Abstract

UDP-Galactopyranose mutase (UGM) is a unique flavin-dependent enzyme that catalyzes the conversion of UDPgalactopyranose (UDP-Galp) to UDP-galactofuranose (UDP-Galf). The product of this reaction is the precursor to Galf, a major component of the cell wall and of cell surface glycoproteins and glycolipids in many eukaryotic and prokaryotic human pathogens. The function of UGM is important in the virulence of fungi, parasites, and bacteria. Its role in virulence and its absence in humans suggest that UGM is an ideal drug target. Significant structural and mechanistic information has been accumulated on the prokaryotic UGMs; however, in the past few years the research interest has shifted to UGMs from eukaryotic human pathogens such as fungi and protozoan parasites. It has become clear that UGMs from prokaryotic and eukaryotic organisms have different structural and mechanistic features. The amino acid sequence identity between these two classes of enzymes is low, resulting in differences in oligomeric states, substrate binding, active site flexibility, and interaction with redox partners. However, the unique role of the flavin cofactor in catalysis is conserved among this enzyme family. In this review, recent findings on eukaryotic UGMs are discussed and presented in comparison with prokaryotic UGMs. © 2013 Bentham Science Publishers.

Department(s)

Chemistry

Comments

National Institute of General Medical Sciences, Grant R01GM094469

Keywords and Phrases

Enzyme drug target; Eukaryotic pathogens; Flavoenzyme; Galactofuranose; Galactopyranose; Inhibitors; Non-redox reaction; UDP-galactopyranose mutase

International Standard Serial Number (ISSN)

1873-4286; 1381-6128

Document Type

Article - Journal

Document Version

Citation

File Type

text

Language(s)

English

Rights

© 2024 Bentham Science Publishers, All rights reserved.

Publication Date

21 May 2013

PubMed ID

23116395

Download

Full Text Link

Included in

Chemistry Commons

Share

 
COinS