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Subunit interaction of monomeric alanine racemases from four Shigella species in catalytic reaction by Kumio Yokoigawa; Yoko Okubo; Kenji Soda is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.
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Bacterial alanine racemases are classified into two types of subunit structure (monomer and homodimer). To clarify the catalytic unit of monomeric alanine racemases, we examined the apparent molecular mass of the monomeric alanine racemases from Shigella dysenteriae, Shigella boydii, Shigella flexneri, and Shigella sonnei by gel filtration in the presence of the substrate and inhibitor. The enzymes were eluted on gel filtration as a monomer of about 39,000 Da at low protein concentration and in the absence of L-alanine and D-cycloserine. An increase in the apparent molecular mass was induced by increasing the protein concentration or by adding the ligands in the elution buffer. The increase ratio depended on the ligand concentration, and the maximum apparent molecular masses of all enzymes were 60,000 and 76,000 Da in the presence of 100 mM L-alanine and 5 mM D-cycloserine, respectively. D-cycloserine may induce an inactive dimer and L-alanine may induce an intermediate between the monomer and dimer because of dynamic equilibrium. The apoenzyme also showed similar behavior in the presence of the ligands, but the increase ratios were lower than those of the holoenzymes. The Bacillus
Who reads Subunit interaction of monomeric alanine racemases from four Shigella species in catalytic reaction?
It is typically read by researchers, students, and practitioners in Biochemistry, Genetics and Molecular Biology.
- Author
- Kumio Yokoigawa; Yoko Okubo; Kenji Soda
- Publisher
- John Wiley and Sons; Oxford University Press; Oxford University Press (OUP); Elsevier BV (ISSN 0378-1097)
- Published
- 2003
- Language
- EN
- Field
- Biochemistry, Genetics and Molecular Biology (Life Sciences)