Heparan N-sulfatase: Cysteine 70 plays a role in the enzyme catalysis and processing

9Citations
Citations of this article
9Readers
Mendeley users who have this article in their library.

Abstract

Sulfatases are members of a highly conserved family of enzymes that catalyze the hydrolysis of sulfate ester bonds from a variety of substrates. The functional correlation reflects a high degree of amino acid sequence similarity along the entire length, in particular in the active site where the C(X)PSR consensus sequence is present. Cysteine undergoes an important co- or post-translation modification essential for the accomplishment of catalytic activity: conversion in formylglycine. In this work, the cysteine of heparan N-sulfatase (NS) was replaced either by a serine (C70S) or by a methionine (C70M) using site-directed mutagenesis. C70S and C70M mutant cDNAs were expressed and analyzed in COS cells; both mutations caused a loss of NS activity; however, while C70S showed a normal precursor form undergoing processing to a reduced mature form within the lysosomes, C70M was poorly synthesized and formed a complex with the molecular chaperone immunoglobulin binding protein. © 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

Cite

CITATION STYLE

APA

Daniele, A., & Di Natale, P. (2001). Heparan N-sulfatase: Cysteine 70 plays a role in the enzyme catalysis and processing. FEBS Letters, 505(3), 445–448. https://doi.org/10.1016/S0014-5793(01)02867-8

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free