ArticleBMC structural biology2009
Biochemical and structural characterization of alanine racemase from Bacillus anthracis (Ames).
Article in BMC structural biology, 2009. 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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16 citing papers in PubMed, 32 citations in OpenAlex.
- Exploring the reaction dynamics of alanine racemase using serial femtosecond crystallography.Scientific reports · 2024Article
- Biofilm formation displays intrinsic offensive and defensive features ofNPJ biofilms and microbiomes · 2020Article
- Purification, Characterization and Inhibition of Alanine Racemase from a Pathogenic Strain ofPolish journal of microbiology · 2019Article
- Function of alanine racemase in the physiological activity and cariogenicity of Streptococcus mutans.Scientific reports · 2018Article
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- 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
- Structural basis for the broad specificity of a new family of amino-acid racemases.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
- Structural features and kinetic characterization of alanine racemase from Staphylococcus aureus (Mu50).Acta crystallographica. Section D, Biological crystallography · 2012Article
- Crystal structure of a zinc-dependent D-serine dehydratase from chicken kidney.The Journal of biological chemistry · 2011Article
- The crystal structure of alanine racemase from Streptococcus pneumoniae, a target for structure-based drug design.BMC microbiology · 2011Article
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5 authors at 3 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
backgroundBacillus anthracis is the causative agent of anthrax and a potential bioterrorism threat. Here we report the biochemical and structural characterization of B. anthracis (Ames) alanine racemase (AlrBax), an essential enzyme in prokaryotes and a target for antimicrobial drug development. We also compare the native AlrBax structure to a recently reported structure of the same enzyme obtained through reductive lysine methylation.
resultsB. anthracis has two open reading frames encoding for putative alanine racemases. We show that only one, dal1, is able to complement a D-alanine auxotrophic strain of E. coli. Purified Dal1, which we term AlrBax, is shown to be a dimer in solution by dynamic light scattering and has a Vmax for racemization (L- to D-alanine) of 101 U/mg. The crystal structure of unmodified AlrBax is reported here to 1.95 A resolution. Despite the overall similarity of the fold to other alanine racemases, AlrBax makes use of a chloride ion to position key active site residues for catalysis, a feature not yet observed for this enzyme in other species. Crystal contacts are more extensive in the methylated structure compared to the unmethylated structure.
conclusionThe chloride ion in AlrBax is functioning effectively as a carbamylated lysine making it an integral and unique part of this structure. Despite differences in space group and crystal form, the two AlrBax structures are very similar, supporting the case that reductive methylation is a valid rescue strategy for proteins recalcitrant to crystallization, and does not, in this case, result in artifacts in the tertiary structure.
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