ArticleBioinformation2013
Molecular characterization of α-amylase from Staphylococcus aureus.
Article in Bioinformation, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 33 citations in OpenAlex.
- Key Salivary Proteins Implicated in the Inhibition of Staphylococcus Aureus Biofilms by Chlorogenic Acid.European journal of dentistry · 2026Article
- Characterization of aroma profile and microbial community of cigar tobacco leaves from different aging periods and varieties and their correlations analysis.Bioresources and bioprocessing · 2025Article
- Characterization of aroma profiles and microbial communities of cigar tobacco leaves from different varieties and origins and their correlations analysis.Scientific reports · 2025Article
- The Impact of Antibiofilm Strategies in Controlling Microbial Colonization.Current microbiology · 2025Review
- Activity-Based Protein Profiling Identifies an α-Amylase Family Protein Contributing to the Virulence of Methicillin-ResistantACS infectious diseases · 2025Article
- Integrated metagenomics and metabolomics analysis reveals dynamic changes of microbiota and metabolic profile during fermentation of cigar tobacco (Frontiers in genetics · 2025Article
- Thymoquinone/β-Frontiers in cellular and infection microbiology · 2025Article
- Isolation and characterization of methicillin-resistant Staphylococcus aureus from bovine mastitis in North West Cameroon: public health implications.BMC research notes · 2024Article
- Vaginal community state types (CSTs) alter environmental cues and production of theJournal of bacteriology · 2024Article
- Oxygen regulation of microbial communities and chemical compounds in cigar tobacco curing.Frontiers in microbiology · 2024Article
- Multi-omics reveals the phyllosphere microbial community and material transformations in cigars.Frontiers in microbiology · 2024Article
- Detection of Methicillin-ResistantFoods (Basel, Switzerland) · 2023Article
- Development ofFrontiers in microbiology · 2023Article
- Virulence Potential and Antibiotic Susceptibility ofMicroorganisms · 2022Article
- Comparative structural and functional analysis of the PGU1 protein fromBioinformation · 2022Article
- Article
- Comparative study of virulence factors among methicillin resistant Staphylococcus aureus clinical isolates.BMC infectious diseases · 2018Article
- Thermal adaptation of α-amylases: a review.Extremophiles : life under extreme conditions · 2014Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Staphylococcus aureus is one of the prominent Gram positive human pathogen secretes many surface and secretary proteins including various enzymes and pathogenic factors that favour the successful colonization and infection of host tissue. α-amylase is one of the enzymes secreted by S. aureus which catalyses the breakdown of complex sugars to monosaccharides, which are required for colonization and survival of this pathogen in any anatomical locales. In the present study we have cloned, sequenced, expressed and characterized α-amylase gene from S. aureus ATCC12600. The recombinant enzyme has a molecular weight of 58kDa and the kinetics showed Vmax 0.0208±0.033 (mg/ml)/mg/min and Km 10.633±0.737mg/ml. The multiple sequence analysis showed α- amylase of S. aureus exhibited large differences with Bacillus subtilis and Streptococcus bovis. As the crystal structure of S. aureus α- amylase was unavailable, we used homology modelling method to build the structure. The built structure was validated by Ramachandran plot which showed 90% of the residues in the allowed region while no residue was found in the disallowed region and the built structure was close to the crystal structure with Z-Score: -6.85. The structural superimposition studies with α- amylases of Bacillus subtilis and Streptococcus bovis showed distinct differences with RMSD values of 18.158Åand 7.091Å respectively which correlated with enzyme kinetics, indicating α-amylase is different among these bacteria.
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