title: Purification and characterization of trehalose phosphorylase from Catellatospora ferruginea.
abstract: Trehalose phosphorylase was purified from the cell extracts of Catellatospora ferruginea. The enzyme had an apparent molecular weight of 400,000 by gel filtration and 98,000 by SDS-PAGE, suggesting that the enzyme was a tetramer. The enzyme was specific for trehalose in phosphorolysis and specific for beta-D-glucose 1-phosphate in synthesis. In addition to D-glucose, D-xylose and D-fucose were also possible sugar acceptors during synthesis. Phosphate ions were a key to the activity and stability of the enzyme, controlling the equilibrium of the reversible reaction and the heat stability of the enzyme. The enzyme was strongly inhibited by p-chloromercuribenzoate and pyridoxal phosphate. The enzyme was inactivated by heat or by storage frozen with ammonium chloride and lithium chloride.
authors.affiliation: Tokyo Research Laboratories, Kyowa Hakko Kogyo Co., Ltd., Japan.
authors.forename: K
authors.initials: K
authors.lastname: Aisaka
authors.forename: T
authors.initials: T
authors.lastname: Masuda
authors.forename: T
authors.initials: T
authors.lastname: Chikamune
authors.forename: K
authors.initials: K
authors.lastname: Kamitori
mesh_terms: D000191:Actinomycetaceae / Q000201:enzymology*; D000595:Amino Acid Sequence; D002412:Cations / Q000494:pharmacology; D003470:Culture Media; D005656:Fungal Proteins / Q000032:analysis / Q000302:isolation & purification; D005964:Glucosyltransferases / Q000737:chemistry / Q000302:isolation & purification*; D006863:Hydrogen-Ion Concentration; D007525:Isoelectric Focusing; D008969:Molecular Sequence Data; D008970:Molecular Weight; D013379:Substrate Specificity; D013696:Temperature
chemical_list: D002412:Cations; D003470:Culture Media; D005656:Fungal Proteins; D005964:Glucosyltransferases; C023181:alpha,alpha-trehalose phosphorylase