ArticleActa crystallographica. Section D, Biological crystallography2012
Structural features and kinetic characterization of alanine racemase from Staphylococcus aureus (Mu50).
Article in Acta crystallographica. Section D, Biological crystallography, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
16 citing papers in PubMed, 25 citations in OpenAlex.
- D-alanine synthesis and exogenous alanine affect the antimicrobial susceptibility ofAntimicrobial agents and chemotherapy · 2025Article
- Nitrate Reductase NarGHJI Modulates Virulence via Regulation ofMicrobiology spectrum · 2023Article
- Assembly of Peptidoglycan Fragments-A Synthetic Challenge.Pharmaceuticals (Basel, Switzerland) · 2020Review
- Purification, Characterization and Inhibition of Alanine Racemase from a Pathogenic Strain ofPolish journal of microbiology · 2019Article
- Mining the cellular inventory of pyridoxal phosphate-dependent enzymes with functionalized cofactor mimics.Nature chemistry · 2018Article
- Function of alanine racemase in the physiological activity and cariogenicity of Streptococcus mutans.Scientific reports · 2018Article
- A D-Alanine auxotrophic live vaccine is effective against lethal infection caused by Staphylococcus aureus.Virulence · 2018Article
- Selection and characterization of alanine racemase inhibitors against Aeromonas hydrophila.BMC microbiology · 2017Article
- Mechanistic and Evolutionary Insights from the Reciprocal Promiscuity of Two Pyridoxal Phosphate-dependent Enzymes.The Journal of biological chemistry · 2016Article
- Characterization of Lactobacillus salivarius alanine racemase: short-chain carboxylate-activation and the role of A131.SpringerPlus · 2015Article
- The structure of alanine racemase from Acinetobacter baumannii.Acta crystallographica. Section F, Structural biology communications · 2014Article
- Structural and biochemical analyses of alanine racemase from the multidrug-resistant Clostridium difficile strain 630.Acta crystallographica. Section D, Biological crystallography · 2014Article
- Characterization and preliminary mutation analysis of a thermostable alanine racemase from Thermoanaerobacter tengcongensis MB4.Extremophiles : life under extreme conditions · 2013Article
- Crystallization and preliminary X-ray study of a thermostable alanine racemase from Thermoanaerobacter tengcongensis MB4.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- Structure of alanine racemase from Oenococcus oeni with bound pyridoxal 5'-phosphate.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- Crystallization and preliminary X-ray diffraction analysis of alanine racemase from Pseudomonas putida YZ-26.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Staphylococcus aureus is an opportunistic Gram-positive bacterium which causes a wide variety of diseases ranging from minor skin infections to potentially fatal conditions such as pneumonia, meningitis and septicaemia. The pathogen is a leading cause of nosocomial acquired infections, a problem that is exacerbated by the existence of methicillin- and glycopeptide antibiotic-resistant strains which can be challenging to treat. Alanine racemase (Alr) is a pyridoxal-5'-phosphate-dependent enzyme which catalyzes reversible racemization between enantiomers of alanine. As D-alanine is an essential component of the bacterial cell-wall peptidoglycan, inhibition of Alr is lethal to prokaryotes. Additionally, while ubiquitous amongst bacteria, this enzyme is absent in humans and most eukaryotes, making it an excellent antibiotic drug target. The crystal structure of S. aureus alanine racemase (Alr(Sas)), the sequence of which corresponds to that from the highly antibiotic-resistant Mu50 strain, has been solved to 2.15 Å resolution. Comparison of the Alr(Sas) structure with those of various alanine racemases demonstrates a conserved overall fold, with the enzyme sharing most similarity to those from other Gram-positive bacteria. Structural examination indicates that the active-site binding pocket, dimer interface and active-site entryway of the enzyme are potential targets for structure-aided inhibitor design. Kinetic constants were calculated in this study and are reported here. The potential for a disulfide bond in this structure is noted. This structural and biochemical information provides a template for future structure-based drug-development efforts targeting Alr(Sas).
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