence and the putative RBS sequence (GGAGG), was amplified by PCR using Pfu DNA polymerase (Thermo, Waltham, MA, USA) and genomic DNA from A. utahensis NRRL 12052 [ 23 ] as a template. PCR was performed in Mastercycler Personal equipment (Eppendorf, Hamburg, Germany), and amplification conditions were set according to the high G + C content of the actinomycetes genome [ 29 , 39 ].…”

Section: Methodsmentioning

confidence: 99%

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Novel Bifunctional Acylase from Actinoplanes utahensis: A Versatile Enzyme to Synthesize Antimicrobial Compounds and Use in Quorum Quenching Processes

et al. 2021

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Many intercellular communication processes, known as quorum sensing (QS), are regulated by the autoinducers N-acyl-l-homoserine lactones (AHLs) in Gram-negative bacteria. The inactivation of these QS processes using different quorum quenching (QQ) strategies, such as enzymatic degradation of the autoinducers or the receptor blocking with non-active analogs, could be the basis for the development of new antimicrobials. This study details the heterologous expression, purification, and characterization of a novel N-acylhomoserine lactone acylase from Actinoplanes utahensis NRRL 12052 (AuAHLA), which can hydrolyze different natural penicillins and N-acyl-homoserine lactones (with or without 3-oxo substitution), as well as synthesize them. Kinetic parameters for the hydrolysis of a broad range of substrates have shown that AuAHLA prefers penicillin V, followed by C12-HSL. In addition, AuAHLA inhibits the production of violacein by Chromobacterium violaceum CV026, confirming its potential use as a QQ agent. Noteworthy, AuAHLA is also able to efficiently synthesize penicillin V, besides natural AHLs and phenoxyacetyl-homoserine lactone (POHL), a non-natural analog of AHLs that could be used to block QS receptors and inhibit signal of autoinducers, being the first reported AHL acylase capable of synthesizing AHLs.

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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Novel Bifunctional Acylase from Actinoplanes utahensis: A Versatile Enzyme to Synthesize Antimicrobial Compounds and Use in Quorum Quenching Processes

et al. 2021

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“…In addition, we investigated potential HisN orthologs from Actinoplanes utahensis NRRL 12052 [ 31 ]. This actinobacterium possesses two genes encoding IMPase-like proteins that are most similar to HisN Cg .…”

Section: Resultsmentioning

confidence: 99%

“…DNA of Dietzia sp. strain Chol2 [ 50 ], Zymomonas mobilis ZM4 [ 30 ], and Actinoplanes utahensis NRRL 12052 [ 31 ] was used for the amplification of hisN homologs from these bacteria.…”

Section: Methodsmentioning

confidence: 99%

Sequence-based identification of inositol monophosphatase-like histidinol-phosphate phosphatases (HisN) in Corynebacterium glutamicum, Actinobacteria, and beyond

et al. 2017

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Background: The eighth step of L-histidine biosynthesis is carried out by an enzyme called histidinol-phosphate phosphatase (HolPase). Three unrelated HolPase families are known so far. Two of them are well studied: HAD-type HolPases known from Gammaproteobacteria like Escherichia coli or Salmonella enterica and PHP-type HolPases known from yeast and Firmicutes like Bacillus subtilis. However, the third family of HolPases, the inositol monophosphatase (IMPase)-like HolPases, present in Actinobacteria like Corynebacterium glutamicum (HisN) and plants, are poorly characterized. Moreover, there exist several IMPase-like proteins in bacteria (e.g. CysQ, ImpA, and SuhB) which are very similar to HisN but most likely do not participate in L-histidine biosynthesis. Results: Deletion of hisN, the gene encoding the IMPase-like HolPase in C. glutamicum, does not result in complete L-histidine auxotrophy. Out of four hisN homologs present in the genome of C. glutamicum (impA, suhB, cysQ, and cg0911), only cg0911 encodes an enzyme with HolPase activity. The enzymatic properties of HisN and Cg0911 were determined, delivering the first available kinetic data for IMPase-like HolPases. Additionally, we analyzed the amino acid sequences of potential HisN, ImpA, SuhB, CysQ and Cg0911 orthologs from bacteria and identified six conserved sequence motifs for each group of orthologs. Mutational studies confirmed the importance of a highly conserved aspartate residue accompanied by several aromatic amino acid residues present in motif 5 for HolPase activity. Several bacterial proteins containing all identified HolPase motifs, but showing only moderate sequence similarity to HisN from C. glutamicum, were experimentally confirmed as IMPase-like HolPases, demonstrating the value of the identified motifs. Based on the confirmed IMPase-like HolPases two profile Hidden Markov Models (HMMs) were build using an iterative approach. These HMMs allow the fast, reliable detection and differentiation of the two paralog groups from each other and other IMPases. Conclusion: The kinetic data obtained for HisN from C. glutamicum, as an example for an IMPase-like HolPases, shows remarkable differences in enzyme properties as compared to HAD-or PHP-type HolPases. The six sequence motifs and the HMMs presented in this study can be used to reliably differentiate between IMPase-like HolPases and IMPase-like proteins with no such activity, with the potential to enhance current and future genome annotations. A phylogenetic analysis reveals that IMPase-like HolPases are not only present in Actinobacteria and plant but can be found in further bacterial phyla, including, among others, Proteobacteria, Chlorobi and Planctomycetes.

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Biocatalysis for Industrial Production of Active Pharmaceutical Ingredients (APIs)

Arroyo

Mata

García

et al. 2017

Biotechnology of Microbial Enzymes

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Draft Genome Sequence of Actinoplanes utahensis NRRL 12052, a Microorganism Involved in Industrial Production of Pharmaceutical Intermediates

Cited by 4 publications

References 17 publications

Novel Bifunctional Acylase from Actinoplanes utahensis: A Versatile Enzyme to Synthesize Antimicrobial Compounds and Use in Quorum Quenching Processes

Novel Bifunctional Acylase from Actinoplanes utahensis: A Versatile Enzyme to Synthesize Antimicrobial Compounds and Use in Quorum Quenching Processes

Sequence-based identification of inositol monophosphatase-like histidinol-phosphate phosphatases (HisN) in Corynebacterium glutamicum, Actinobacteria, and beyond

Biocatalysis for Industrial Production of Active Pharmaceutical Ingredients (APIs)

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