Neomycin Sensitivity in the

Patrick, Judith

doi:10.1001/archderm.1970.04000110048008

Cited by 19 publications

(1 citation statement)

References 11 publications

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“…MUGlc, pNPG) (Dance et al, 1969;Glew et al, 1976;Peters et al, 1976). The lysosomal fl-glucosidase, glucocerebrosidase, is the deficient enzyme in Gaucher's disease, and its role in the degradation of glucocerebroside has been firmly established (Patrick, 1965;Brady et al, 1965). The second, non-lysosomal, fl-glucosidase is actually a broad-specificity ,1-glycosidase with no known function (Daniels et al, 1981).…”

Section: Introductionmentioning

confidence: 99%

Hydrolysis of a naturally occurring β-glucoside by a broad-specificity β-glucosidase from liver

LaMarco¹,

Glew²

1986

Biochemical Journal

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We have isolated from guinea-pig liver a broad-specificity beta-glucosidase of unknown function that utilizes as its substrate non-physiological aryl glycosides (e.g. 4-methylumbelliferyl beta-D-glucopyranoside, p-nitrophenyl beta-D-glucopyranoside). The present paper documents that this enzyme can be inhibited by various naturally occurring glycosides, including L-picein, dhurrin and glucocheirolin. In addition, L-picein, which acts as a competitive inhibitor of the broad-specificity beta-glucosidase (Ki 0.65 mM), is also a substrate for this enzyme (Km 0.63 mM; Vmax. 277,000 units/mg). Heat-denaturation, kinetic competition studies, chromatographic properties and pH optima all argue strongly that the broad-specificity beta-glucosidase is responsible for the hydrolysis of both the non-physiological aryl glycosides and L-picein. This paper demonstrates that beta-glucosidase can catalyse the hydrolysis of a natural glycoside, and may provide a key to understanding the function of this enigmatic enzyme. A possible role in the metabolism of xenobiotic compounds is discussed.

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