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

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Chapter 3 The GlcNAc-PI de-N-acetylase. Structure, function, and activity. / Urbaniak, Michael D.; Ferguson, Michael A J.
In: Enzymes, Vol. 26, No. C, 01.12.2009, p. 49-64.

Research output: Contribution to Journal/Magazine › Review article › peer-review

Harvard

Urbaniak, MD & Ferguson, MAJ 2009, 'Chapter 3 The GlcNAc-PI de-N-acetylase. Structure, function, and activity', Enzymes, vol. 26, no. C, pp. 49-64. https://doi.org/10.1016/S1874-6047(09)26003-3

APA

Urbaniak, M. D., & Ferguson, M. A. J. (2009). Chapter 3 The GlcNAc-PI de-N-acetylase. Structure, function, and activity. Enzymes, 26(C), 49-64. https://doi.org/10.1016/S1874-6047(09)26003-3

Vancouver

Urbaniak MD, Ferguson MAJ. Chapter 3 The GlcNAc-PI de-N-acetylase. Structure, function, and activity. Enzymes. 2009 Dec 1;26(C):49-64. doi: 10.1016/S1874-6047(09)26003-3

Author

Urbaniak, Michael D. ; Ferguson, Michael A J. / Chapter 3 The GlcNAc-PI de-N-acetylase. Structure, function, and activity. In: Enzymes. 2009 ; Vol. 26, No. C. pp. 49-64.

Bibtex

@article{4ebead0b6ad04412b25991a54fdeef5a,
title = "Chapter 3 The GlcNAc-PI de-N-acetylase. Structure, function, and activity",
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.",
author = "Urbaniak, {Michael D.} and Ferguson, {Michael A J}",
year = "2009",
month = dec,
day = "1",
doi = "10.1016/S1874-6047(09)26003-3",
language = "English",
volume = "26",
pages = "49--64",
journal = "Enzymes",
issn = "1874-6047",
publisher = "Academic Press Inc.",
number = "C",

}

RIS

TY - JOUR

T1 - Chapter 3 The GlcNAc-PI de-N-acetylase. Structure, function, and activity

AU - Urbaniak, Michael D.

AU - Ferguson, Michael A J

PY - 2009/12/1

Y1 - 2009/12/1

N2 - 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.

AB - 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.

U2 - 10.1016/S1874-6047(09)26003-3

DO - 10.1016/S1874-6047(09)26003-3

M3 - Review article

AN - SCOPUS:77954838969

VL - 26

SP - 49

EP - 64

JO - Enzymes

JF - Enzymes

SN - 1874-6047

IS - C

ER -