Inhibition of glycosyltransferases by bis-(p-nitrophenyl)phosphate: general effect and relation to their membrane integration.

doi:10.1016/S0300-9084(83)80106-0

Paper

Inhibition of glycosyltransferases by bis-(p-nitrophenyl)phosphate: general effect and relation to their membrane integration.

Published Nov 26, 1983 · F. Guette, R. Cacan, J. Montreuil

Biochimie

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Abstract

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In Vitro Study

Study Snapshot

Bis-(p-nitrophenyl)phosphate is a common inhibitor of glycosyltransferases, with its effect varying depending on the enzyme's membrane integration and accessibility to the active site.

PopulationOlder adults (50-71 years)

Sample size24

MethodsObservational

OutcomesBody Mass Index projections

ResultsSocial networks mitigate obesity in older groups.

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Paper

Inhibition of glycosyltransferases by bis-(p-nitrophenyl)phosphate: general effect and relation to their membrane integration.

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References

Developmental alterations in guanine nucleotide regulation of the beta-adrenergic receptor-adenylate cyclase system of skeletal muscle.

The development of catecholamine-sensitive cAMP synthesis in muscle is governed by coordinated expression of adenylate cyclase regulatory and catalytic proteins, but not the beta-receptor.

Effect of bis-(p-nitrophenyl) phosphate on the biosynthesis and the utilization of lipid-intermediates.

Bis-(p-nitrophenyl) phosphate strongly inhibits reactions involving dolichyl diphosphate sugar as substrate in the dolichol pathway, affecting only those involving N-glycosylation of proteins.

Human erythrocyte galactosyltransferase. Characterization, membrane association and sidedness of active site.

Human erythrocyte galactosyltransferase is membrane-bound and has a substrate-inaccessible active site in the membrane, with cytosolic orientation.

Inhibition of lipid-linked oligosaccharide synthesis by aryl phosphates.

Phenyl phosphate inhibits lipid-linked oligosaccharide synthesis in rat liver microsomal fractions, potentially due to its direct effect on Dol-P-Man synthesis.

Inhibitors of protein glycosylation

Sugar analogues and antibioies can inhibit protein glycosylation, providing valuable tools in glycoprotein research.

Citations