Journal ArticleDOI
Efficient synthesis of a nucleoside-diphospho-exo-glycal displaying time-dependent inactivation of UDP-galactopyranose mutase
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TLDR
In this article, a short and efficient synthesis of UDP-exo-galactofuranosyl-glycal was presented, which displayed an interesting time-dependent inactivation of UDP -galactopyranose mutase, an essential enzyme of the mycobacterial cell wall biosynthesis.About:
This article is published in Chemical Communications.The article was published on 2004-05-10. It has received 39 citations till now. The article focuses on the topics: Mutase & Glycal.read more
Citations
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Journal ArticleDOI
Chemistry and biology of galactofuranose-containing polysaccharides.
TL;DR: Recent advances both in the understanding of the mechanism of UGM and in the synthesis of galactofuranose and its derivatives are highlighted in this review.
Journal ArticleDOI
Recent knowledge and innovations related to hexofuranosides: structure, synthesis and applications
TL;DR: This review will first focus on the structure of the oligosaccharidic part of hexofuranosyl conjugates found in natural sources, and original syntheses will be presented, stressing more particularly on the development of chemical and chemo-enzymatic tools for the access to 1,2-trans or 1, 2-cis linkages.
PatentDOI
Inhibitors of udp-galactopyranose mutase thwart mycobacterial growth
TL;DR: In this paper, the authors proposed compounds which inhibit UDP-galactopyranose mutase (UGM) and have activity as inhibitors of microbial growth of microorganisms which contain this enzyme and particularly those microorganisms in which this enzyme is responsible for the incorporation of galactofuranose residues.
Journal ArticleDOI
A new methodology for the synthesis of fluorinated exo-glycals and their time-dependent inhibition of UDP-galactopyranose mutase.
TL;DR: The two diastereomeric molecules were found to display time-dependent inactivation of UGM, as expected from preliminary results using non-fluorinated exo-glycal nucleotides, and it is suggested that the inactivation mechanism proceeds through two-electron processes, despite the presence of the flavin cofactor within the UGM catalytic site.
Journal ArticleDOI
Synthesis and biological evaluation of new inhibitors of UDP-Galf transferase--a key enzyme in M. tuberculosis cell wall biosynthesis.
TL;DR: Two iminosugars have been designed and synthesized as potential inhibitors of UDP-Galf transferase, an enzyme involved in Mycobacterium tuberculosis cell wall biosynthesis and one of the two racemic compounds is the first reported inhibitor of the target enzyme from M. smegmatis.
References
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Journal ArticleDOI
Trypanosoma cruzi Trans-sialidase Operates through a Covalent Sialyl−Enzyme Intermediate: Tyrosine Is the Catalytic Nucleophile
Andrew G. Watts,Iben Damager,Maria L. Amaya,Alejandro Buschiazzo,Pedro M. Alzari,and Alberto C. Frasch,Stephen G. Withers +6 more
TL;DR: Modified sialic acid substrates have been used to label Trypanosoma cruzi trans-sialidase, demonstrating that the enzyme catalyses the transfer of sIALic acid through a covalent glycosyl-enzyme intermediate, a mechanism common to most retaining glycosidases.
Journal ArticleDOI
Cell Wall Core Galactofuran Synthesis Is Essential for Growth of Mycobacteria
TL;DR: It is demonstrated here that glf can be knocked out in Mycobacterium smegmatis by allelic replacement only in the presence of two rescue plasmids carrying functional copies of glf and Rv3808c, which supports the development of UDP-galactopyranose mutase and galactofuranosyl transferase as important targets for theDevelopment of new antituberculosis drugs.
Journal ArticleDOI
Mechanisms of glycosyl transferases and hydrolases
TL;DR: Three-dimensional structures of several of these glycosyl–enzyme complexes, along with those of Michaelis complexes, have been determined through X-ray crystallographic analysis, revealing the identities of important amino acid residues involved in catalysis.
Journal ArticleDOI
UDP-galactopyranose mutase has a novel structure and mechanism.
David A. R. Sanders,Adam G. Staines,Stephen A. McMahon,Stephen A. McMahon,Michael R. McNeil,Chris Whitfield,James H. Naismith +6 more
TL;DR: The crystal structure of Escherichia coli mutase is solved and it is concluded that mutase most likely functions by transient reduction of substrate.
Journal ArticleDOI
Flavoenzymes that catalyse reactions with no net redox change.
TL;DR: This review covers unusual flavoenzymes that catalyse reactions with no net redox change and whether the flavin has a redox role in some other flavoproteins is not yet clear.
Related Papers (5)
Cell Wall Core Galactofuran Synthesis Is Essential for Growth of Mycobacteria
Mechanistic investigation of UDP-galactopyranose mutase from Escherichia coli using 2- and 3-fluorinated UDP-galactofuranose as probes.
Qibo Zhang,Hung-wen Liu +1 more