Purification, Characterization and Inhibition of Alanine Racemase from a Pathogenic Strain of Streptococcus iniae

  title={Purification, Characterization and Inhibition of Alanine Racemase from a Pathogenic Strain of Streptococcus iniae},
  author={M. Muhammad and Yangyang Li and Siyu Gong and Yanmin Shi and J. Ju and Baohua Zhao and D. Liu},
  journal={Polish Journal of Microbiology},
  pages={331 - 341}
Abstract Streptococcus iniae is a pathogenic and zoonotic bacteria that impacted high mortality to many fish species as well as capable of causing serious disease to humans. Alanine racemase (Alr, EC is a pyridoxal-5’-phosphate (PLP)-containing homodimeric enzyme that catalyzes the racemization of L-alanine and D-alanine. In this study, we purified alanine racemase from S. iniae that was isolated from an infected Chinese sturgeon (Acipenser sinensis), as well as determined its… Expand
Significance of Glutamate Racemase for the Viability and Cell Wall Integrity of Streptococcus iniae
It is demonstrated that the MurI knockout leads to the generation of S. iniae auxotroph with damaged cell walls, and the mutant lost its virulence when incubated in fish blood. Expand
Homology Modeling of Bifunctional Enzyme Alanine Racemase from Taibaiella Chishuiensis
Alanine Racemase from Taibaiella chishuiensis bacteria is one of the bifunctional enzymes that catalyze the Land D-alanine racemization of peptidoglycan biosynthesis in bacteria and ligationExpand


Structural and functional characterization of the alanine racemase from Streptomyces coelicolor A3(2).
An alr deletion mutant of S. coelicolor which depends on D-Ala for growth and shows increased sensitivity to the antibiotic d-cycloserine (DCS), and the crystal structures revealed that Alr is a homodimer with residues from both monomers contributing to the active site. Expand
Biochemical and structural characterization of alanine racemase from Bacillus anthracis (Ames)
The chloride ion is functioning effectively as a carbamylated lysine making it an integral and unique part of this structure, 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. Expand
Biochemical characteristics of an alanine racemase from Aeromonas hydrophil HBNUAh01
The alanine racemase was shown to belong to the pyridoxal 5′-phosphate (PLP)-dependent family of enzymes that require a certain concentration of PLP for activity. Expand
Purification of an alanine racemase from Streptococcus faecalis and analysis of its inactivation by (1-aminoethyl)phosphonic acid enantiomers.
Enzymic activation and processing as the basis for irreversible inhibition is ruled out and enzyme after exposure to [14C]Ala-P or [alpha-3H]AlA-P and gel filtration contains stoichiometric amounts of radioactive label, but denaturation quantitatively releases intact Ala-P into solution as revealed by high-performance liquid chromatography and cocrystallization with authentic material. Expand
Purification and preliminary crystallization of alanine racemase from Streptococcus pneumoniae
The alanine racemase gene from the opportunistic human pathogen S. pneumoniae is isolated and characterized and shows sufficient homology with other alanines racemases to allow its integration into the ongoing structure-based drug design project. Expand
Thermolabile alanine racemase from a psychotroph, Pseudomonas fluorescens: purification and properties.
The enzyme is extremely labile over 30 degrees C, and shows the high catalytic activity even at 0 degrees C; it is thermolabile and psychotrophic. Expand
Characterization of endogenous pyridoxal 5'-phosphate-dependent alanine racemase from Bacillus pseudofirmus OF4.
An open reading frame of 1100 bp in the partially sequenced genome sequence of alkaliphilic Bacillus pseudofirmus OF4 was identified as a putative alanine racemase gene (dadX(OF4)), which was clonedExpand
Alanine racemase is essential for the growth and interspecies competitiveness of Streptococcus mutans
It is found that alr deletion was lethal to S. mutans and may represent a promising target to modulate the cariogenicity of oral biofilms and to benefit the management of dental caries. Expand
Alanine Racemase from an Acidophile, Acidiphilium organovorum: Purification and Characterization.
An alanine racemase (EC 5.1.1) from an acidophilic heterotrophic bacterium, Acidiphilium organovorum 13H, was purified and characterized, finding that 1 mole of enzyme contained 2 moles of PLP. Expand
Mycobacterium smegmatis d-Alanine Racemase Mutants Are Not Dependent on d-Alanine for Growth
The viability of the mutants and independence of d-alanine for growth indicate that inactivation of alrA does not impose an auxotrophic requirement for d-Alanine, suggesting the existence of a new pathway of d -alanine biosynthesis in M. smegmatis. Expand