Molecular properties of lysine-2,3-aminomutase.

摘要: Lysine-2,3-aminomutase purified from Clostridium subterminale SB4 is reported to exhibit an apparent subunit Mr of 48,000, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and the undenatured enzyme exhibits 285,000, electrophoretic mobility permeation chromatography (Chirpich, T. P., Zappia, V., Costilow, R. N., Barker, H. A. (1970) J. Biol. Chem. 245, 1778-1789). The diffusion coefficient 3.36 x 10(-7) cm2/s, quasielastic light scattering. overall calculated published sedimentation 259,000. Cross-linking experiments using glutaraldehyde dithiobis(succinimidylpropionate) cross-linking reagents indicate that has a hexameric quaternary structure. number major cyanogen bromide peptides, compared with methionine content enzyme, consistent subunits being identical, isoelectric focusing also identical subunits. circular dichroism indicates it highly ordered structure, which estimated consist 26% alpha-helix 48% beta-sheet. contains approximately six molecules pyridoxal 5'-phosphate per hexamer, phenyl-hydrazine method. amino acid analysis after performic oxidation, 13 cysteine residues subunit. Six sulfhydryl groups hexamer react readily 5,5'-dithiobis-2-nitrobenzoate, indicating one group accessible