The need for new antibiotic therapies is acute and growing in large part because of the emergence of drug-resistant pathogens. A vast number of resistance determinants are, however, found in nonpathogenic micro-organisms. The resistance totality in the global microbiota is the antibiotic resistome and includes not only established resistance genes but also genes that have the potential to evolve into resistance elements. We term these proto-resistance genes and hypothesize that they share common ancestry with other functional units known as housekeeping genes. Genomic enzymology is the study of protein structure-function in light of genetic context and evolution of protein superfamilies. This concept is highly applicable to study of antibiotic resistance evolution from proto-resistance elements. In this review, we summarize some of the genomic enzymology evidence for resistance enzymes pointing to common ancestry with genes of other metabolic functions. Genomic enzymology plays a key role in understanding the origins of antibiotic resistance and aids in designing strategies for diagnosis and prevention thereof.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1146/annurev-genet-102209-163517 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Genome-Wide Identification and Expression Profile of () Gene Family in L.
Int J Mol Sci
January 2025
State Key Laboratory of Tropical Crop Breeding, Sanya Institute, Rubber Research Institute, Chinese Academy of Tropical Agricultural Sciences, Sanya 572025, China.
The biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), which are essential for sesquiterpenes and triterpenes, respectively, is primarily governed by the mevalonate pathway, wherein () plays a pivotal role. This study identified eight members of the FPS gene family in , designated -, through bioinformatics analysis, revealing their distribution across several chromosomes and a notable tandem gene cluster. The genes exhibited strong hydrophilic properties and key functional motifs crucial for enzyme activity.
View Article and Find Full Text PDFEvidence for the Worldwide Distribution of a Bile Salt Hydrolase Gene in Through Horizontal Gene Transfer.
Int J Mol Sci
January 2025
Bioproduction Research Institute, National Institute of Advanced Industrial Science and Technology, Tsukuba 305-8566, Ibaraki, Japan.
Bile salt hydrolase (BSH), a probiotic-related enzyme with cholesterol-assimilating and anti-hypercholesterolemic abilities, has been isolated from intestinal bacteria; however, BSH activity of bacteria in bile-salt-free (non-intestinal) environments is largely unknown. Here, we aimed to identify BSH from non-intestinal and characterize its enzymatic function. We successfully isolated a plasmid-encoded () from , and the recombinant EfpBSH showed BSH activity that preferentially hydrolyzed taurine-conjugated bile salts, unlike the activity of known BSHs.
View Article and Find Full Text PDFThe Construction of Heterothallic Strains of Using the I-SceI Meganuclease.
Biomolecules
January 2025
National Research Center "Kurchatov Institute", 123182 Moscow, Russia.
The methylotrophic yeast belongs to the group of homothallic fungi that are able to spontaneously change their mating type by inversion of chromosomal DNA in the MAT locus region. As a result, natural and genetically engineered cultures of these yeasts typically contain a mixture of sexually dimorphic cells that are prone to self-diploidisation and spore formation accompanied by genetic rearrangements. These characteristics pose a significant challenge to the development of genetically stable producers for industrial use.
View Article and Find Full Text PDFGenome Mining and Characterization of Two Novel Probiotic Candidates with Bile Salt Hydrolase Activity.
Biomolecules
January 2025
Department of Agriculture, Food and Environment, University of Catania, 95123 Catania, Italy.
Bile salt hydrolase (BSH; EC 3.5.1.
View Article and Find Full Text PDF[Mining and characterization of new enzymes based on Phi29 DNA polymerase].
Sheng Wu Gong Cheng Xue Bao
January 2025
Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin 300308, China.
In recent years, the bacteriophage Φ29 (Phi29) DNA polymerase has garnered increasing attention due to its high-fidelity amplification capacity at constant temperatures. To advance the industrial application of this type of isothermal polymerases, this study mined and characterized new enzymes from the microbial metagenome based on the known Phi29 DNA polymerase sequence. The results revealed that a new enzyme, Php29 DNA polymerase, was identified in the microbial metagenome with plants as the hosts.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!