Chapter 3 The GlcNAc-PI de-N-acetylase. Structure, function, and activity

Urbaniak, Michael D. and Ferguson, Michael A J (2009) Chapter 3 The GlcNAc-PI de-N-acetylase. Structure, function, and activity. Enzymes, 26 (C). pp. 49-64. ISSN 1874-6047

Full text not available from this repository.

Abstract

The N-acetylglucosamine phosphatidylinositol (GlcNAc-PI) de-. N-acetylase catalyzes the removal of the N-acetyl group from GlcNAc-PI in the second step of GPI biosynthesis. The GlcNAc-PI de-. N-acetylase is a 252-residue integral membrane protein containing a single N-terminal membrane spanning domain, with the majority of the protein on the cytoplasmic face of the ER. Site-directed mutagenesis studies have lead to the proposal of a zinc-dependent mechanism of action analogous to zinc peptidases. The activity of the GlcNAc-PI de-. N-acetylase can be measured both in vivo and in vitro, and active recombinant protein has been obtained. The enzyme is a potential drug target for the treatment of African sleeping sickness, and differences in substrate recognition and channeling between mammalian and trypanosomal enzymes have been exploited to produce species-specific inhibitors.

Item Type:
Journal Article
Journal or Publication Title:
Enzymes
Uncontrolled Keywords:
/dk/atira/pure/subjectarea/asjc/1300/1303
Subjects:
?? biochemistrybiotechnologybiophysicsmolecular biology ??
ID Code:
129154
Deposited By:
Deposited On:
27 Nov 2018 11:30
Refereed?:
Yes
Published?:
Published
Last Modified:
17 Sep 2024 14:15