Ontology highlight
ABSTRACT:
SUBMITTER: Christianson TM
PROVIDER: S-EPMC1133815 | biostudies-literature | 2004 Sep
REPOSITORIES: biostudies-literature
Christianson Terri M TM Starr Chris M CM Zankel Todd C TC
The Biochemical journal 20040901 Pt 2
Arylsulphatases B (ASB) and A (ASA) are subject to a unique post-translational modification that is required for their function. The modification reaction, conversion of an active-site cysteine into a formylglycine, becomes saturated when these enzymes are overexpressed. We have removed the possibility of in vivo modification by expressing mutants of ASB and ASA in which the active-site cysteine is substituted with a serine. These mutants are expressed much more efficiently when compared with th ...[more]