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2-fluoro-deoxy-UDP-galactopyranose
2-fluoro-deoxy-UDP-galactofuranose
-
-
-
?
UDP-(6-deoxy-6-fluoro)-D-galactofuranose
?
-
-
-
-
?
UDP-(6-deoxy-6-fluoro)-D-galactofuranose
UDP-(6-deoxy-6-fluoro)-D-galactopyranose
-
-
-
-
r
UDP-2,3-dideoxy-2,2,3,3-tetrafluoro-alpha-D-galactopyranose
UDP-2,3-dideoxy-2,2,3,3-tetrafluoro-alpha-D-galactofuranose
-
-
-
r
UDP-2-amino-2-deoxy-D-galactopyranose
?
-
-
-
-
?
UDP-2-deoxy-2-fluoro-D-galactofuranose
?
-
-
-
-
?
UDP-2-deoxy-2-fluoro-D-galactopyranose
?
-
-
-
-
?
UDP-2-fluoro-galactofuranose
?
-
-
-
-
?
UDP-3''-deoxy-3''-fluoro-D-galactopyranose
UDP-3''-deoxy-3''-fluoro-D-galactofuranose
-
-
-
r
UDP-3-deoxy-3-fluoro-D-galactofuranose
?
UDP-3-deoxy-3-fluoro-D-galactopyranose
?
-
-
-
-
?
UDP-6-deoxy-6-fluoro-D-galactopyranose
?
-
-
-
-
?
UDP-6-deoxy-D-galactopyranose
?
-
-
-
-
?
UDP-alpha-D-galactofuranose
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
UDP-beta-L-arabinofuranose
?
-
-
-
-
?
UDP-beta-L-arabinofuranose
UDP-beta-L-arabinopyranose
-
-
-
r
UDP-beta-L-arabinopyranose
UDP-beta-L-arabinofuranose
-
-
-
r
UDP-D-galactofuranose
UDP-D-galactopyranose
UDP-D-galactopyranose
UDP-D-galactofuranose
UDP-galactofuranose
UDP-galactopyranose
UDP-galactopyranose
UDP-galactofuranose
UDP-L-arabinofuranose
?
-
-
-
-
?
UDP-N-acetyl-2-deoxy-2-amino-alpha-D-galactopyranose
UDP-N-acetyl-2-deoxy-2-amino-alpha-D-galactofuranose
Uridine 5'-(trihydrogen diphosphate) P'-alpha-D-galactopyranosyl ester
Uridine 5'-(trihydrogen diphosphate) P'-alpha-D-galactofuranosyl ester
-
-
-
?
additional information
?
-
UDP-3-deoxy-3-fluoro-D-galactofuranose
?
-
-
-
-
?
UDP-3-deoxy-3-fluoro-D-galactofuranose
?
-
-
-
-
?
UDP-alpha-D-galactofuranose
UDP-alpha-D-galactopyranose
-
-
-
r
UDP-alpha-D-galactofuranose
UDP-alpha-D-galactopyranose
-
-
-
-
r
UDP-alpha-D-galactofuranose
UDP-alpha-D-galactopyranose
-
-
-
-
r
UDP-alpha-D-galactofuranose
UDP-alpha-D-galactopyranose
-
UGM-catalyzed interconversion
-
-
r
UDP-alpha-D-galactofuranose
UDP-alpha-D-galactopyranose
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
-
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
-
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
-
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
-
the equilibrium of the UGM-catalyzed reaction favors UDP-Galp by the ratio of 11:1
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
-
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
-
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
-
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
-
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
-
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
-
the equilibrium of the UGM-catalyzed reaction favors UDP-Galp by the ratio of 11:1
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
-
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
-
the equilibrium of the UGM-catalyzed reaction favors UDP-Galp by the ratio of 11:1
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
-
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
-
the equilibrium of the UGM-catalyzed reaction favors UDP-Galp by the ratio of 11:1
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
-
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
-
the equilibrium of the UGM-catalyzed reaction favors UDP-Galp by the ratio of 11:1
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
-
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
-
the equilibrium of the UGM-catalyzed reaction favors UDP-Galp by the ratio of 11:1
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
-
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
-
the equilibrium of the UGM-catalyzed reaction favors UDP-Galp by the ratio of 11:1
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
-
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
-
the equilibrium of the UGM-catalyzed reaction favors UDP-Galp by the ratio of 11:1
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
-
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
-
the equilibrium of the UGM-catalyzed reaction favors UDP-Galp by the ratio of 11:1
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
substrate binding structure of wild-type and mutant P306R, three-dimensional structure of the reduced MtUGM:UDP-Galp dimer, detailed overview. Substrate binding induces local changes in MtUGM active site
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
-
UGM-catalyzed interconversion
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
-
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
-
the equilibrium of the UGM-catalyzed reaction favors UDP-Galp by the ratio of 11:1
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
-
via iminium ion intermediates
-
-
r
UDP-D-galactofuranose
UDP-D-galactopyranose
-
-
-
-
r
UDP-D-galactofuranose
UDP-D-galactopyranose
-
-
-
-
r
UDP-D-galactofuranose
UDP-D-galactopyranose
-
-
-
-
r
UDP-D-galactopyranose
UDP-D-galactofuranose
-
-
-
-
r
UDP-D-galactopyranose
UDP-D-galactofuranose
-
-
-
-
r
UDP-D-galactopyranose
UDP-D-galactofuranose
-
-
-
r
UDP-D-galactopyranose
UDP-D-galactofuranose
-
-
-
?
UDP-D-galactopyranose
UDP-D-galactofuranose
-
-
-
-
?
UDP-D-galactopyranose
UDP-D-galactofuranose
-
-
-
-
r
UDP-D-galactopyranose
UDP-D-galactofuranose
-
-
-
?
UDP-D-galactopyranose
UDP-D-galactofuranose
-
-
-
-
r
UDP-D-galactopyranose
UDP-D-galactofuranose
-
-
-
-
?
UDP-D-galactopyranose
UDP-D-galactofuranose
-
-
-
-
r
UDP-D-galactopyranose
UDP-D-galactofuranose
-
-
-
-
?
UDP-galactofuranose
UDP-galactopyranose
-
-
8-5% product yield, 92-95% product yield
-
r
UDP-galactofuranose
UDP-galactopyranose
-
-
8-5% product yield, 92-95% product yield
-
r
UDP-galactopyranose
UDP-galactofuranose
-
-
-
?
UDP-galactopyranose
UDP-galactofuranose
-
-
-
r
UDP-galactopyranose
UDP-galactofuranose
-
-
-
-
?
UDP-galactopyranose
UDP-galactofuranose
-
-
-
-
?
UDP-galactopyranose
UDP-galactofuranose
-
-
-
-
?
UDP-galactopyranose
UDP-galactofuranose
-
-
-
-
r
UDP-galactopyranose
UDP-galactofuranose
-
pH 7.1, 30°C
-
-
r
UDP-galactopyranose
UDP-galactofuranose
-
-
-
-
?
UDP-galactopyranose
UDP-galactofuranose
-
-
-
-
?
UDP-galactopyranose
UDP-galactofuranose
-
-
-
r
UDP-galactopyranose
UDP-galactofuranose
pH 7.1, 30°C
-
-
r
UDP-galactopyranose
UDP-galactofuranose
-
-
-
-
r
UDP-galactopyranose
UDP-galactofuranose
-
-
-
?
UDP-galactopyranose
UDP-galactofuranose
-
-
-
?
UDP-galactopyranose
UDP-galactofuranose
-
-
-
-
?
UDP-galactopyranose
UDP-galactofuranose
-
-
-
-
r
UDP-galactopyranose
UDP-galactofuranose
-
-
?
UDP-galactopyranose
UDP-galactofuranose
-
-
-
?
UDP-galactopyranose
UDP-galactofuranose
-
-
-
-
?
UDP-galactopyranose
UDP-galactofuranose
-
-
-
-
r
UDP-galactopyranose
UDP-galactofuranose
-
-
-
r
UDP-galactopyranose
UDP-galactofuranose
-
-
-
-
r
UDP-galactopyranose
UDP-galactofuranose
-
-
-
r
UDP-galactopyranose
UDP-galactofuranose
pH 7.1, 30°C
-
-
r
UDP-galactopyranose
UDP-galactofuranose
-
-
-
-
?
UDP-galactopyranose
UDP-galactofuranose
-
-
-
-
r
UDP-galactopyranose
UDP-galactofuranose
-
-
-
r
UDP-galactopyranose
UDP-galactofuranose
-
essential step of mycobacterial cell wall biosynthesis
-
-
r
UDP-galactopyranose
UDP-galactofuranose
-
-
-
-
r
UDP-galactopyranose
UDP-galactofuranose
-
-
-
r
UDP-galactopyranose
UDP-galactofuranose
pH 7.1, 30°C
-
-
r
UDP-N-acetyl-2-deoxy-2-amino-alpha-D-galactopyranose
UDP-N-acetyl-2-deoxy-2-amino-alpha-D-galactofuranose
-
-
-
-
r
UDP-N-acetyl-2-deoxy-2-amino-alpha-D-galactopyranose
UDP-N-acetyl-2-deoxy-2-amino-alpha-D-galactofuranose
-
-
-
-
r
additional information
?
-
-
the enzyme is active in the oxidized state, being 2-3fold less active than in the reduced state. In the oxidized state, UGM does not bind UDP-galactopyranose
-
-
?
additional information
?
-
-
development of a fluorescence polarization binding assay for the Aspergillus fumigatus enzyme, evaluation, overview
-
-
?
additional information
?
-
active site and substrate binding structure, overview, the UDP exosite is located at a junction between domains 1 and 3
-
-
?
additional information
?
-
-
active site and substrate binding structure, overview, the UDP exosite is located at a junction between domains 1 and 3
-
-
?
additional information
?
-
-
UDP-galactopyranose mutase as an important protein in fungal cell wall biosynthesis
-
-
?
additional information
?
-
-
UDP-galactopyranose mutase as an important protein in fungal cell wall biosynthesis
-
-
?
additional information
?
-
-
UGM does not interconvert UDP-GalpNAc and UDP-GalfNAc
-
-
?
additional information
?
-
-
the bifunctional pyranose-furanose mutase recognizes both UDP-Gal and UDP-GalNAc
-
-
?
additional information
?
-
-
the bifunctional pyranose-furanose mutase recognizes both UDP-Gal and UDP-GalNAc
-
-
?
additional information
?
-
-
UGM does not interconvert UDP-GalpNAc and UDP-GalfNAc
-
-
?
additional information
?
-
-
no activity with UDP-6-deoxy-Dgalactopyranose, UDP-2-azido-2-deoxy-D-galactopyranose, and UDP-2-acetamido-2-deoxy-D-galactopyranose
-
-
?
additional information
?
-
UDP-D-glucose is not a substrate for UGM
-
-
?
additional information
?
-
-
UDP-D-glucose is not a substrate for UGM
-
-
?
additional information
?
-
-
the enzyme is active only in the reduced state
-
-
?
additional information
?
-
-
1,4-anhydrogalactopyranose does not react with UGM and UDP to form UDP-galactopyranose or UDP-galactofuranose
-
-
?
additional information
?
-
analysis of the structural basis of ligand binding to UDP-galactopyranose mutase from Mycobacterium tuberculosis using substrate and tetrafluorinated substrate analogues, overview
-
-
?
additional information
?
-
-
analysis of the structural basis of ligand binding to UDP-galactopyranose mutase from Mycobacterium tuberculosis using substrate and tetrafluorinated substrate analogues, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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(1R,3S,4R,7R,8S)-3-hydroxymethyl-2,6-dioxa-bicyclo-[2.2.2]-octane-7,8-diol
-
17% inhibition at 4 mM
(2R,3S,4S,5S,2'R,3'S,4'S,5'S)-2,2'-butane-1,4-diylbis[5-[(1S)-1,2-dihydroxyethyl]-3,4-dihydroxypyrrolidinium] dichloride
-
-
(2S)-2-deoxy-2-selenonium-2-[(2S,3S,4R,5S)-2,3,4,5,6-pentahydroxyhexyl]-D-arabinitol chloride
-
a transition-state analogue, shows about 25% inhibition at 0.5 mm
(2S)-2-deoxy-2-sulfonium-2-[(2S,3S,4R,5S)-2,3,4,5,6-pentahydroxyhexyl]-D-arabinitol chloride
-
a transition-state analogue, shows about 25% inhibition at 0.5 mm
(2S,3S,4S,5R)-2-[(1S)-1,2-dihydroxyethyl]-5-propylpyrrolidine-3,4-diol
-
-
(2S,3S,4S,5R)-2-[(1S)-1,2-dihydroxyethyl]-5-[(1E)-prop-1-en-1-yl]pyrrolidine-3,4-diol
-
-
(2Z)-2-(2-chloro-4-hydroxy-5-nitrobenzylidene)[1,3]thiazolo[3,2-a]benzimidazol-3(2H)-one
-
comparison with inhibition of Mycobacterium tuberculosis enzyme; dissociation constant 0.0053 mM, comparison with inhibition of Klebsiella pneumoniae enzyme
(4-chlorophenyl)(1-(4-chlorophenyl)-5-hydroxy-1H-pyrazol-4-yl)methanone
-
i.e. MS-208, a non-substrate-like inhibitor, mixed inhibition due to a lack of direct competition between MS-208 and the enzyme substrate. Molecular dynamics studies reveal that the MS-208 inhibition occurs by preventing complete closure of an active site mobile loop that is necessary for productive substrate binding. The results suggest the presence of an A-site with potential druggability. Kinetic analysis, docking, and molecular dynamics simulation and modeling of enzyme binding, overview. Model of the tertiary complex MtUGM:UDP-Galp:MS-208. Two A-loop residues, Glu321 and Asp322, are stabilized by MS-208 binding yet destabilized by UDP-Galp binding, with the former effect being more pronounced
(4-chlorophenyl)-[1-(4-chlorophenyl)-3-hydroxy-5-methyl-1H-pyrazol-4-yl]-methanone
(4E)-4-(4-chloro-3-nitrobenzylidene)-1-(3,4-dichlorophenyl)pyrazolidine-3,5-dione
-
comparison with inhibition of Mycobacterium tuberculosis enzyme; dissociation constant 0.0049 mM, comparison with inhibition of Klebsiella pneumoniae enzyme
(Z)-N-((E)-5-(5-nitro-2-oxoindolin-3-ylidene)-4-oxothiazolidin-2-ylidene) benzenesulfonamide
-
-
1(R)-1,4-dideoxy-1-C-3-[(ethyl)(uridin-5'-yl)phosphono]-2-propen-1-yl-1,4-imino-D-galactitol
-
25 mM, 52% residual activity
1(R)-1,4-dideoxy-1-C-3-[(uridin-5'-yl)phosphono]-2-propen-1-yl-1,4-imino-D-galactitol
-
2.5 mM, 43% residual activity
1(R)-1-C-allyl-1,4-dideoxy-1,4-imino-D-galactitol
-
25 mM, 61% residual activity
1,4-anhydro-beta-D-galactopyranose (1,5-anhydro-alpha-D-galactofuranose)
-
15% inhibition at 4 mM
1,4-bis-[1(R)-1,4-dideoxy-1,4-imino-D-galactit-1-yl]-2-butene
-
2.5 mM, 50% residual activity
1-[5-O-(alpha-D-galactopyranosyl)-D-glucityl]pyrimidine-2,4(3H)-dione
-
28% enzyme inhibition at 0.5 mM
-
1-[5-O-(beta-D-galactopyranosyl)-D-glucityl]pyrimidine-2,4(3H)-dione
-
30% enzyme inhibition at 0.5 mM
-
2-((4-(3,4-dichlorophenyl)thiazol-2-yl)amino)-3-(4-iodophenyl)propanoic acid
2-(([2-(4-bromophenyl)-1,3-dioxo-2,3-dihydro-1H-isoindol-5-yl]carbonyl)amino)benzoic acid
-
comparison with inhibition of Mycobacterium tuberculosis enzyme
2-(2-(4-bromophenyI)-1, 3-dioxoisoindolin-5-carboxamido) benzoic acid
-
-
2-(3-((4-chlorophenoxy)methyl)-6-(p-tolyl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
2-(3-((4-chlorophenoxy)methyl)-6-(thiophen-2-yl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
2-(3-(2-methylfuran-3-yl)-6-phenyl-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
2-(3-(4-bromobenzyl)-6-(4-chlorophenyl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
2-(3-(4-fluorobenzyl)-6-(p-tolyl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
2-(3-(4-fluorobenzyl)-6-(thiophen-2-yl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
2-(3-(4-fluorobenzyl)-6-phenyl-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
2-(3-(4-fluorophenyl)-6-phenyl-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
2-(3-(furan-2-yl)-6-(p-tolyl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
2-(3-(furan-2-yl)-6-(thiophen-2-yl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
2-(3-(furan-2-yl)-6-phenyl-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
2-(3-cyclopropyl-6-phenyl-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
2-(6-(4-chlorophenyl)-3-(2-methoxyphenyl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
2-(6-(4-chlorophenyl)-3-(4-fluorophenyl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
2-(6-(4-chlorophenyl)-3-(thiophen-2-yl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
2-(6-(4-chlorophenyl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
2-(6-(4-fluorophenyl)-3-(furan-2-yl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
2-[(5E)-5-(3-bromobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
-
comparison with inhibition of Mycobacterium tuberculosis enzyme; dissociation constant 0.0094 mM, comparison with inhibition of Klebsiella pneumoniae enzyme
2-[(5E)-5-(4-bromobenzylidene)-2-thioxo-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
-
dissociation constant 0.0093 mM, comparison with inhibition of Klebsiella pneumoniae enzyme
2-[(5Z)-5-[(3-chlorophenyl)methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
-
-
2-[5-(3-bromo-benzylidene)-4-oxo-2-thioxo-thiazolidin-3-yl]-3-phenyl-propionic acid
-
-
2-[[2-(4-bromo-phenyl)-1,3-dioxo-2,3-dihydro-1H-isoindole-5-carbonyl]-amino]-benzoic acid
-
-
2-[[4-(3,4-dichlorophenyl)-1,3-thiazol-2-yl]amino]-3-(3-iodophenyl)propanoic acid
-
-
3-(3-(2-(allylamino)thiazol-4-yl)-2,5-dimethyl-1H-pyrrol-1-yl)propanoic acid
3-(4-bromobenzyl)-6-(4-chlorophenyl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazine-7-carboxylic acid
-
3-(4-iodophenyl)-2-[4-(3,4-dichlorophenyl)-thiazol-2-ylamino]-propionic acid
3-(6-(benzyloxy)-1H-indol-1-yl)propanoic acid
6-(4-chlorophenyl)-3-(thiophen-2-yl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazine-7-carboxylic acid
-
flavopiridol
a compound that increases the melting temperature of Aspergillus fumigatus UGM. Flavopiridol also is a non-competitive inhibitor of UGM, and docking studies reveal that flavopiriol binds in the adenine-galactopyranose pocket and interacts with several residues. This compound does not inhibit the prokaryotic UGM from Mycobacteria tuberculosis. Inhibition mechanism of flavopiriodol
N-(4-[4-[8-([[3-carboxy-4-(6-hydroxy-3-oxo-3H-xanthen-9-yl)phenyl]carbamothioyl]amino)octyl]phenyl]-2,3-dihydro-1,3-thiazol-2-yl)-4-chlorophenylalanine
-
-
N-[4-oxo-5-(2-oxo-1,2-dihydro-indol-3-ylidene)-thiazolidin-2-ylidene]-benzenesulfonamide
-
-
Sodium cyanoborohydride
-
-
UDP-(1(1')E)-1_-fluoro-exo-glycal-D-galactofuranose
-
less than 10% inhibition at 1 mM. Time-dependent inactivation proceeds via two-electron processes
UDP-(1(1')Z)-1'-fluoro-exo-glycal-D-galactofuranose
-
less than 10% inhibition at 1 mM. Time-dependent inactivation proceeds via two-electron processes
UDP-2,3-dideoxy-2,2,3,3-tetrafluoro-alpha-D-galactofuranose
UDP-F4-Galf, enzyme binding structure analysis and binding mode, overview
UDP-2,3-dideoxy-2,2,3,3-tetrafluoro-alpha-D-galactopyranose
UDP-F4-Galp, enzyme binding structure analysis and binding mode, overview
UDP-3-deoxy-3-fluoro-alpha-D-galactofuranose
-
UDP-C-alpha-D-galactofuranose
-
91% inhibition at 1 mM
UDP-C-alpha-D-galactopyranose
-
36% inhibition at 1 mM
UDP-C-beta-D-galactopyranose
-
8% inhibition at 1 mM
UDP-D-glucose
-
poor inhibitor of UGM
UDP-[1(1')Z]-exo-glycal-D-galactopyranose
-
42% inhibition at 1 mM
uridine-5'-diphospho-(N-fluoresceinisothiocyano)hexanolamine
-
-
(4-chlorophenyl)-[1-(4-chlorophenyl)-3-hydroxy-5-methyl-1H-pyrazol-4-yl]-methanone
-
-
(4-chlorophenyl)-[1-(4-chlorophenyl)-3-hydroxy-5-methyl-1H-pyrazol-4-yl]-methanone
-
-
2-((4-(3,4-dichlorophenyl)thiazol-2-yl)amino)-3-(4-iodophenyl)propanoic acid
-
-
2-((4-(3,4-dichlorophenyl)thiazol-2-yl)amino)-3-(4-iodophenyl)propanoic acid
-
2-((4-(3,4-dichlorophenyl)thiazol-2-yl)amino)-3-(4-iodophenyl)propanoic acid
-
-
2-((4-(3,4-dichlorophenyl)thiazol-2-yl)amino)-3-(4-iodophenyl)propanoic acid
-
2-((4-(3,4-dichlorophenyl)thiazol-2-yl)amino)-3-(4-iodophenyl)propanoic acid
-
-
2-(3-((4-chlorophenoxy)methyl)-6-(p-tolyl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
97% inhibition at 0.1 mM
2-(3-((4-chlorophenoxy)methyl)-6-(p-tolyl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
-
97% inhibition at 0.1 mM
2-(3-((4-chlorophenoxy)methyl)-6-(thiophen-2-yl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
95% inhibition at 0.1 mM
2-(3-((4-chlorophenoxy)methyl)-6-(thiophen-2-yl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
-
95% inhibition at 0.1 mM
2-(3-(2-methylfuran-3-yl)-6-phenyl-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
25% inhibition at 0.1 mM
2-(3-(2-methylfuran-3-yl)-6-phenyl-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
-
25% inhibition at 0.1 mM
2-(3-(4-bromobenzyl)-6-(4-chlorophenyl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
-
-
2-(3-(4-bromobenzyl)-6-(4-chlorophenyl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
-
2-(3-(4-bromobenzyl)-6-(4-chlorophenyl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
second generation compound, competitive, 100% inhibition at 0.1 mM
2-(3-(4-bromobenzyl)-6-(4-chlorophenyl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
-
second generation compound, competitive, 100% inhibition at 0.1 mM
2-(3-(4-fluorobenzyl)-6-(p-tolyl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
96% inhibition at 0.1 mM
2-(3-(4-fluorobenzyl)-6-(p-tolyl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
-
96% inhibition at 0.1 mM
2-(3-(4-fluorobenzyl)-6-(thiophen-2-yl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
92% inhibition at 0.1 mM
2-(3-(4-fluorobenzyl)-6-(thiophen-2-yl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
-
92% inhibition at 0.1 mM
2-(3-(4-fluorobenzyl)-6-phenyl-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
92% inhibition at 0.1 mM
2-(3-(4-fluorobenzyl)-6-phenyl-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
-
92% inhibition at 0.1 mM
2-(3-(4-fluorophenyl)-6-phenyl-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
74% inhibition at 0.1 mM
2-(3-(4-fluorophenyl)-6-phenyl-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
-
74% inhibition at 0.1 mM
2-(3-(furan-2-yl)-6-(p-tolyl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
62% inhibition at 0.1 mM
2-(3-(furan-2-yl)-6-(p-tolyl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
-
62% inhibition at 0.1 mM
2-(3-(furan-2-yl)-6-(thiophen-2-yl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
46% inhibition at 0.1 mM
2-(3-(furan-2-yl)-6-(thiophen-2-yl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
-
46% inhibition at 0.1 mM
2-(3-(furan-2-yl)-6-phenyl-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
34% inhibition at 0.1 mM
2-(3-(furan-2-yl)-6-phenyl-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
-
34% inhibition at 0.1 mM
2-(3-cyclopropyl-6-phenyl-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
8.9% inhibition at 0.1 mM
2-(3-cyclopropyl-6-phenyl-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
-
8.9% inhibition at 0.1 mM
2-(6-(4-chlorophenyl)-3-(2-methoxyphenyl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
91% inhibition at 0.1 mM
2-(6-(4-chlorophenyl)-3-(2-methoxyphenyl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
-
91% inhibition at 0.1 mM
2-(6-(4-chlorophenyl)-3-(4-fluorophenyl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
96% inhibition at 0.1 mM
2-(6-(4-chlorophenyl)-3-(4-fluorophenyl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
-
96% inhibition at 0.1 mM
2-(6-(4-chlorophenyl)-3-(thiophen-2-yl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
-
-
2-(6-(4-chlorophenyl)-3-(thiophen-2-yl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
-
2-(6-(4-chlorophenyl)-3-(thiophen-2-yl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
first generation compound, competitive, 95% inhibition at 0.1 mM
2-(6-(4-chlorophenyl)-3-(thiophen-2-yl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
-
first generation compound, competitive, 95% inhibition at 0.1 mM
2-(6-(4-chlorophenyl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
72% inhibition at 0.1 mM
2-(6-(4-chlorophenyl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
-
72% inhibition at 0.1 mM
2-(6-(4-fluorophenyl)-3-(furan-2-yl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
38% inhibition at 0.1 mM
2-(6-(4-fluorophenyl)-3-(furan-2-yl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazin-7-yl)acetic acid
-
38% inhibition at 0.1 mM
3-(3-(2-(allylamino)thiazol-4-yl)-2,5-dimethyl-1H-pyrrol-1-yl)propanoic acid
-
3-(3-(2-(allylamino)thiazol-4-yl)-2,5-dimethyl-1H-pyrrol-1-yl)propanoic acid
-
-
3-(4-iodophenyl)-2-[4-(3,4-dichlorophenyl)-thiazol-2-ylamino]-propionic acid
-
-
3-(4-iodophenyl)-2-[4-(3,4-dichlorophenyl)-thiazol-2-ylamino]-propionic acid
-
-
3-(6-(benzyloxy)-1H-indol-1-yl)propanoic acid
-
3-(6-(benzyloxy)-1H-indol-1-yl)propanoic acid
-
-
ethambutol
-
-
Quinine
-
-
UDP
-
competitive
UDP
enzyme binding structure analysis and binding mode, overview
UDP-CH2-Galp
moderate inhibition of UGM
UDP-CH2-Galp
-
moderate inhibition of UGM
UDP-CH2-Galp
-
moderate inhibition of UGM
additional information
identification of eukaryotic UDP-galactopyranose mutase inhibitors using the ThermoFAD assay, docking studies
-
additional information
-
identification of eukaryotic UDP-galactopyranose mutase inhibitors using the ThermoFAD assay, docking studies
-
additional information
-
structure-based virtual screening for UDP-galactopyranose mutase ligands identifies a class of antimycobacterial agents, triazolothiadiazine inhibitors, using structures of UGMs from Aspergillus fumigatus, Trypanosoma cruzi, and Klebsiella pneumoniae (PDB ID 3INT)
-
additional information
structure-based virtual screening for UDP-galactopyranose mutase ligands identifies a class of antimycobacterial agents, triazolothiadiazine inhibitors, using structures of UGMs from Aspergillus fumigatus, Trypanosoma cruzi, and Klebsiella pneumoniae (PDB ID 3INT)
-
additional information
the enzyme can be inhibited by 2-aminothiazoles, e.g. 2-((4-(3,4-dichlorophenyl)thiazol-2-yl)amino)-3-(4-iodophenyl)propanoic acid, or triazolothiadiazines, such as 6-(4-chlorophenyl)-3-(thiophen-2-yl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazine-7-carboxylic acid or 3-(4-bromobenzyl)-6-(4-chlorophenyl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazine-7-carboxylic acid
-
additional information
-
the enzyme can be inhibited by 2-aminothiazoles, e.g. 2-((4-(3,4-dichlorophenyl)thiazol-2-yl)amino)-3-(4-iodophenyl)propanoic acid, or triazolothiadiazines, such as 6-(4-chlorophenyl)-3-(thiophen-2-yl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazine-7-carboxylic acid or 3-(4-bromobenzyl)-6-(4-chlorophenyl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazine-7-carboxylic acid
-
additional information
structure-based virtual screening for UDP-galactopyranose mutase ligands identifies a class of antimycobacterial agents, triazolothiadiazine inhibitors, using structures of UGMs from Aspergillus fumigatus, Trypanosoma cruzi, and Klebsiella pneumoniae (PDB ID 3INT)
-
additional information
-
fluorinated substrate analogues under non-reducing conditions
-
additional information
-
structure-based virtual screening for UDP-galactopyranose mutase ligands identifies a class of antimycobacterial agents, triazolothiadiazine inhibitors, using structures of UGMs from Aspergillus fumigatus, Trypanosoma cruzi, and Klebsiella pneumoniae (PDB ID 3INT)
-
additional information
-
identification of eukaryotic UDP-galactopyranose mutase inhibitors using the ThermoFAD assay. Flavopiridol does not inhibit the prokaryotic UGM from Mycobacterium tuberculosis, in contrast to the eukaryotic enzyme from Aspergillus fumigatus
-
additional information
-
synthesis of 1-[5-O-(alpha-D-galactopyranosyl)-D-glucityl]pyrimidine-2,4(3H)-dione and 1-[5-O-(beta-D-galactopyranosyl)-D-glucityl]pyrimidine-2,4(3H)-dione as non-ionic substrate mimics of substrate UDP-alpha-D-galactopyranose. The nonionic polyhydroxylated chain is intended to mimic the ionic diphosphate group and the ribose moiety in UDP-Galp and to increase the bioavailabilities of the candidate inhibitors. Inhibition assays with UGM of Mycobacterium tuberculosis show only weak inhibition of the enzyme by the compounds. Retrosynthetic analysis of the target compounds, overview
-
additional information
-
synthesis of a sulfonium and selenonium ion with an appended polyhydroxylated side chain. The compounds are designed as transition state mimics of the UGM-catalyzed reaction, where the head groups carrying a permanent positive charge, and are designed to mimic both the shape and positive charge of the proposed galactopyranosyl cation-like transition state, HPLC-based UGM inhibition assay. Even modifying one of these inhibitors by attaching the uridine monophosphate (UMP) fragment via an alpha-linkage to the 1,4-dideoxy-1,4-imino-D-galctitol moiety using a three-carbon linker does not improve the inhibitory profile significantly. Retrosynthetic inhibitor analysis, detailed overview
-
additional information
-
modeling of binding of substrate-like inhibitors using enzyme crystal structures, PDB IDs 1V0J and 4RPH. Modeling of non-substrate-like inhibitors using an integrated approach that combines saturation transfer difference (STD) NMR spectroscopy, enzyme kinetic assays, molecular modeling, and mutagenesis, leading to the discovery of a second binding site, distinct from the enzyme active site, to which (4-chlorophenyl)(1-(4-chlorophenyl)-5-hydroxy-1H-pyrazol-4-yl)methanone binds, affecting productive substrate binding at the active site and inhibiting enzyme function. Competition STD NMR experiments
-
additional information
dissociation constants for the inhibitors by saturation transfer difference (STD) NMR spectroscopy measurements
-
additional information
-
dissociation constants for the inhibitors by saturation transfer difference (STD) NMR spectroscopy measurements
-
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acetyl-coa c-acyltransferase deficiency
Inhibition of the glycine cleavage system by branched-chain amino acid metabolites.
Acidosis
Concentration of 2,3 bisphosphoglycerate in cattle affected with acute ruminal acidosis.
Aspergillosis
Crystal structures and small-angle X-ray scattering analysis of UDP-galactopyranose mutase from the pathogenic fungus Aspergillus fumigatus.
Brain Ischemia
Structural Basis of the Molecular Switch between Phosphatase and Mutase Functions of Human Phosphomannomutase 1 under Ischemic Conditions.
Breast Neoplasms
UGM: a more stable procedure for large-scale multiple testing problems, new solutions to identify oncogene.
Carcinogenesis
A practical method to screen and identify functioning biomarkers in nasopharyngeal carcinoma.
Carcinogenesis
Evidence that androgen-independent stromal growth factor signals promote androgen-insensitive prostate cancer cell growth in vivo.
Carcinogenesis
Role of mesenchymal-epithelial interactions in normal and abnormal development of the mammary gland and prostate.
Carcinogenesis
Role of the stromal microenvironment in carcinogenesis of the prostate.
Carcinoma
A human prostatic epithelial model of hormonal carcinogenesis.
Carcinoma
Influence of male genital tract mesenchymes on differentiation of Dunning prostatic adenocarcinoma.
Carcinoma
Role of mesenchymal-epithelial interactions in normal and abnormal development of the mammary gland and prostate.
Chagas Disease
Chemical mechanism of UDP-galactopyranose mutase from Trypanosoma cruzi: a potential drug target against Chagas' disease.
Colorectal Neoplasms
Purification and identification of monoubiquitin-phosphoglycerate mutase B complex from human colorectal cancer tissues.
Communicable Diseases
The impact of suitability of empirical antibiotics use on therapeutic outcome of respiratory tract infection patients at inpatient wards of Universitas Gadjah Mada Academic Hospital.
Genetic Diseases, Inborn
Recognition, isolation, and characterization of rat liver D-methylmalonyl coenzyme A hydrolase.
Heart Failure
Atrial natriuretic factor as a marker in congestive heart failure.
Infections
Characterization of the Caenorhabditis elegans UDP-galactopyranose mutase homolog glf-1 reveals an essential role for galactofuranose metabolism in nematode surface coat synthesis.
Infections
Molecular Dynamics Simulations of Substrate Release from Trypanosoma cruzi UDP-Galactopyranose Mutase.
Infections
Porphyromonas gingivalis Placental Atopobiosis and Inflammatory Responses in Women With Adverse Pregnancy Outcomes.
Infections
Specificity of a UDP-GalNAc pyranose-furanose mutase: a potential therapeutic target for Campylobacter jejuni infections.
Infections
The impact of suitability of empirical antibiotics use on therapeutic outcome of respiratory tract infection patients at inpatient wards of Universitas Gadjah Mada Academic Hospital.
Infections
[Prevalence of urogenital mycoplasma infection in women infected with HIV in Bangui (Central African Republic)]
Infertility
Antifertility and ultrastructural effects of optical isomers of gossypol administered intratesticularly in rats.
Infertility
[Urogenital mycoplasmosis and Mycoplasma carriage during pregnancy and in inflammatory processes of the genitalia in workers in the electronics industry]
Ischemic Stroke
SLC17A3 rs9379800 and Ischemic Stroke Susceptibility at the Northern Region of Malaysia.
Leishmaniasis
Identification of novel inhibitors against UDP-galactopyranose mutase to combat leishmaniasis.
Leishmaniasis, Visceral
Alkaloids and leishmania donovani UDP-galactopyarnose mutase: Anovel approach in drug designing against Visceral leishmaniasis.
Lung Neoplasms
A practical method to screen and identify functioning biomarkers in nasopharyngeal carcinoma.
Melanoma
Cobalamin metabolism in methionine-dependent human tumour and leukemia cell lines.
Mitochondrial Myopathies
Neuromuscular disorders in infancy and childhood.
Muscle Hypotonia
Neuromuscular disorders in infancy and childhood.
Muscular Atrophy, Spinal
Neuromuscular disorders in infancy and childhood.
Muscular Dystrophies
Neuromuscular disorders in infancy and childhood.
Neoplasms
A human prostatic epithelial model of hormonal carcinogenesis.
Neoplasms
Evidence that androgen-independent stromal growth factor signals promote androgen-insensitive prostate cancer cell growth in vivo.
Neoplasms
Morphologic and biochemical alterations in rat prostatic tumors induced by fetal urogenital sinus mesenchyme.
Neoplasms
Normal and abnormal development of the male urogenital tract. Role of androgens, mesenchymal-epithelial interactions, and growth factors.
Neoplasms
Phosphoglycerate mutase, 2,3-bisphosphoglycerate phosphatase and enolase activity and isoenzymes in lung, colon and liver carcinomas.
Osteoarthritis
The association between degenerative hip joint pathology and size of the gluteus maximus and tensor fascia lata muscles.
phosphoglycerate mutase (2,3-diphosphoglycerate-dependent) deficiency
Phosphorus magnetic resonance spectroscopy of partially blocked muscle glycolysis. An in vivo study of phosphoglycerate mutase deficiency.
Polycythemia
Erythrocytosis due to bisphosphoglycerate mutase deficiency with concurrent glucose-6-phosphate dehydrogenase (G-6-PD) deficiency.
Polycythemia
Hereditary erythrocytosis, thrombocytosis and neutrophilia.
Polycythemia
Polycythemia and oxygen sensing.
Propionic Acidemia
Biochemical and anaplerotic applications of in vitro models of propionic acidemia and methylmalonic acidemia using patient-derived primary hepatocytes.
Propionic Acidemia
Gestational age-related reference values for amniotic fluid organic acids.
Propionic Acidemia
Identification of 2,2-Dimethylbutanoic Acid (HST5040), a Clinical Development Candidate for the Treatment of Propionic Acidemia and Methylmalonic Acidemia.
Propionic Acidemia
Inhibition of the glycine cleavage system by branched-chain amino acid metabolites.
propionyl-coa carboxylase deficiency
Inhibition of the glycine cleavage system by branched-chain amino acid metabolites.
Protein Deficiency
A diagnostic algorithm for metabolic myopathies.
Respiratory Tract Infections
The impact of suitability of empirical antibiotics use on therapeutic outcome of respiratory tract infection patients at inpatient wards of Universitas Gadjah Mada Academic Hospital.
Sexually Transmitted Diseases
[Prevalence of urogenital mycoplasma infection in women infected with HIV in Bangui (Central African Republic)]
Small Cell Lung Carcinoma
A practical method to screen and identify functioning biomarkers in nasopharyngeal carcinoma.
Tuberculosis
A Microbiological, Toxicological, and Biochemical Study of the Effects of Fucoxanthin, a Marine Carotenoid, on Mycobacterium tuberculosis and the Enzymes Implicated in Its Cell Wall: A Link Between Mycobacterial Infection and Autoimmune Diseases.
Tuberculosis
A Second, Druggable Binding Site in UDP-Galactopyranose Mutase from Mycobacterium tuberculosis?
Tuberculosis
Antimycobacterial activity of UDP-galactopyranose mutase inhibitors.
Tuberculosis
Biosynthesis of Galactan in Mycobacterium tuberculosis as a Viable TB Drug Target?
Tuberculosis
Biosynthesis of the galactan component of the mycobacterial cell wall.
Tuberculosis
Chemical probes of UDP-galactopyranose mutase.
Tuberculosis
Combined molecular dynamics, STD-NMR, and CORCEMA protocol yields structural model for a UDP-galactopyranose mutase-inhibitor complex.
Tuberculosis
Comparing Galactan Biosynthesis in Mycobacterium tuberculosis and Corynebacterium diphtheriae.
Tuberculosis
Conformational Control of UDP-Galactopyranose Mutase Inhibition.
Tuberculosis
Contributions of unique active site residues of eukaryotic UDP-galactopyranose mutases to substrate recognition and active site dynamics.
Tuberculosis
Crystal structures of Mycobacteria tuberculosis and Klebsiella pneumoniae UDP-galactopyranose mutase in the oxidised state and Klebsiella pneumoniae UDP-galactopyranose mutase in the (active) reduced state.
Tuberculosis
Drug targeting Mycobacterium tuberculosis cell wall synthesis: development of a microtiter plate-based screen for UDP-galactopyranose mutase and identification of an inhibitor from a uridine-based library.
Tuberculosis
Expression, purification and preliminary X-ray crystallographic analysis of UDP-galactopyranose mutase from Deinococcus radiodurans.
Tuberculosis
Identification of eukaryotic UDP-galactopyranose mutase inhibitors using the ThermoFAD assay.
Tuberculosis
Identification of inhibitors of UDP-galactopyranose mutase via combinatorial in situ screening.
Tuberculosis
Identification of potential inhibitors for mycobacterial uridine diphosphogalactofuranose-galactopyranose mutase enzyme: A novel drug target through in silico approach.
Tuberculosis
Inhibitors of UDP-galactopyranose mutase thwart mycobacterial growth.
Tuberculosis
Ligand binding and substrate discrimination by UDP-galactopyranose mutase.
Tuberculosis
Natural and Synthetic Flavonoids as Potent Mycobacterium tuberculosis UGM Inhibitors.
Tuberculosis
Potent ligands for prokaryotic UDP-galactopyranose mutase that exploit an enzyme subsite.
Tuberculosis
Reversible and efficient inhibition of UDP-galactopyranose mutase by electrophilic, constrained and unsaturated UDP-galactitol analogues.
Tuberculosis
Structural Basis of Ligand Binding to UDP-Galactopyranose Mutase from Mycobacterium tuberculosis Using Substrate and Tetrafluorinated Substrate Analogues.
Tuberculosis
Synthesis and biological evaluation of nonionic substrate mimics of UDP-Galp as candidate inhibitors of UDP galactopyranose mutase (UGM).
Tuberculosis
Synthesis and evaluation of heterocycle structures as potential inhibitors of Mycobacterium tuberculosis UGM.
Tuberculosis
Synthesis and evaluation of nitrofuranylamides as novel antituberculosis agents.
Tuberculosis
Synthesis of a carbasugar analogue of a putative intermediate in the UDP-galp-mutase catalyzed isomerization.
Tuberculosis
Tetrafluorination of sugars as strategy for enhancing protein-carbohydrate affinity: application to UDP-Galp mutase inhibition.
udp-galactopyranose mutase deficiency
Anaesthetic considerations in a child with methylmalonic acidemia and its literature review.
udp-galactopyranose mutase deficiency
Anaesthetic considerations in a patient with methylmalonyl-coenzyme A mutase deficiency.
udp-galactopyranose mutase deficiency
Anesthetic management of a child with methylmalonyl-coenzyme A mutase deficiency.
udp-galactopyranose mutase deficiency
Causes of and diagnostic approach to methylmalonic acidurias.
udp-galactopyranose mutase deficiency
Enzymologic studies on patients with methylmalonic aciduria: basis for a clinical trial of deoxyadenosylcobalamin in a hydroxocobalamin-unresponsive patient.
udp-galactopyranose mutase deficiency
Epilepsy in children with methylmalonic acidemia: Electroclinical features and prognosis.
udp-galactopyranose mutase deficiency
Gestational age-related reference values for amniotic fluid organic acids.
udp-galactopyranose mutase deficiency
Inhibition of the glycine cleavage system by branched-chain amino acid metabolites.
udp-galactopyranose mutase deficiency
Methylmalonic acidemia with a severe chemical but benign clinical phenotype.
udp-galactopyranose mutase deficiency
Methylmalonic semialdehyde dehydrogenase deficiency: psychomotor delay and methylmalonic aciduria without metabolic decompensation.
udp-galactopyranose mutase deficiency
Neuromuscular disorders in infancy and childhood.
udp-galactopyranose mutase deficiency
Phosphorus magnetic resonance spectroscopy of partially blocked muscle glycolysis. An in vivo study of phosphoglycerate mutase deficiency.
udp-galactopyranose mutase deficiency
Polycythemia and oxygen sensing.
udp-galactopyranose mutase deficiency
Prenatal diagnosis for methylmalonic acidemia and inborn errors of vitamin B12 metabolism and transport.
udp-galactopyranose mutase deficiency
Prolonged exclusive breast-feeding from vegan mother causing an acute onset of isolated methylmalonic aciduria due to a mild mutase deficiency.
udp-galactopyranose mutase deficiency
Screening for methylmalonic aciduria in Alberta: a voluntary program with particular significance for the Hutterite Brethren.
udp-galactopyranose mutase deficiency
Selective Screening for Organic Acidurias and Amino Acidopathies in Pakistani Children.
udp-galactopyranose mutase deficiency
Stabilization of blood methylmalonic acid level in methylmalonic acidemia after liver transplantation.
udp-galactopyranose mutase deficiency
Varying neurological phenotypes among muto and mut- patients with methylmalonylCoA mutase deficiency.
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24
UDP-(6-deoxy-6-fluoro)-D-galactofuranose
0.023
UDP-2,3-dideoxy-2,2,3,3-tetrafluoro-alpha-D-galactopyranose
pH 7.5, 37°C, recombinant enzyme
1.14
UDP-2-amino-2-deoxy-D-galactopyranose
-
in 50 mM MOPS, 10 mM sodium dithionite, 2 mM MgCl2 pH 7.4, at 37°C
0.065
UDP-2-deoxy-2-fluoro-D-galactofuranose
-
-
0.203
UDP-2-deoxy-2-fluoro-D-galactopyranose
-
in 50 mM MOPS, 10 mM sodium dithionite, 2 mM MgCl2 pH 7.4, at 37°C
0.065
UDP-2-fluoro-galactofuranose
-
-
0.861
UDP-3-deoxy-3-fluoro-D-galactofuranose
0.28
UDP-3-deoxy-3-fluoro-D-galactopyranose
-
in 50 mM MOPS, 10 mM sodium dithionite, 2 mM MgCl2 pH 7.4, at 37°C
0.2
UDP-6-deoxy-6-fluoro-D-galactopyranose
-
in 50 mM MOPS, 10 mM sodium dithionite, 2 mM MgCl2 pH 7.4, at 37°C
3.15
UDP-6-deoxy-D-galactopyranose
-
in 50 mM MOPS, 10 mM sodium dithionite, 2 mM MgCl2 pH 7.4, at 37°C
0.032 - 2.153
UDP-alpha-D-galactofuranose
0.022 - 0.607
UDP-alpha-D-galactopyranose
0.094 - 0.7
UDP-beta-L-arabinofuranose
0.016 - 0.194
UDP-D-galactofuranose
0.043 - 1.002
UDP-D-galactopyranose
0.02 - 0.19
UDP-galactofuranose
0.022 - 0.055
UDP-galactopyranose
0.6
UDP-L-arabinofuranose
-
-
additional information
additional information
-
24
UDP-(6-deoxy-6-fluoro)-D-galactofuranose
-
-
24
UDP-(6-deoxy-6-fluoro)-D-galactofuranose
-
-
0.861
UDP-3-deoxy-3-fluoro-D-galactofuranose
-
-
0.861
UDP-3-deoxy-3-fluoro-D-galactofuranose
-
-
0.032
UDP-alpha-D-galactofuranose
pH and temperature not specified in the publication, recombinant mutant Y100A
0.057
UDP-alpha-D-galactofuranose
pH and temperature not specified in the publication, recombinant mutant Y104A
0.078
UDP-alpha-D-galactofuranose
-
pH and temperature not specified in the publication, recombinant wild-type enzyme
0.11
UDP-alpha-D-galactofuranose
pH and temperature not specified in the publication, recombinant wild-type enzyme
0.14
UDP-alpha-D-galactofuranose
pH and temperature not specified in the publication, recombinant wild-type enzyme
0.166
UDP-alpha-D-galactofuranose
pH and temperature not specified in the publication, recombinant mutant N207A
0.193
UDP-alpha-D-galactofuranose
pH 7.0, 37°C, recombinant mutant W315A
0.334
UDP-alpha-D-galactofuranose
pH and temperature not specified in the publication, recombinant mutant Y317A
0.38
UDP-alpha-D-galactofuranose
pH and temperature not specified in the publication, recombinant mutant Y317A
0.45
UDP-alpha-D-galactofuranose
pH 7.0, 37°C, recombinant wild-type enzyme
0.478
UDP-alpha-D-galactofuranose
pH and temperature not specified in the publication, recombinant mutant Q103A
2.153
UDP-alpha-D-galactofuranose
pH and temperature not specified in the publication, recombinant mutant Q107A
0.022
UDP-alpha-D-galactopyranose
pH 7.0, 37°C, mutant R182K
0.0334
UDP-alpha-D-galactopyranose
-
mutant Y317F, pH 7.5, 37°C
0.0425
UDP-alpha-D-galactopyranose
pH 7.0, 37°C, wild-type enzyme
0.0429
UDP-alpha-D-galactopyranose
pH 7.0, 37°C, mutant R327K
0.09
UDP-alpha-D-galactopyranose
-
mutant R327A, pH 7.5, 37°C
0.091
UDP-alpha-D-galactopyranose
-
mutant Y395F, pH 7.5, 37°C
0.1
UDP-alpha-D-galactopyranose
-
mutant Y429F, pH 7.5, 37°C
0.134
UDP-alpha-D-galactopyranose
-
mutant R176A, pH 7.5, 37°C
0.14
UDP-alpha-D-galactopyranose
-
wild-type enzyme, pH 7.5, 37°C
0.607
UDP-alpha-D-galactopyranose
pH 7.0, 37°C, mutant R182A
0.094
UDP-beta-L-arabinofuranose
pH 7.0, 37°C, recombinant wild-type enzyme
0.7
UDP-beta-L-arabinofuranose
pH 7.0, 37°C, recombinant mutant W315A
0.016
UDP-D-galactofuranose
-
in 50 mM MOPS, 10 mM sodium dithionite, 2 mM MgCl2 pH 7.4, at 37°C
0.022
UDP-D-galactofuranose
-
37°C, pH 7.5, in presence of 20 mM sodium dithionite
0.087
UDP-D-galactofuranose
-
in 25 mM HEPES, 125 mM NaCl, 20 mM dithionite, pH 7.5, at 37°C
0.11
UDP-D-galactofuranose
-
in 25 mM HEPES, 125 mM NaCl, 20 mM dithionite, pH 7.5, at 37°C
0.194
UDP-D-galactofuranose
-
37°C, pH 7.5
0.043
UDP-D-galactopyranose
wild-type, pH 8.0
0.205
UDP-D-galactopyranose
mutant E301A, pH 8.0
0.386
UDP-D-galactopyranose
mutant Y185F, pH 8.0
0.619
UDP-D-galactopyranose
mutant Y155F, pH 8.0
0.739
UDP-D-galactopyranose
mutant Y349F, pH 8.0
0.805
UDP-D-galactopyranose
-
in 50 mM MOPS, 10 mM sodium dithionite, 2 mM MgCl2 pH 7.4, at 37°C
0.819
UDP-D-galactopyranose
mutant Y314F, pH 8.0
1.002
UDP-D-galactopyranose
mutant D351A, pH 8.0
0.02
UDP-galactofuranose
-
under reducing conditions
0.022
UDP-galactofuranose
-
-
0.19
UDP-galactofuranose
-
under non-reducing (native) conditions
0.022
UDP-galactopyranose
-
-
0.055
UDP-galactopyranose
-
wild type enzyme, in 50 mM sodium phosphate buffer pH 7.0
additional information
additional information
steady-state kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
-
steady-state kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
-
high-affinity binding to the enzyme is only obtained with the chromophore 5-carboxytetramethylrhodamine, i.e. TAMRA, linked to UDP by either 2 or 6 carbons, 6times less when UDP is linked to fluorescein, kinetics, overview
-
additional information
additional information
-
Michaelis-Menten kinetics of wild-type and mutant enzymes
-
additional information
additional information
Michaelis-Menten kinetics and kinetic solvent viscosity effects with wild-type and mutant enzymes. A strong dependence of the kcat value on solution viscosity is observed when UDP-beta-L-arabinofuranose is used as the substrate with the wild-type enzyme
-
additional information
additional information
-
Michaelis-Menten kinetics and kinetic solvent viscosity effects with wild-type and mutant enzymes. A strong dependence of the kcat value on solution viscosity is observed when UDP-beta-L-arabinofuranose is used as the substrate with the wild-type enzyme
-
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7.4
UDP-(6-deoxy-6-fluoro)-D-galactofuranose
1.4
UDP-2-amino-2-deoxy-D-galactopyranose
-
in 50 mM MOPS, 10 mM sodium dithionite, 2 mM MgCl2 pH 7.4, at 37°C
0.033
UDP-2-deoxy-2-fluoro-D-galactofuranose
-
-
0.0007
UDP-2-deoxy-2-fluoro-D-galactopyranose
-
in 50 mM MOPS, 10 mM sodium dithionite, 2 mM MgCl2 pH 7.4, at 37°C
0.033
UDP-2-fluoro-galactofuranose
-
-
5.7
UDP-3-deoxy-3-fluoro-D-galactofuranose
0.9
UDP-3-deoxy-3-fluoro-D-galactopyranose
-
in 50 mM MOPS, 10 mM sodium dithionite, 2 mM MgCl2 pH 7.4, at 37°C
3.5
UDP-6-deoxy-6-fluoro-D-galactopyranose
-
in 50 mM MOPS, 10 mM sodium dithionite, 2 mM MgCl2 pH 7.4, at 37°C
42.2
UDP-6-deoxy-D-galactopyranose
-
in 50 mM MOPS, 10 mM sodium dithionite, 2 mM MgCl2 pH 7.4, at 37°C
0.03 - 100
UDP-alpha-D-galactofuranose
0.0224 - 13.4
UDP-alpha-D-galactopyranose
0.14 - 0.23
UDP-beta-L-arabinofuranose
1.5 - 72
UDP-D-galactofuranose
0.13 - 35.3
UDP-D-galactopyranose
27
UDP-galactofuranose
-
-
27 - 66
UDP-galactopyranose
12
UDP-L-arabinofuranose
-
-
7.4
UDP-(6-deoxy-6-fluoro)-D-galactofuranose
-
-
7.4
UDP-(6-deoxy-6-fluoro)-D-galactofuranose
-
-
5.7
UDP-3-deoxy-3-fluoro-D-galactofuranose
-
-
5.7
UDP-3-deoxy-3-fluoro-D-galactofuranose
-
-
0.03
UDP-alpha-D-galactofuranose
pH and temperature not specified in the publication, recombinant mutant Y100A
0.13
UDP-alpha-D-galactofuranose
pH and temperature not specified in the publication, recombinant mutant N207A
0.14
UDP-alpha-D-galactofuranose
pH and temperature not specified in the publication, recombinant mutant Q103A
0.17
UDP-alpha-D-galactofuranose
pH and temperature not specified in the publication, recombinant mutant Y104A
0.27
UDP-alpha-D-galactofuranose
pH 7.0, 37°C, recombinant mutant W315A
0.28
UDP-alpha-D-galactofuranose
pH and temperature not specified in the publication, recombinant mutant Y317A
0.3
UDP-alpha-D-galactofuranose
pH and temperature not specified in the publication, recombinant mutant Y317A
4.7
UDP-alpha-D-galactofuranose
pH and temperature not specified in the publication, recombinant mutant Q107A
13.4
UDP-alpha-D-galactofuranose
pH and temperature not specified in the publication, recombinant wild-type enzyme
71
UDP-alpha-D-galactofuranose
-
pH and temperature not specified in the publication, recombinant wild-type enzyme
72
UDP-alpha-D-galactofuranose
pH and temperature not specified in the publication, recombinant wild-type enzyme
100
UDP-alpha-D-galactofuranose
pH 7.0, 37°C, recombinant wild-type enzyme
0.0224
UDP-alpha-D-galactopyranose
-
mutant R176A, pH 7.5, 37°C
0.079
UDP-alpha-D-galactopyranose
pH 7.0, 37°C, mutant R182A
0.12
UDP-alpha-D-galactopyranose
pH 7.0, 37°C, mutant R327K
0.248
UDP-alpha-D-galactopyranose
-
mutant Y395F, pH 7.5, 37°C
0.291
UDP-alpha-D-galactopyranose
-
mutant Y317F, pH 7.5, 37°C
0.44
UDP-alpha-D-galactopyranose
pH 7.0, 37°C, mutant R182K
4.26
UDP-alpha-D-galactopyranose
-
mutant R327A, pH 7.5, 37°C
6.296
UDP-alpha-D-galactopyranose
-
mutant Y429F, pH 7.5, 37°C
8.72
UDP-alpha-D-galactopyranose
pH 7.0, 37°C, wild-type enzyme
13.4
UDP-alpha-D-galactopyranose
-
wild-type enzyme, pH 7.5, 37°C
0.14
UDP-beta-L-arabinofuranose
pH 7.0, 37°C, recombinant wild-type enzyme
0.23
UDP-beta-L-arabinofuranose
pH 7.0, 37°C, recombinant mutant W315A
1.5
UDP-D-galactofuranose
-
37°C, pH 7.5
5
UDP-D-galactofuranose
-
in 25 mM HEPES, 125 mM NaCl, 20 mM dithionite, pH 7.5, at 37°C
27
UDP-D-galactofuranose
-
37°C, pH 7.5, in presence of 20 mM sodium dithionite
36.8
UDP-D-galactofuranose
-
in 50 mM MOPS, 10 mM sodium dithionite, 2 mM MgCl2 pH 7.4, at 37°C
72
UDP-D-galactofuranose
-
in 25 mM HEPES, 125 mM NaCl, 20 mM dithionite, pH 7.5, at 37°C
0.13
UDP-D-galactopyranose
mutant D351A, pH 8.0
0.3
UDP-D-galactopyranose
mutant E301A, pH 8.0
1.3
UDP-D-galactopyranose
mutant Y185F, pH 8.0
1.7
UDP-D-galactopyranose
mutant Y349F, pH 8.0
3.6
UDP-D-galactopyranose
mutant Y155F, pH 8.0
5.2
UDP-D-galactopyranose
mutant Y314F, pH 8.0
5.5
UDP-D-galactopyranose
wild-type, pH 8.0
35.3
UDP-D-galactopyranose
-
in 50 mM MOPS, 10 mM sodium dithionite, 2 mM MgCl2 pH 7.4, at 37°C
27
UDP-galactopyranose
-
-
66
UDP-galactopyranose
-
wild type enzyme, in 50 mM sodium phosphate buffer pH 7.0
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evolution
conserved active site residues in Aspegillus fumigatus UGM compared to prokaryotic UGMs, overview
evolution
-
substrate recognition of bacterial and eukaryotic enzyme, involving a dynamic Arg, conserved steric interactions, and enzyme-substrate noncovalent interactions, overview. Domain 1 is important for positioning Galp for nucleophilic attack, domain 2 provides most of the interactions with the uridine group, and domain 3 figures prominently in binding the diphosphate
evolution
-
substrate recognition of bacterial and eukaryotic enzyme, involving a dynamic Arg, conserved steric interactions, and enzyme-substrate noncovalent interactions, overview. Domain 1 is important for positioning Galp for nucleophilic attack, domain 2 provides most of the interactions with the uridine group, and domain 3 figures prominently in binding the diphosphate
evolution
-
substrate recognition of bacterial and eukaryotic enzyme, involving a dynamic Arg, conserved steric interactions, and enzyme-substrate noncovalent interactions, overview. Domain 1 is important for positioning Galp for nucleophilic attack, domain 2 provides most of the interactions with the uridine group, and domain 3 figures prominently in binding the diphosphate
evolution
-
substrate recognition of bacterial and eukaryotic enzyme, involving a dynamic Arg, conserved steric interactions, and enzyme-substrate noncovalent interactions, overview. Domain 1 is important for positioning Galp for nucleophilic attack, domain 2 provides most of the interactions with the uridine group, and domain 3 figures prominently in binding the diphosphate
evolution
-
substrate recognition of bacterial and eukaryotic enzyme, involving a dynamic Arg, conserved steric interactions, and enzyme-substrate noncovalent interactions, overview. Domain 1 is important for positioning Galp for nucleophilic attack, domain 2 provides most of the interactions with the uridine group, and domain 3 figures prominently in binding the diphosphate
evolution
-
substrate recognition of bacterial and eukaryotic enzyme, involving a dynamic Arg, conserved steric interactions, and enzyme-substrate noncovalent interactions, overview. Domain 1 is important for positioning Galp for nucleophilic attack, domain 2 provides most of the interactions with the uridine group, and domain 3 figures prominently in binding the diphosphate
evolution
-
substrate recognition of bacterial and eukaryotic enzyme, involving a dynamic Arg, conserved steric interactions, and enzyme-substrate noncovalent interactions, overview. Domain 1 is important for positioning Galp for nucleophilic attack, domain 2 provides most of the interactions with the uridine group, and domain 3 figures prominently in binding the diphosphate
evolution
-
substrate recognition of bacterial and eukaryotic enzyme, involving a dynamic Arg, conserved steric interactions, and enzyme-substrate noncovalent interactions, overview. Domain 1 is important for positioning Galp for nucleophilic attack, domain 2 provides most of the interactions with the uridine group, and domain 3 figures prominently in binding the diphosphate
evolution
-
substrate recognition of bacterial and eukaryotic enzyme, involving a dynamic Arg, conserved steric interactions, and enzyme-substrate noncovalent interactions, overview. Domain 1 is important for positioning Galp for nucleophilic attack, domain 2 provides most of the interactions with the uridine group, and domain 3 figures prominently in binding the pyrophosphate
evolution
-
the enzyme is a member of the UGM family
evolution
-
all organisms that generate Galf-containing glycans encode a UGM homologue
evolution
-
all organisms that generate Galf-containing glycans encode a UGM homologue
evolution
all organisms that generate Galf-containing glycans encode a UGM homologue
evolution
all organisms that generate Galf-containing glycans encode a UGM homologue
evolution
the enzyme belongs to the group of flavoenzymes, a unifying concept of flavin hot spots is introduced to understand and categorize the mechanisms and reactivities of both traditional and noncanonical flavoenzymes. The major hot spots of reactivity include the N5, C4a, and C4O atoms of the isoalloxazine, and the 20 hydroxyl of the ribityl chain. The role of hot spots in traditional flavoenzymes, such as monooxygenases, and description of flavin hot spots in noncanonical flavoenzymes, overview
evolution
-
substrate recognition of bacterial and eukaryotic enzyme, involving a dynamic Arg, conserved steric interactions, and enzyme-substrate noncovalent interactions, overview. Domain 1 is important for positioning Galp for nucleophilic attack, domain 2 provides most of the interactions with the uridine group, and domain 3 figures prominently in binding the diphosphate
-
evolution
-
the enzyme is a member of the UGM family
-
malfunction
-
glf-1 mutants display significant late embryonic and larval lethality, and other phenotypes indicative of defective surface coat synthesis, the glycan-rich outermost layer of the nematode cuticle
malfunction
-
Aspergillus nidulans strains deleted for UgmA lack immunolocalizable UDP-D-galactofuranose, have growth and sporulation defects, abnormal wall architecture, and significantly larger hyphal surface subunits and lower cell wall viscoelastic moduli
malfunction
AfUgmA residues R182 and R327 are important for its function in vivo, with even conservative amino (RK) substitutions producing AnugmADELTA-phenotype strains. Loss of cell wall alpha-D-galactofuranose is associated with increased hyphal surface adhesion. AfUgmA active site mutations do not affect UgmA-GFP cytoplasmic distribution. Mutant phenotypes, overview
malfunction
deletion or repression of Aspergillus nidulans gene ugmA (AnugmA), involved in galactofuranose biosynthesis, impairs growth and increases sensitivity to caspofungin, a beta-1,3-glucan synthesis antagonist. Alteration in galactofuranose affects wall glucan composition in Aspergillus nidulans. Wild-type and complemented wild-type hyphal walls have relatively low alpha-glucan content compared to mutant and AnugmADELTA strains. Mutant phenotypes, overview
malfunction
kinetic parameters for the reduction of AfUGM mutant enzymes by NADPH compared to wild-type enzyme, overview. The active site mutants show high losses of catalytic efficiency compared to the wild-type
malfunction
-
the active site mutant shows high losses of catalytic efficiency compared to the wild-type enzyme
malfunction
the active site mutants show high losses of catalytic efficiency compared to the wild-type
malfunction
the UGM H63A lacks catalytic activity
malfunction
without residue His63, the distance between the FAD C4OH and the Galp O5 is not decreased by bending of the flavin ring preventing the proton transfer step. Therefore, the reaction will stall at the FAD-Galp step, accounting for why this intermediate is observed in the AfUGMH63A structure
malfunction
-
deletion or repression of Aspergillus nidulans gene ugmA (AnugmA), involved in galactofuranose biosynthesis, impairs growth and increases sensitivity to caspofungin, a beta-1,3-glucan synthesis antagonist. Alteration in galactofuranose affects wall glucan composition in Aspergillus nidulans. Wild-type and complemented wild-type hyphal walls have relatively low alpha-glucan content compared to mutant and AnugmADELTA strains. Mutant phenotypes, overview
-
malfunction
-
glf-1 mutants display significant late embryonic and larval lethality, and other phenotypes indicative of defective surface coat synthesis, the glycan-rich outermost layer of the nematode cuticle
-
physiological function
-
glf-1 is required for normal post-embryonic development
physiological function
-
UDP-galactopyranose mutase is a virulence factor in Leishmania major
physiological function
-
UgmA is important for cell wall surface subunit organization and wall viscoelasticity
physiological function
-
the enzyme is involved in the biosynthesis of capsular polysaccharides in Campylobacter jejuni 11168. These capsular polysaccharides are known virulence factors that are required for adhesion and invasion of human epithelial cells. Production of suitable quantities of the sugar nucleotide substrate required for the assembly of a capsular polysaccharide containing N-acetyl-alpha-D-galactofuranose, which is essential for viability
physiological function
the enzyme is involved in the synthesis of the cell wall
physiological function
-
the flavoenzyme UDP-galactopyranose mutase catalyzes the conversion of UDP-galactopyranose to UDP-galactofuranose, a precursor of the cell surface beta-galactofuranose that is involved in the virulence of the pathogen
physiological function
-
UDP-galactopyranose mutase catalyzes the isomerization of UDP-galactopyranose to UDP-galactofuranose, the biosynthetic precursor of galactofuranose residues, which are essential components of the cell wall and play an important role in Aspergillus fumigatus virulence
physiological function
galactofuranose (Galf) biosynthesis begins with the conversion of UDP-galactopyranose (UDP-Galp) to UDP-Galf as a rate-limiting step catalyzed by the flavoenzyme UDP-galactopyranose mutase (UGM). Enzyme UGM is essential for the survival and proliferation of several pathogens. UGM from the pathogenic fungus Aspergillus fumigatus also catalyzes the isomerization of UDP-arabinopyranose (UDP-Arap), which differs from UDPGalp by lacking a -CH2-OH substituent at the C5 position of the hexose ring
physiological function
-
the enzyme catalyzes the formation of UDP-galactofuranose (UDP-Galf), which is required to produce Galf-containing glycoconjugates
physiological function
-
the enzyme catalyzes the formation of UDP-galactofuranose (UDP-Galf), which is required to produce Galf-containing glycoconjugates
physiological function
the enzyme catalyzes the formation of UDP-galactofuranose (UDP-Galf), which is required to produce Galf-containing glycoconjugates
physiological function
the enzyme catalyzes the formation of UDP-galactofuranose (UDP-Galf), which is required to produce Galf-containing glycoconjugates
physiological function
-
the enzyme UDP-galactopyranose mutase (UGM) catalyses the conversion of galactopyranose into galactofuranose. It is critical for the survival and proliferation of several pathogenic agents, both prokaryotic and eukaryotic
physiological function
-
UDP-alpha-D-galactopyranose (UDP-Galp) is a precursor of galactofuranose (Galf), which is a primary component of the cell-wall glycans of several microorganisms. The interconversion of UDP-Galp and UDP-Galf is catalyzed by UDP galactopyranose mutase (UGM)
physiological function
-
UDP-galactopyranose mutase (UGM) catalyzes the interconversion between UDP-galactopyranose and UDPgalactofuranose. Galactofuranose is found in bacterial and fungal cell walls and is a cell surface virulence factor in protozoan parasites. UGMs are active only in the reduced form
physiological function
UDP-galactopyranose mutase (UGM) catalyzes the interconversion between UDP-galactopyranose and UDPgalactofuranose. Galactofuranose is found in bacterial and fungal cell walls and is a cell surface virulence factor in protozoan parasites. UGMs are active only in the reduced form
physiological function
UDP-galactopyranose mutase (UGM) catalyzes the interconversion between UDP-galactopyranose and UDPgalactofuranose. Galactofuranose is found in bacterial and fungal cell walls and is a cell surface virulence factor in protozoan parasites. UGMs are active only in the reduced form
physiological function
UDP-galactopyranose mutase (UGM) is a flavin-containing enzyme that catalyzes the reversible conversion of UDP-galactopyranose (UDP-Galp) to UDP-galactofuranose (UDP-Galf) and plays a key role in the biosynthesis of the mycobacterial cell wall galactofuran. Substrate binding induces local changes in MtUGM active site
physiological function
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UDP-galactopyranose mutase (UGM) is a key enzyme in the biosynthesis of mycobacterial cell walls. Galactofuranose (Galf) is an essential building block of the galactan chains in the cell walls of mycobacteria
physiological function
UDP-galactopyranose mutase (UGM) plays an essential role in galactofuranose biosynthesis in pathogens by catalyzing the conversion of UDP-galactopyranose to UDP-galactofuranose
physiological function
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UDP-galactopyranose mutase (UGM), an enzyme found in many eukaryotic and prokaryotic human pathogens, catalyzes the interconversion of UDP-galactopyranose (UDP-Galp) and UDPgalactofuranose (UDP-Galf), the latter being used as the biosynthetic precursor of the galactofuranose polymer portion of the mycobacterium cell wall
physiological function
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glf-1 is required for normal post-embryonic development
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physiological function
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the enzyme is involved in the biosynthesis of capsular polysaccharides in Campylobacter jejuni 11168. These capsular polysaccharides are known virulence factors that are required for adhesion and invasion of human epithelial cells. Production of suitable quantities of the sugar nucleotide substrate required for the assembly of a capsular polysaccharide containing N-acetyl-alpha-D-galactofuranose, which is essential for viability
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additional information
Arg182 and Arg327 play important roles in stabilizing the position of the diphosphates of the nucleotide sugar and help to facilitate the positioning of the galactose moiety for catalysis. Substrate recognition and structural changes observed upon substrate binding involving the mobile loops and the critical arginine residues Arg182 and Arg327, overview. The Aspergillus fumigatus enzyme contains a third flexible loop (loop III) above the si-face of the isoalloxazine ring that changes position depending on the redox state of the flavin cofactor
additional information
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Arg182 and Arg327 play important roles in stabilizing the position of the diphosphates of the nucleotide sugar and help to facilitate the positioning of the galactose moiety for catalysis. Substrate recognition and structural changes observed upon substrate binding involving the mobile loops and the critical arginine residues Arg182 and Arg327, overview. The Aspergillus fumigatus enzyme contains a third flexible loop (loop III) above the si-face of the isoalloxazine ring that changes position depending on the redox state of the flavin cofactor
additional information
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enzyme-substrate binding analysis by combination of UV/visible spectroscopy, X-ray crystallography, saturation transfer difference NMR spectroscopy, molecular dynamics, and CORCEMA-ST calculations. Two arginines in the enzyme, Arg59 and Arg168, play critical roles in the catalytic mechanism of the enzyme and in controlling its specificity to ultimately lead to an N-acetyl-alpha-D-galactofuranose-containing capsular polysaccharides. Substrate-recognition patterns compared to the Eschericia coli enzyme, overview
additional information
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molecular details of the mechanism that controls the uptake and retention of the substrate in the presence or absence of an active site ligand, overview. Interactions with the substrate diphosphate moiety are especially important for stabilizing the closed active site. Protein dynamics play a key role in substrate recognition by UDP-galactopyranose mutases. Residues Arg176, Asn201, and Tyr317, Tyr34, Tyr429, and Arg327 are involved in the active site
additional information
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molecular dynamics studies of active site flexibility, overview
additional information
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molecular dynamics studies of active site flexibility, overview
additional information
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molecular dynamics studies of active site flexibility, overview
additional information
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molecular dynamics studies of active site flexibility, overview
additional information
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molecular dynamics studies of active site flexibility, overview
additional information
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molecular dynamics studies of active site flexibility, overview
additional information
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molecular dynamics studies of active site flexibility, overview
additional information
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substrate recognition mechanism, overview. Molecular dynamics studies of active site flexibility, overview
additional information
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substrate recognition mechanism, overview. Molecular dynamics studies of active site flexibility, overview
additional information
active site structure, the citrate ion forms salt bridges with UGM residues R288 and H290 and numerous ordered water molecules, thereby participating in a hydrogen-bonding network with the active site residues. A strong density feature is observed bridging the citrate ion and the oxidized FAD
additional information
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active site structure, the citrate ion forms salt bridges with UGM residues R288 and H290 and numerous ordered water molecules, thereby participating in a hydrogen-bonding network with the active site residues. A strong density feature is observed bridging the citrate ion and the oxidized FAD
additional information
AfUgmA residues R182 and R327 are important for its function in vivo, with even conservative amino (RK) substitutions producing AnugmADELTA phenotype strains
additional information
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AfUgmA residues R182 and R327 are important for its function in vivo, with even conservative amino (RK) substitutions producing AnugmADELTA phenotype strains
additional information
analysis of the structure of the UGM adduct in combination with quantum mechanics/molecular mechanics (QM/MM) molecular dynamics studies, overview. The simulations indicate that after formation of the N5-galactose adduct, the next step is deprotonation of the N5-atom by the C4O. The distance between the N5-H and the C4O in the reduced FAD is 2.4 A (from about 2.7 A in the oxidized form) due to bending of the flavin. Molecular dynamics simulations indicate that the bending is further increased in the transition state, decreasing the distance between these two atoms to 1.5 A. This process is stabilized by interactions of the positively charged His63 with the electron rich flavin. The next step in the reaction is opening of the sugar ring. This step is coupled to the formation of the N5-iminum ion and is facilitated by protonation of Galp O5 atom. Bending of the flavin, which brings the FAD C4OH and the Galp O5 together for proton transfer, is also required in this step. The Galp O5 atom is shifts 1.2 A towards the FAD C4O in the FADGalp adduct structure. Formation of the FAD-Galp-iminium ion activates the Galp C1 for attack by the C4-OH to generate the furanose form of the sugar. Deprotonation of the sugar C4-OH prior to this step is facilitated by the FAD C4O atom. The proton now at the FAD C4O position is then transferred back to the FAD N5 atom. The final step is the attack of the Galf C1 by UDP to form UDP-Galf, which yields the reduced flavin
additional information
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enzyme TcUGM active site structure, overview
additional information
molecular dynamics simulations. Binding modes of substrates in the active site of enzyme AfUGM
additional information
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molecular dynamics simulations. Binding modes of substrates in the active site of enzyme AfUGM
additional information
residues F66, Y104, Q107, N207, and Y317 are important for promoting the transition state conformation for UDP-galactofuranose formation. The active site residues are conserved in eukaryotic UGMs but are absent or different in bacterial UGMs
additional information
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residues F66, Y104, Q107, N207, and Y317 are important for promoting the transition state conformation for UDP-galactofuranose formation. The active site residues are conserved in eukaryotic UGMs but are absent or different in bacterial UGMs
additional information
residues H66, Y100, Q103, N201, and Y317 are important for promoting the transition state conformation for UDP-galactofuranose formation. The active site residues are conserved in eukaryotic UGMs but are absent or different in bacterial UGMs
additional information
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residues H66, Y100, Q103, N201, and Y317 are important for promoting the transition state conformation for UDP-galactofuranose formation. The active site residues are conserved in eukaryotic UGMs but are absent or different in bacterial UGMs
additional information
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residues H68 is important for promoting the transition state conformation for UDP-galactofuranose formation
additional information
structure analysis reveals UDP bound in the active site and galactopyranose linked to the FAD through a covalent bond between the anomeric C of galactopyranose and N5 of the FAD. The structure confirms the role of the flavin as nucleophile and supports the hypothesis that the proton destined for O5 of galactofuranose is shuttled from N5 of the FAD via O4 of the FAD. His63 is part of the conserved histidine loop, which has the sequence GGHVIF in AfUGM. All UGMs have Gly and His at positions 1 and 3 of the loop, respectively. The conformation of the His loop of AfUGM depends on the redox state of the flavin. The protein-flavin interactions are thought be essential for maintaining the active conformation of UGM
additional information
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substrate recognition mechanism, overview. Molecular dynamics studies of active site flexibility, overview
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additional information
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enzyme-substrate binding analysis by combination of UV/visible spectroscopy, X-ray crystallography, saturation transfer difference NMR spectroscopy, molecular dynamics, and CORCEMA-ST calculations. Two arginines in the enzyme, Arg59 and Arg168, play critical roles in the catalytic mechanism of the enzyme and in controlling its specificity to ultimately lead to an N-acetyl-alpha-D-galactofuranose-containing capsular polysaccharides. Substrate-recognition patterns compared to the Eschericia coli enzyme, overview
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crystal structure analysis, two crystal forms, hexagonal and triclinic
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purified ligand-free recombinant oxidized mutant enzyme variants F66A, Y104A, Q107A, N207A, and Y317A, grown in sitting drops at room temperature with a reservoir solution containing 1.2-1.4 M ammonium sulfate and 0.1 M sodium acetate at pH 4.5, equal volumes of protein solution, containing 5-9 mg/ml enzyme in 125 mM NaCl, 25 mM HEPES, pH 7.5, and 1 mM Tris(3-hydroxypropyl)phosphine, and reservoir solution are mixed, and large yellow hexagonal crystals are obtained. Crystals of reduced, ligand-free AfUGM mutant enzymes and of reduced mutants AfUGMF66A, AfUGMN207A, and AfUGMY317A in complex with UDP are obtained by exchanging the mother liquor of the respective oxidized crystal with a reducing cryobuffer containing 1.6 M ammonium sulfate, 0.2 M sodium acetate pH 4.5, 25% ethylene glycol or glycerol, and 80 mM dithionite, with or without 200 mM UDP, AfUGM is fully reduced in solution by 80 mM dithionite, and the yellow color of the crystals is bleached upon soaking, consistent with reduction, X-ray diffraction structure determination and analysis at 2.05-2.30 A resolution
purified recombinant enzyme mutant H63A with bound UDP-alpha-D-galactopyranose substrate, X-ray diffraction structure determination and analysis. In crystallo capture of a covalent intermediate in the UDP-galactopyranose mutase reaction, structure analysis, detailed overview
purified recombinant enzyme, sitting drop vapour diffusion method, mixing of 500 nl 15 mg/ml protein solution with 500 nl reservoir solution, containing 0.1 M HEPES, pH 7.5, 20% PEG 3350, 0.4 M ammonium sulfate, 4% formamide, and equilibration against 0.07 ml reservoir solution, for enzyme complex crystals, the enzyme is incubated for 10 min on ice with various substrate/inhibitor/reducing ligands 10 mM UDP-Galp, 10 mM UDP, 5 mM UDP-glucose, 5-20 mM sodium dithionite, respectively, before crystallization, 2 days, X-ray diffraction structure determination and analysis at 3.25 A resolution. Incorporation of selenomethionine is achieved, but the resulting crystals do not allow solution of the phase problem
the structure of enzyme mutant AfUGMH63A complexed with the substrate UDP-Galp shows the presence of a C1-galactose-N5-FAD adduct (PDB ID 5HHF), a covalent intermediate bound to AfUGMH63A
wild-type and mutant enzyme in complex with substrate UDP-alpha-D-galactopyranose or with inhibitor UDP, microbatch method at room temperature, for the substrate complex crystals: 10 mg/ml protein in 50 mM Tris, pH 8.0, 5 mM DTT, with 10 mM UDP-alpha-D-galactopyranose, and 10 mM dithionite, for the inhibitor complex crystals: 10 mg/ml protein in 25 mM Tris malonate, pH 8.0, and 10 mM UDP, for mutant enzyme-substrate complexes: 10 mg/ml protein in 25 mM Tris malonate, pH 8.0, with 15 mM UDP-alpha-D-galactopyranose, mixing of equal volumes of protein solution (with or without ligand) and crystallization solution and overlaid with oil, X-ray diffraction structure determination and analysis at 2.3-3.15 A resolution
purified recombinant His6-tagged enzyme in complex with citrate and GSG-tagged enzyme in complex with UDP, by hanging drop vapor diffusion method, mixing of 0.002 ml of 10 mg/ml protein in 20 mM Tris, pH 7.0, with 0.002 ml of reservoir solution containing for the citrate-complexed enzyme 100 mM sodium citrate, pH 5.6, 15% isopropanol, and 16-18% PEG 5000 MME, for 3-4 days, and containing for the UDP-complexed enzyme 100 mM Bis-Tris, pH 5.5, 200 mM lithium sulfate, and 21% PEG 3350, for 1-2 weeks, X-ray diffraction structure determination and analysis at 1.95-2.35 A resolution, molecular replacement using KpUGM monomer structure in an open conformation (PDB ID 2BI7) as template for the citrate-complexed enzyme crystals and the structure of Mycobacterium smegmatis UGM (MsUGM) in a closed conformation (PDB ID 5EQD) for the UDP-complexed enzyme crystals, structure comparisons, overview
crystal structure analysis
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in complex with UDP-CH2-Galp, hanging drop vapor diffusion method, using 0.1 M HEPES (pH 6.5), 0.2 M LiCl, and 28% (w/v) polyethylene glycol 6000
in complex with UDP-galactopyranose and UDP and uridine diphosphate, microbatch under oil method, using 0.1 M HEPES, pH 6.5, 0.2 M lithium chloride and 28% (w/v) PEG 6000
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in complex with UDP-galactopyranose, microbatch-under-oil method, using 0.1 M HEPES pH 7.0, 0.2 M LiCl, and 20% (w/v) PEG 6000
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crystal structure analysis
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FAD is located in a cleft lined with conserved residues
vapour-diffusion method in hanging drops, orthorhombic, space group P21 with a: 71.12 A, b: 58.42 A, c: 96.38 A, beta: 96.38°
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crystal structure analysis
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in complex with UDP-D-glucose
in the (active) reduced state, with FAD, crystal structure at 2.2 A resolution, with FADH-, crystal structure at 2.25 A resolution
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crystal structure analysis
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in the oxidized state, with FAD, crystal structure at 2.25 A resolution
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purified detagged recombinant enzyme complexed with substrate UDP-Galp and inhibitors UDP, UDP-F4-Galf, and UDP-F4-Galp, hanging drop vapour diffusion method, mixing of 0.0012 ml of protein solution containing 6.5 mg/ml enzyme in 25 mM Tris, pH 7.5, 500 mM NaCl, and, added prior to crystallization, 20 mM sodium dithionite (final concentration), with 0.0012 ml of reservoir solution containing 20% PEG 3350, 0.1 M Bis-Tris pH 5.5, and additives, 1-4 weeks, X-ray diffraction structure determination and analysis at 2.25-2.60 A resolution
substrate-bound enzyme in oxidized and reduced forms
crystal structure analysis
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crystal structure analysis, molecular dynamics simulations and modeling, overview
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H63A
site-directed mutagenesis, inactive mutant
N207A
site-directed mutagenesis, the mutant enzyme shows a high decrease in kcat/KM value compared to wild-type, but the mutation does not significantly affect the kinetics of enzyme activation by NADPH. Crystal structure determination of the enzyme ligand-free or in complex with UDP
Q107A
site-directed mutagenesis, the mutant enzyme shows a high decrease in kcat/KM value compared to wild-type, but the mutation does not significantly affect the kinetics of enzyme activation by NADPH. Crystal structure determination of the ligand-free enzyme
W315A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme. The extra space afforded by the absence of the Trp315 wall possibly lowers the free energy barrier of the cyclization step of the catalytic mechanism, allowing product release to become rate-limiting
Y104A
site-directed mutagenesis, the mutant enzyme shows a high decrease in kcat/KM value compared to wild-type, but the mutation does not significantly affect the kinetics of enzyme activation by NADPH. Crystal structure determination of the ligand-free enzyme
Y317A
site-directed mutagenesis, the mutant enzyme shows a high decrease in kcat/KM value compared to wild-type, but the mutation does not significantly affect the kinetics of enzyme activation by NADPH. Crystal structure determination of the enzyme ligand-free or in complex with UDP
D351A
mutation of conserved residue of putative active site cleft. 4% of wild-type activity
E301A
mutation of conserved residue of putative active site cleft. 21% of wild-type activity
R174A
no catalytic activity
R280A
mutation of conserved residue of putative active site cleft. No catalytic activity
W156A
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lower activity than wild-type enzyme
W156Y
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lower activity than wild-type enzyme
Y151F
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lower activity than wild-type enzyme
Y155F
7% of wild-type activity
Y181F
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lower activity than wild-type enzyme
Y185F
11% of wild-type activity
Y311F
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lower activity than wild-type enzyme
Y314F
5% of wild-type activity
Y346F
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lower activity than wild-type enzyme
Y349F
6% of wild-type activity
D322A
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site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type with substrate UDP-alpha-D-galactofuranose
H68A
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site-directed mutagenesis, the mutant shows highly reduced catalytic efficiency compared to wild-type
P306R
site-directed mutagenesis, the mutant shows similar kinetics compared to wild-type. Pro306 is located on the solvent-exposed loop (His300-Lys309) connecting the small helix nu3 and beta strand beta14 of the beta-sheet domain, over 25 A from the FAD. The Cdelta atom of Pro306 is 3.5 A from the main-chain oxygen of Thr53, located on the small sharp turn (Glu52-Gly56) connecting beta strands beta3 and beta4.The Pro306Arg mutation releases this clash and results in a 1 A shift in the position of the two solvent-exposed loops without affecting the position of side chains and interaction with the protein. Arg306 forms a salt bridge with the side chain of Asp308 and the main-chain oxygen of Gln54 and replaces a salt bridge formed by Lys309. The Lys309 side chain has rotated and forms a new salt bridge with Gln54. In addition, Lys309 is involved in crystal contacts with the side chain of Asp202. The Pro306Ala mutation therefore may be stabilizing the two loops and promoting the crystallization of MtUGM complex structures
Y253A
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site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type with substrate UDP-alpha-D-galactofuranose
N201A
site-directed mutagenesis, the mutant shows highly reduced catalytic efficiency compared to wild-type
Q103A
site-directed mutagenesis, the mutant shows highly reduced catalytic efficiency compared to wild-type
R176A
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R327A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y100A
site-directed mutagenesis, the mutant shows highly reduced catalytic efficiency compared to wild-type
Y395F
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y429F
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
F66A
site-directed mutagenesis, the mutant enzyme shows a high decrease in kcat/KM value compared to wild-type, but the mutation does not significantly affect the kinetics of enzyme activation by NADPH. Crystal structure determination of the enzyme ligand-free or in complex with UDP or UDP and substrate UDP-alpha-D-galactopyranose
F66A
site-directed mutagenesis, the residue is located at the end of AfUgmA loop III and may control loop III flipping and consequently opening of the mobile loops depending on the redox state of the cofactor. The colony morphology, cell wall composition, hyphal surface adhesion and response to antifungal drugs of the mutant are altered compared to wild-type
H63N
site-directed mutagenesis, the residue is part of the flexible loop (loop III) above the si-face of the isoalloxazine ring. The colony morphology, cell wall composition, hyphal surface adhesion and response to antifungal drugs of the mutant are altered compared to wild-type
H63N
site-directed mutagenesis, the structure of enzyme mutant AfUGMH63A complexed with the substrate UDP-Galp shows the presence of a C1-galactose-N5-FAD adduct (PDB ID 5HHF)
R182A
site-directed mutagenesis, the mutant is almost inactive
R182A
site-directed mutagenesis, the colony morphology, cell wall composition, hyphal surface adhesion and response to antifungal drugs of the mutant are altered compared to wild-type
R182K
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R182K
site-directed mutagenesis, the colony morphology, cell wall composition, hyphal surface adhesion and response to antifungal drugs of the mutant are altered compared to wild-type
R327A
site-directed mutagenesis, inactive mutant
R327A
site-directed mutagenesis, the colony morphology, cell wall composition, hyphal surface adhesion and response to antifungal drugs of the mutant are altered compared to wild-type
R327K
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R327K
site-directed mutagenesis, the colony morphology, cell wall composition, hyphal surface adhesion and response to antifungal drugs of the mutant are altered compared to wild-type
W160A
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catalytically inert
W160A
mutation of conserved residue on edge putative active site cleft, defective in binding of substrate
W160A
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redox-switched binding affinity of substrate reverses in the W160A mutant where it only binds when oxidized
W70F/W290F
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wild type UGM and the W70F/W290F double mutant show competition of UDP and UDP-galactopyranose for the same site
W70F/W290F
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the double mutant binds substrate in a similar manner to wild type and has comparable enzyme activity (90%)
Y317F
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Y317F
site-directed mutagenesis, the mutant shows highly reduced catalytic efficiency compared to wild-type
additional information
kinetic parameters for the reduction of AfUGM mutant enzymes by NADPH compared to wild-type enzyme, overview
additional information
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kinetic parameters for the reduction of AfUGM mutant enzymes by NADPH compared to wild-type enzyme, overview
additional information
the AfUgmA enzyme deletion mutant shows increased sensitivity to antifungal drugs, particularly caspofungin. Reduced beta-glucan content is correlated with increased caspofungin sensitivity
additional information
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the AfUgmA enzyme deletion mutant shows increased sensitivity to antifungal drugs, particularly caspofungin. Reduced beta-glucan content is correlated with increased caspofungin sensitivity
additional information
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compared to a wild type morphology strain, the UGM-deficient ugmA? strain has aberrant hyphal morphology, producing wide, uneven, highly-branched hyphae, with thick, relatively electron-dense walls
additional information
Construction of an AnugmADELTA enzyme deletion mutant. An Aspergillus fumigatus enzyme AfUgmA mutant with altered enzyme activity is transformed into enzyme-lacking Aspergillus nidulans mutant AnugmDELTA to assess the effect on growth and wall composition in Aspergillus nidulans. The complemented AnugmA::wild-type AfugmA strain has wild-type phenotype. Aspergillus nidulans strains that host mutated AfUgmA constructs with low enzyme activity show increased hyphal surface adhesion, and AnugmAn and AfugmA-mutated Aspergillus nidulans strains have increased alpha-glucan and decreased beta-glucan in their cell walls compared to wild-type and AfugmA-complemented strains
additional information
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Construction of an AnugmADELTA enzyme deletion mutant. An Aspergillus fumigatus enzyme AfUgmA mutant with altered enzyme activity is transformed into enzyme-lacking Aspergillus nidulans mutant AnugmDELTA to assess the effect on growth and wall composition in Aspergillus nidulans. The complemented AnugmA::wild-type AfugmA strain has wild-type phenotype. Aspergillus nidulans strains that host mutated AfUgmA constructs with low enzyme activity show increased hyphal surface adhesion, and AnugmAn and AfugmA-mutated Aspergillus nidulans strains have increased alpha-glucan and decreased beta-glucan in their cell walls compared to wild-type and AfugmA-complemented strains
additional information
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Construction of an AnugmADELTA enzyme deletion mutant. An Aspergillus fumigatus enzyme AfUgmA mutant with altered enzyme activity is transformed into enzyme-lacking Aspergillus nidulans mutant AnugmDELTA to assess the effect on growth and wall composition in Aspergillus nidulans. The complemented AnugmA::wild-type AfugmA strain has wild-type phenotype. Aspergillus nidulans strains that host mutated AfUgmA constructs with low enzyme activity show increased hyphal surface adhesion, and AnugmAn and AfugmA-mutated Aspergillus nidulans strains have increased alpha-glucan and decreased beta-glucan in their cell walls compared to wild-type and AfugmA-complemented strains
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additional information
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gene replacement mutant is deficient in lipophosphoglycan backbone and expresses truncated glycoinositolphospholipids. The structural changes do not influence the in vitro growth but lead to an attenuation of virulence
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Lee, R.; Monsey, D.; Weston, A.; Duncan, K.; Rithner, C.; McNeil, M.
Enzymic synthesis of UDP-galactofuranose and an assay for UDP-galactopyranose mutase based on high-performance liquid chromatography
Anal. Biochem.
242
1-7
1996
Escherichia coli
brenda
Kplin, R.; Brisson, J.R.; Whitfield, C.
UDP-galactofuranose precursor required for formation of the lipopolysaccharide O antigen of Klebsiella pneumoniae serotype O1 is synthesized by the product of the rfbDKPO1 gene
J. Biol. Chem.
272
4121-4128
1997
Klebsiella pneumoniae
brenda
McMahon, S.A.; Leonard, G.A.; Buchanan, L.V.; Giraud, M.F.; Naismith, J.H.
Initiating a crystallographic study of UDP-galactopyranose mutase from Escherichia coli
Acta Crystallogr. Sect. D
55
399-402
1999
Escherichia coli
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brenda
Fullerton, S.W.; Daff, S.; Sanders, D.A.; Ingledew, W.J.; Whitfield, C.; Chapman, S.K.; Naismith, J.H.
Potentiometric analysis of UDP-galactopyranose mutase: stabilization of the flavosemiquinone by substrate
Biochemistry
42
2104-2109
2003
Klebsiella pneumoniae
brenda
Zhang, Q.; Liu, H.w.
Studies of UDP-galactopyranose mutase from Escherichia coli: An unusual role of reduced FAD in its catalysis
J. Am. Chem. Soc.
122
9065-9070
2000
Escherichia coli
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brenda
Sanders, D.A.; Staines, A.G.; McMahon, S.A.; McNeil, M.R.; Whitfield, C.; Naismith, J.H.
UDP-galactopyranose mutase has a novel structure and mechanism
Nat. Struct. Biol.
8
858-863
2001
Klebsiella pneumoniae, Escherichia coli (P37747), Escherichia coli
brenda
Bakker, H.; Kleczka, B.; Gerardy-Schahn, R.; Routier, F.H.
Identification and partial characterization of two eukaryotic UDP-galactopyranose mutases
Biol. Chem.
386
657-661
2005
Aspergillus fumigatus (Q4W1X2), Aspergillus fumigatus, Leishmania major (Q5EEK0), Leishmania major
brenda
Caravano, A.; Sinay, P.; Vincent, S.P.
1,4-Anhydrogalactopyranose is not an intermediate of the mutase catalyzed UDP-galactopyranose/furanose interconversion
Bioorg. Med. Chem. Lett.
16
1123-1125
2006
Mycobacterium tuberculosis
brenda
Beverley, S.M.; Owens, K.L.; Showalter, M.; Griffith, C.L.; Doering, T.L.; Jones, V.C.; McNeil, M.R.
Eukaryotic UDP-galactopyranose mutase (GLF gene) in microbial and metazoal pathogens
Eukaryot. Cell
4
1147-1154
2005
Caenorhabditis elegans, Leishmania major (Q5EEK0), Trypanosoma cruzi (Q5EEK1), Cryptococcus neoformans (Q5KEL8)
brenda
Soltero-Higgin, M.; Carlson, E.E.; Phillips, J.H.; Kiessling, L.L.
Identification of inhibitors for UDP-galactopyranose mutase
J. Am. Chem. Soc.
126
10532-10533
2004
Klebsiella pneumoniae
brenda
Beis, K.; Srikannathasan, V.; Liu, H.; Fullerton, S.W.; Bamford, V.A.; Sanders, D.A.; Whitfield, C.; McNeil, M.R.; Naismith, J.H.
Crystal structures of Mycobacteria tuberculosis and Klebsiella pneumoniae UDP-galactopyranose mutase in the oxidised state and Klebsiella pneumoniae UDP-galactopyranose mutase in the (active) reduced state
J. Mol. Biol.
348
971-982
2005
Klebsiella pneumoniae, Mycobacterium tuberculosis
brenda
Soltero-Higgin, M.; Carlson, E.E.; Gruber, T.D.; Kiessling, L.L.
A unique catalytic mechanism for UDP-galactopyranose mutase
Nat. Struct. Mol. Biol.
11
539-543
2004
Klebsiella pneumoniae
brenda
Chad, J.M.; Sarathy, K.P.; Gruber, T.D.; Addala, E.; Kiessling, L.L.; Sanders, D.A.
Site-directed mutagenesis of UDP-galactopyranose mutase reveals a critical role for the active-site, conserved arginine residues
Biochemistry
46
6723-6732
2007
Klebsiella pneumoniae (Q48485), Klebsiella pneumoniae
brenda
Carlson, E.E.; May, J.F.; Kiessling, L.L.
Chemical probes of UDP-galactopyranose mutase
Chem. Biol.
13
825-837
2006
Klebsiella pneumoniae
brenda
Caravano, A.; Dohi, H.; Sinay, P.; Vincent, S.P.
A new methodology for the synthesis of fluorinated exo-glycals and their time-dependent inhibition of UDP-galactopyranose mutase
Chemistry
12
3114-3123
2006
Escherichia coli
brenda
Kleczka, B.; Lamerz, A.C.; van Zandbergen, G.; Wenzel, A.; Gerardy-Schahn, R.; Wiese, M.; Routier, F.H.
Targeted gene deletion of Leishmania major UDP-galactopyranose mutase leads to attenuated virulence
J. Biol. Chem.
282
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2007
Leishmania major
brenda
Eppe, G.; Peltier, P.; Daniellou, R.; Nugier-Chauvin, C.; Ferrieres, V.; Vincent, S.P.
Probing UDP-galactopyranose mutase binding pocket: A dramatic effect on substitution of the 6-position of UDP-galactofuranose
Bioorg. Med. Chem. Lett.
19
814-816
2008
Escherichia coli, Mycobacterium tuberculosis
brenda
Schmalhorst, P.S.; Krappmann, S.; Vervecken, W.; Rohde, M.; Mueller, M.; Braus, G.H.; Contreras, R.; Braun, A.; Bakker, H.; Routier, F.H.
Contribution of galactofuranose to the virulence of the opportunistic pathogen Aspergillus fumigatus
Eukaryot. Cell
7
1268-1277
2008
Aspergillus fumigatus (Q4W1X2), Aspergillus fumigatus
brenda
El-Ganiny, A.M.; Sanders, D.A.; Kaminskyj, S.G.
Aspergillus nidulans UDP-galactopyranose mutase, encoded by ugmA plays key roles in colony growth, hyphal morphogenesis, and conidiation
Fungal Genet. Biol.
45
1533-1542
2008
Aspergillus nidulans
brenda
Damveld, R.A.; Franken, A.; Arentshorst, M.; Punt, P.J.; Klis, F.M.; van den Hondel, C.A.; Ram, A.F.
A novel screening method for cell wall mutants in Aspergillus niger identifies UDP-galactopyranose mutase as an important protein in fungal cell wall biosynthesis
Genetics
178
873-881
2008
Aspergillus niger, Aspergillus niger RD6.13
brenda
Yuan, Y.; Bleile, D.W.; Wen, X.; Sanders, D.A.; Itoh, K.; Liu, H.W.; Pinto, B.M.
Investigation of binding of UDP-Galf and UDP-[3-F]Galf to UDP-galactopyranose mutase by STD-NMR spectroscopy, molecular dynamics, and CORCEMA-ST calculations
J. Am. Chem. Soc.
130
3157-3168
2008
Klebsiella pneumoniae (Q48485), Klebsiella pneumoniae
brenda
Dykhuizen, E.C.; May, J.F.; Tongpenyai, A.; Kiessling, L.L.
Inhibitors of UDP-galactopyranose mutase thwart mycobacterial growth
J. Am. Chem. Soc.
130
6706-6707
2008
Klebsiella pneumoniae, Mycobacterium tuberculosis, Mycolicibacterium smegmatis
brenda
Liautard, V.; Desvergnes, V.; Itoh, K.; Liu, H.W.; Martin, O.R.
Convergent and stereoselective synthesis of iminosugar-containing Galf and UDP-Galf mimicks: evaluation as inhibitors of UDP-Gal mutase
J. Org. Chem.
73
3103-3115
2008
Escherichia coli
brenda
Dykhuizen, E.C.; Kiessling, L.L.
Potent ligands for prokaryotic UDP-galactopyranose mutase that exploit an enzyme subsite
Org. Lett.
11
193-196
2009
Klebsiella pneumoniae, Mycobacterium tuberculosis
brenda
Yao, X.; Bleile, D.W.; Yuan, Y.; Chao, J.; Sarathy, K.P.; Sanders, D.A.; Pinto, B.M.; ONeill, M.A.
Substrate directs enzyme dynamics by bridging distal sites: UDP-galactopyranose mutase
Proteins
74
972-979
2008
Klebsiella pneumoniae
brenda
Karunan Partha, S.; Bonderoff, S.A.; van Straaten, K.E.; Sanders, D.A.
Expression, purification and preliminary X-ray crystallographic analysis of UDP-galactopyranose mutase from Deinococcus radiodurans
Acta Crystallogr. Sect. F
65
843-845
2009
Deinococcus radiodurans
brenda
Gruber, T.D.; Westler, W.M.; Kiessling, L.L.; Forest, K.T.
X-ray crystallography reveals a reduced substrate complex of UDP-galactopyranose mutase poised for covalent catalysis by flavin
Biochemistry
48
9171-9173
2009
Mycobacterium tuberculosis (P9WIQ1), Mycobacterium tuberculosis
brenda
Novelli, J.F.; Chaudhary, K.; Canovas, J.; Benner, J.S.; Madinger, C.L.; Kelly, P.; Hodgkin, J.; Carlow, C.K.
Characterization of the Caenorhabditis elegans UDP-galactopyranose mutase homolog glf-1 reveals an essential role for galactofuranose metabolism in nematode surface coat synthesis
Dev. Biol.
335
340-355
2009
Caenorhabditis elegans, Caenorhabditis elegans N2
brenda
Caravano, A.; Vincent, S.
Synthesis of three C-glycoside analogues of UDP-galactopyranose as conformational probes for the mutase-catalyzed furanose/pyranose interconversion
Eur. J. Org. Chem.
2009
1771-1780
2009
Escherichia coli
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brenda
Poulin, M.B.; Nothaft, H.; Hug, I.; Feldman, M.F.; Szymanski, C.M.; Lowary, T.L.
Characterization of a bifunctional pyranose-furanose mutase from Campylobacter jejuni 11168
J. Biol. Chem.
285
493-501
2010
Campylobacter jejuni, Campylobacter jejuni 11168
brenda
Gruber, T.D.; Borrok, M.J.; Westler, W.M.; Forest, K.T.; Kiessling, L.L.
Ligand binding and substrate discrimination by UDP-galactopyranose mutase
J. Mol. Biol.
391
327-340
2009
Klebsiella pneumoniae (Q48485), Klebsiella pneumoniae
brenda
Partha, S.K.; van Straaten, K.E.; Sanders, D.A.
Structural basis of substrate binding to UDP-galactopyranose mutase: crystal structures in the reduced and oxidized state complexed with UDP-galactopyranose and UDP
J. Mol. Biol.
394
864-877
2009
Deinococcus radiodurans
brenda
Errey, J.C.; Mann, M.C.; Fairhurst, S.A.; Hill, L.; McNeil, M.R.; Naismith, J.H.; Percy, J.M.; Whitfield, C.; Field, R.A.
Sugar nucleotide recognition by Klebsiella pneumoniae UDP-D-galactopyranose mutase: Fluorinated substrates, kinetics and equilibria
Org. Biomol. Chem.
7
1009-1016
2009
Klebsiella pneumoniae
brenda
Sadeghi-Khomami, A.; Forcada, T.J.; Wilson, C.; Sanders, D.A.; Thomas, N.R.
The UDP-Galp mutase catalyzed isomerization: synthesis and evaluation of 1,4-anhydro-beta-D-galactopyranose and its [2.2.2] methylene homologue
Org. Biomol. Chem.
8
1596-1602
2010
Klebsiella pneumoniae
brenda
Yao, X.; Bleile, D.; Yuan, Y.; Chao, J.; Sarathy, K.; Sanders, D.; Pinto, B.; ONeill, M.
Substrate directs enzyme dynamics by bridging distal sites: UDP-galactopyranose mutase
Proteins Struct. Funct. Bioinform.
74
972-979
2009
Klebsiella pneumoniae
brenda
Oppenheimer, M.; Poulin, M.B.; Lowary, T.L.; Helm, R.F.; Sobrado, P.
Characterization of recombinant UDP-galactopyranose mutase from Aspergillus fumigatus
Arch. Biochem. Biophys.
502
31-38
2010
Aspergillus fumigatus
brenda
Oppenheimer, M.; Valenciano, A.L.; Sobrado, P.
Isolation and characterization of functional Leishmania major virulence factor UDP-galactopyranose mutase
Biochem. Biophys. Res. Commun.
407
552-556
2011
Leishmania major
brenda
Paul, B.C.; El-Ganiny, A.M.; Abbas, M.; Kaminskyj, S.G.; Dahms, T.E.
Quantifying the importance of galactofuranose in Aspergillus nidulans hyphal wall surface organization by atomic force microscopy
Eukaryot. Cell
10
646-653
2011
Aspergillus nidulans
brenda
Borrelli, S.; Zandberg, W.F.; Mohan, S.; Ko, M.; Martinez-Gutierrez, F.; Partha, S.K.; Sanders, D.A.; Av-Gay, Y.; Pinto, B.M.
Antimycobacterial activity of UDP-galactopyranose mutase inhibitors
Int. J. Antimicrob. Agents
36
364-368
2010
Klebsiella pneumoniae, Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
brenda
Partha, S.K.; Sadeghi-Khomami, A.; Slowski, K.; Kotake, T.; Thomas, N.R.; Jakeman, D.L.; Sanders, D.A.
Chemoenzymatic synthesis, inhibition studies, and X-ray crystallographic analysis of the phosphono analog of UDP-Galp as an inhibitor and mechanistic probe for UDP-galactopyranose mutase
J. Mol. Biol.
403
578-590
2010
Klebsiella pneumoniae, Mycobacterium tuberculosis, Deinococcus radiodurans (Q9RYF1), Deinococcus radiodurans
brenda
Penman, G.A.; Lockhart, D.E.; Ferenbach, A.; van Aalten, D.M.
Purification, crystallization and preliminary X-ray diffraction data of UDP-galactopyranose mutase from Aspergillus fumigatus
Acta Crystallogr. Sect. F
68
705-708
2012
Aspergillus fumigatus (Q4W1X2), Aspergillus fumigatus
brenda
Tanner, J.J.; Boechi, L.; Andrew McCammon, J.; Sobrado, P.
Structure, mechanism, and dynamics of UDP-galactopyranose mutase
Arch. Biochem. Biophys.
544
128-141
2014
Aspergillus fumigatus, Deinococcus radiodurans, Escherichia coli, Klebsiella pneumoniae, Leishmania infantum, Leishmania major, Leishmania mexicana, Mycobacterium tuberculosis, Trypanosoma cruzi, Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539
brenda
Poulin, M.B.; Shi, Y.; Protsko, C.; Dalrymple, S.A.; Sanders, D.A.; Pinto, B.M.; Lowary, T.L.
Specificity of a UDP-GalNAc pyranose-furanose mutase: a potential therapeutic target for Campylobacter jejuni infections
ChemBioChem
15
47-56
2014
Campylobacter jejuni, Campylobacter jejuni 11168
brenda
Qi, J.; Oppenheimer, M.; Sobrado, P.
Fluorescence polarization binding assay for Aspergillus fumigatus virulence factor UDP-galactopyranose mutase
Enzyme Res.
2011
513905
2011
Aspergillus fumigatus
brenda
van Straaten, K.E.; Routier, F.H.; Sanders, D.A.
Structural insight into the unique substrate binding mechanism and flavin redox state of UDP-galactopyranose mutase from Aspergillus fumigatus
J. Biol. Chem.
287
10780-10790
2012
Aspergillus fumigatus (Q4W1X2), Aspergillus fumigatus
brenda
Sun, H.G.; Ruszczycky, M.W.; Chang, W.C.; Thibodeaux, C.J.; Liu, H.W.
Nucleophilic participation of reduced flavin coenzyme in mechanism of UDP-galactopyranose mutase
J. Biol. Chem.
287
4602-4608
2012
Mycobacterium tuberculosis
brenda
Boechi, L.; de Oliveira, C.A.; Da Fonseca, I.; Kizjakina, K.; Sobrado, P.; Tanner, J.J.; McCammon, J.A.
Substrate-dependent dynamics of UDP-galactopyranose mutase: implications for drug design
Protein Sci.
22
1490-1501
2013
no activity in Homo sapiens, Trypanosoma cruzi
brenda
Kincaid, V.A.; London, N.; Wangkanont, K.; Wesener, D.A.; Marcus, S.A.; Heroux, A.; Nedyalkova, L.; Talaat, A.M.; Forest, K.T.; Shoichet, B.K.; Kiessling, L.L.
Virtual screening for UDP-galactopyranose mutase ligands identifies a new class of antimycobacterial agents
ACS Chem. Biol.
10
2209-2218
2015
Caenorhabditis elegans, Mycobacterium tuberculosis, Klebsiella pneumoniae (Q48485), Corynebacterium diphtheriae (Q6NER4)
brenda
Sobrado, P.; Tanner, J.J.
Multiple functionalities of reduced flavin in the non-redox reaction catalyzed by UDP-galactopyranose mutase
Arch. Biochem. Biophys.
632
59-65
2017
Aspergillus fumigatus (Q4W1X2)
brenda
Martin Del Campo, J.S.; Eckshtain-Levi, M.; Sobrado, P.
Identification of eukaryotic UDP-galactopyranose mutase inhibitors using the ThermoFAD assay
Biochem. Biophys. Res. Commun.
493
58-63
2017
Aspergillus fumigatus (Q4W1X2), Aspergillus fumigatus, Mycobacterium tuberculosis
brenda
Da Fonseca, I.; Qureshi, I.A.; Mehra-Chaudhary, R.; Kizjakina, K.; Tanner, J.J.; Sobrado, P.
Contributions of unique active site residues of eukaryotic UDP-galactopyranose mutases to substrate recognition and active site dynamics
Biochemistry
53
7794-7804
2014
Mycobacterium tuberculosis, Aspergillus fumigatus (Q4W1X2), Aspergillus fumigatus, Trypanosoma cruzi (Q5EEK1), Trypanosoma cruzi
brenda
Mehra-Chaudhary, R.; Dai, Y.; Sobrado, P.; Tanner, J.J.
In crystallo capture of a covalent intermediate in the UDP-galactopyranose mutase reaction
Biochemistry
55
833-836
2016
Aspergillus fumigatus (Q4W1X2)
brenda
Wangkanont, K.; Winton, V.J.; Forest, K.T.; Kiessling, L.L.
Conformational control of UDP-galactopyranose mutase inhibition
Biochemistry
56
3983-3992
2017
Corynebacterium diphtheriae (Q6NER4), Corynebacterium diphtheriae
brenda
Pierdominici-Sottile, G.; Cossio-Perez, R.; Da Fonseca, I.; Kizjakina, K.; Tanner, J.J.; Sobrado, P.
Steric control of the rate-limiting step of UDP-galactopyranose mutase
Biochemistry
57
3713-3721
2018
Aspergillus fumigatus (Q4W1X2), Aspergillus fumigatus
brenda
Kuppala, R.; Borrelli, S.; Slowski, K.; Sanders, D.A.; Ravindranathan Kartha, K.P.; Pinto, B.M.
Synthesis and biological evaluation of nonionic substrate mimics of UDP-Galp as candidate inhibitors of UDP galactopyranose mutase (UGM)
Bioorg. Med. Chem. Lett.
25
1995-1997
2015
Mycobacterium tuberculosis
brenda
Mahdavi-Amiri, Y.; Mohan, S.; Borrelli, S.; Slowski, K.; Sanders, D.A.; Pinto, B.M.
Mechanism-based candidate inhibitors of uridine diphosphate galactopyranose mutase (UGM)
Carbohydr. Res.
419
1-7
2016
Mycobacterium tuberculosis
brenda
Shi, Y.; Colombo, C.; Kuttiyatveetil, J.R.; Zalatar, N.; van Straaten, K.E.; Mohan, S.; Sanders, D.A.; Pinto, B.M.
A second, druggable binding site in UDP-galactopyranose mutase from Mycobacterium tuberculosis?
ChemBioChem
17
2264-2273
2016
Mycobacterium tuberculosis
brenda
van Straaten, K.E.; Kuttiyatveetil, J.R.; Sevrain, C.M.; Villaume, S.A.; Jimenez-Barbero, J.; Linclau, B.; Vincent, S.P.; Sanders, D.A.
Structural basis of ligand binding to UDP-galactopyranose mutase from Mycobacterium tuberculosis using substrate and tetrafluorinated substrate analogues
J. Am. Chem. Soc.
137
1230-1244
2015
Mycobacterium tuberculosis (P9WIQ1), Mycobacterium tuberculosis
brenda
Pierdominici-Sottile, G.; Cossio Perez, R.; Galindo, J.F.; Palma, J.
QM/MM molecular dynamics study of the galactopyranose -> galactofuranose reaction catalysed by Trypanosoma cruzi UDP-galactopyranose mutase
PLoS ONE
9
e109559
2014
Trypanosoma cruzi
brenda
Alam, M.K.; van Straaten, K.E.; Sanders, D.A.; Kaminskyj, S.G.
Aspergillus nidulans cell wall composition and function change in response to hosting several Aspergillus fumigatus UDP-galactopyranose mutase activity mutants
PLoS ONE
9
e85735
2014
Aspergillus fumigatus (Q4W1X2), Aspergillus fumigatus, Aspergillus nidulans (Q5B8L8), Aspergillus nidulans, Aspergillus nidulans FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139 (Q5B8L8)
brenda