By the same authors

Mechanism, Structure, and Inhibition of O-GlcNAc Processing Enzymes

Research output: Contribution to journalLiterature reviewpeer-review

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Mechanism, Structure, and Inhibition of O-GlcNAc Processing Enzymes. / Gloster, Tracey M.; Vocadlo, David J.

In: CURRENT SIGNAL TRANSDUCTION THERAPY, Vol. 5, No. 1, 01.2010, p. 74-91.

Research output: Contribution to journalLiterature reviewpeer-review

Harvard

Gloster, TM & Vocadlo, DJ 2010, 'Mechanism, Structure, and Inhibition of O-GlcNAc Processing Enzymes', CURRENT SIGNAL TRANSDUCTION THERAPY, vol. 5, no. 1, pp. 74-91.

APA

Gloster, T. M., & Vocadlo, D. J. (2010). Mechanism, Structure, and Inhibition of O-GlcNAc Processing Enzymes. CURRENT SIGNAL TRANSDUCTION THERAPY, 5(1), 74-91.

Vancouver

Gloster TM, Vocadlo DJ. Mechanism, Structure, and Inhibition of O-GlcNAc Processing Enzymes. CURRENT SIGNAL TRANSDUCTION THERAPY. 2010 Jan;5(1):74-91.

Author

Gloster, Tracey M. ; Vocadlo, David J. / Mechanism, Structure, and Inhibition of O-GlcNAc Processing Enzymes. In: CURRENT SIGNAL TRANSDUCTION THERAPY. 2010 ; Vol. 5, No. 1. pp. 74-91.

Bibtex - Download

@article{61e296aaf9f84a1caa3dfe971dd19c7c,
title = "Mechanism, Structure, and Inhibition of O-GlcNAc Processing Enzymes",
abstract = "The post-translational modification of nucleocytoplasmic proteins with O-linked 2-acetamido-2-deoxy-D-glucopyranose (O-GlcNAc) is a topic of considerable interest and attracts a great deal of research effort. O-GlcNAcylation is a dynamic process which can occur multiple times over the lifetime of a protein, sometimes in a reciprocal relationship with phosphorylation. Several hundred proteins, which are involved in a diverse range of cellular processes, have been identified as being modified with the monosaccharide. The control of the O-GlcNAc modification state on different protein targets appears to be important in the aetiology of a number of diseases, including type II diabetes, neurodegenerative diseases and cancer. Two enzymes are responsible for the addition and removal of the O-GlcNAc modification: uridine diphospho-N-acetylglucosamine: polypeptide beta-N-acetylglucosaminyltransferase (OGT) and O-GlcNAcase (OGA), respectively. Over the past decade the volume of information known about these two enzymes has increased significantly. In particular, mechanistic studies of OGA, in conjunction with structural studies of bacterial homologues of OGA have stimulated the design of inhibitors and offered a rationale for the binding of certain potent and selective inhibitors. Mechanistic information about OGT lags a little way behind OGA, but the recent deduction of the structure of an OGT bacterial homologue should now drive these studies forward.",
keywords = "Post-translational modification, O-GlcNAc, O-GlcNAcase, O-GlcNAc transferase, enzyme mechanism, inhibition, three-dimensional structure, BETA-N-ACETYLGLUCOSAMINIDASE, SUBSTRATE-ASSISTED CATALYSIS, TRANSITION-STATE ANALOGS, APOPTOTIC CELL-DEATH, TAY-SACHS-DISEASE, INSULIN-RESISTANCE, LINKED GLCNAC, D-GLUCOSAMINIDASE, HEXOSAMINIDASE-C, TRANSFERASE OGT",
author = "Gloster, {Tracey M.} and Vocadlo, {David J.}",
year = "2010",
month = jan,
language = "English",
volume = "5",
pages = "74--91",
journal = "CURRENT SIGNAL TRANSDUCTION THERAPY",
issn = "1574-3624",
publisher = "Bentham Science Publishers B.V.",
number = "1",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Mechanism, Structure, and Inhibition of O-GlcNAc Processing Enzymes

AU - Gloster, Tracey M.

AU - Vocadlo, David J.

PY - 2010/1

Y1 - 2010/1

N2 - The post-translational modification of nucleocytoplasmic proteins with O-linked 2-acetamido-2-deoxy-D-glucopyranose (O-GlcNAc) is a topic of considerable interest and attracts a great deal of research effort. O-GlcNAcylation is a dynamic process which can occur multiple times over the lifetime of a protein, sometimes in a reciprocal relationship with phosphorylation. Several hundred proteins, which are involved in a diverse range of cellular processes, have been identified as being modified with the monosaccharide. The control of the O-GlcNAc modification state on different protein targets appears to be important in the aetiology of a number of diseases, including type II diabetes, neurodegenerative diseases and cancer. Two enzymes are responsible for the addition and removal of the O-GlcNAc modification: uridine diphospho-N-acetylglucosamine: polypeptide beta-N-acetylglucosaminyltransferase (OGT) and O-GlcNAcase (OGA), respectively. Over the past decade the volume of information known about these two enzymes has increased significantly. In particular, mechanistic studies of OGA, in conjunction with structural studies of bacterial homologues of OGA have stimulated the design of inhibitors and offered a rationale for the binding of certain potent and selective inhibitors. Mechanistic information about OGT lags a little way behind OGA, but the recent deduction of the structure of an OGT bacterial homologue should now drive these studies forward.

AB - The post-translational modification of nucleocytoplasmic proteins with O-linked 2-acetamido-2-deoxy-D-glucopyranose (O-GlcNAc) is a topic of considerable interest and attracts a great deal of research effort. O-GlcNAcylation is a dynamic process which can occur multiple times over the lifetime of a protein, sometimes in a reciprocal relationship with phosphorylation. Several hundred proteins, which are involved in a diverse range of cellular processes, have been identified as being modified with the monosaccharide. The control of the O-GlcNAc modification state on different protein targets appears to be important in the aetiology of a number of diseases, including type II diabetes, neurodegenerative diseases and cancer. Two enzymes are responsible for the addition and removal of the O-GlcNAc modification: uridine diphospho-N-acetylglucosamine: polypeptide beta-N-acetylglucosaminyltransferase (OGT) and O-GlcNAcase (OGA), respectively. Over the past decade the volume of information known about these two enzymes has increased significantly. In particular, mechanistic studies of OGA, in conjunction with structural studies of bacterial homologues of OGA have stimulated the design of inhibitors and offered a rationale for the binding of certain potent and selective inhibitors. Mechanistic information about OGT lags a little way behind OGA, but the recent deduction of the structure of an OGT bacterial homologue should now drive these studies forward.

KW - Post-translational modification

KW - O-GlcNAc

KW - O-GlcNAcase

KW - O-GlcNAc transferase

KW - enzyme mechanism

KW - inhibition

KW - three-dimensional structure

KW - BETA-N-ACETYLGLUCOSAMINIDASE

KW - SUBSTRATE-ASSISTED CATALYSIS

KW - TRANSITION-STATE ANALOGS

KW - APOPTOTIC CELL-DEATH

KW - TAY-SACHS-DISEASE

KW - INSULIN-RESISTANCE

KW - LINKED GLCNAC

KW - D-GLUCOSAMINIDASE

KW - HEXOSAMINIDASE-C

KW - TRANSFERASE OGT

UR - http://www.scopus.com/inward/record.url?scp=77951935988&partnerID=8YFLogxK

M3 - Literature review

VL - 5

SP - 74

EP - 91

JO - CURRENT SIGNAL TRANSDUCTION THERAPY

JF - CURRENT SIGNAL TRANSDUCTION THERAPY

SN - 1574-3624

IS - 1

ER -