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Information on EC 5.4.99.9 - UDP-galactopyranose mutase and Organism(s) Klebsiella pneumoniae and UniProt Accession Q48485
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5.4.99.9 UDP-galactopyranose mutaseIUBMB Comments
A flavoenzyme which generates UDP-alpha-D-glactofuranose required for cell wall formation in bacteria, fungi, and protozoa.
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Word Map
- 5.4.99.9
- phosphoglycerate
-
methylmalonic
- methylmalonyl-coa
- udp-galactofuranose
-
galactofuranose
- chorismate
-
urogenital
-
udp-galf
- acidemia
-
galf
- adenosylcobalamin
-
methylmalonyl-coenzyme
-
sinus
- prephenate
- acidurias
- succinyl-coa
-
b12-dependent
- 2,3-bisphosphoglycerate
-
bisphosphoglycerate
-
flavoenzyme
-
adocbl
-
cobalamin-dependent
- propionyl-coa
-
adenosylcobalamin-dependent
- drug development
- isobutyryl-coa
-
cofactor-dependent
- shermanii
-
cytodifferentiation
- methylcobalamin
- phosphoenzyme
-
cobiialamin
- analysis
- medicine
- synthesis
The taxonomic range for the selected organisms is: Klebsiella pneumoniae
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
mutase, ugm, udp-galactopyranose mutase, udp-galp mutase, afugm, glf-1, mtugm, galactopyranose mutase, tcugm, udp-gal mutase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Mutase, uridine diphosphogalactopyranose
-
-
-
-
UDP-galactopyranose mutase
UGM
-
-
UDP-galactopyranose mutase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose
mobile loop of enzyme must move in order for enzyme to bind UDP-galactose substrate
UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose
chemical reaction mechanism, overview
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
isomerization
isomerization
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
UDP-D-galactopyranose furanomutase
A flavoenzyme which generates UDP-alpha-D-glactofuranose required for cell wall formation in bacteria, fungi, and protozoa.
CAS REGISTRY NUMBER
COMMENTARY
174632-18-9
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-3''-deoxy-3''-fluoro-D-galactopyranose
UDP-3''-deoxy-3''-fluoro-D-galactofuranose
-
-
-
r
2-fluoro-deoxy-UDP-galactopyranose
2-fluoro-deoxy-UDP-galactofuranose
-
-
-
?
Uridine 5'-(trihydrogen diphosphate) P'-alpha-D-galactopyranosyl ester
Uridine 5'-(trihydrogen diphosphate) P'-alpha-D-galactofuranosyl ester
-
-
-
?
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-galactopyranose
UDP-galactofuranose
-
-
-
-
r
additional information
?
-
UDP-D-glucose is not a substrate for UGM
-
-
?
additional information
?
-
-
UDP-D-glucose is not a substrate for UGM
-
-
?
additional information
?
-
-
no activity with UDP-6-deoxy-Dgalactopyranose, UDP-2-azido-2-deoxy-D-galactopyranose, and UDP-2-acetamido-2-deoxy-D-galactopyranose
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
enzyme UGM possesses a flavin adenine dinucleotide (FAD) cofactor that it uses to catalyze ring contraction of UDP-galactopyranose (UDP-Galp) to form UDP-galactofuranose (UDP-Galf)
FAD
-
exists in a reduced state when the enzyme is catalytically active
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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-(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-(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-(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-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-(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-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-(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
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-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
-
(1R,3S,4R,7R,8S)-3-hydroxymethyl-2,6-dioxa-bicyclo-[2.2.2]-octane-7,8-diol
-
17% inhibition at 4 mM
(4-chlorophenyl)-[1-(4-chlorophenyl)-3-hydroxy-5-methyl-1H-pyrazol-4-yl]-methanone
-
-
1,4-anhydro-beta-D-galactopyranose (1,5-anhydro-alpha-D-galactofuranose)
-
15% inhibition at 4 mM
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-[(5E)-5-(3-bromobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
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-(4-iodophenyl)-2-[4-(3,4-dichlorophenyl)-thiazol-2-ylamino]-propionic acid
-
-
N-[4-oxo-5-(2-oxo-1,2-dihydro-indol-3-ylidene)-thiazolidin-2-ylidene]-benzenesulfonamide
-
-
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)
-
(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
(2Z)-2-(2-chloro-4-hydroxy-5-nitrobenzylidene)[1,3]thiazolo[3,2-a]benzimidazol-3(2H)-one
-
dissociation constant 0.0053 mM, comparison with inhibition of Klebsiella pneumoniae enzyme
(4E)-4-(4-chloro-3-nitrobenzylidene)-1-(3,4-dichlorophenyl)pyrazolidine-3,5-dione
-
comparison with inhibition of Mycobacterium tuberculosis enzyme
(4E)-4-(4-chloro-3-nitrobenzylidene)-1-(3,4-dichlorophenyl)pyrazolidine-3,5-dione
-
dissociation constant 0.0049 mM, comparison with inhibition of Klebsiella pneumoniae enzyme
2-[(5E)-5-(3-bromobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
-
comparison with inhibition of Mycobacterium tuberculosis enzyme
2-[(5E)-5-(3-bromobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
-
dissociation constant 0.0094 mM, comparison with inhibition of Klebsiella pneumoniae enzyme
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.203
UDP-2-deoxy-2-fluoro-D-galactopyranose
-
in 50 mM MOPS, 10 mM sodium dithionite, 2 mM MgCl2 pH 7.4, at 37°C
0.28
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
0.016
UDP-D-galactofuranose
-
in 50 mM MOPS, 10 mM sodium dithionite, 2 mM MgCl2 pH 7.4, at 37°C
0.805
UDP-D-galactopyranose
-
in 50 mM MOPS, 10 mM sodium dithionite, 2 mM MgCl2 pH 7.4, at 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.0007
UDP-2-deoxy-2-fluoro-D-galactopyranose
-
in 50 mM MOPS, 10 mM sodium dithionite, 2 mM MgCl2 pH 7.4, at 37°C
0.9
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
36.8
UDP-D-galactofuranose
-
in 50 mM MOPS, 10 mM sodium dithionite, 2 mM MgCl2 pH 7.4, at 37°C
35.3
UDP-D-galactopyranose
-
in 50 mM MOPS, 10 mM sodium dithionite, 2 mM MgCl2 pH 7.4, at 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0016
2-[5-(3-bromo-benzylidene)-4-oxo-2-thioxo-thiazolidin-3-yl]-3-phenyl-propionic acid
-
-
0.0046
2-[[2-(4-bromo-phenyl)-1,3-dioxo-2,3-dihydro-1H-isoindole-5-carbonyl]-amino]-benzoic acid
-
-
0.017
N-[4-oxo-5-(2-oxo-1,2-dihydro-indol-3-ylidene)-thiazolidin-2-ylidene]-benzenesulfonamide
-
-
0.0013
uridine-5'-diphospho-(N-fluoresceinisothiocyano)hexanolamine
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.004 - 0.035
(2Z)-2-(2-chloro-4-hydroxy-5-nitrobenzylidene)[1,3]thiazolo[3,2-a]benzimidazol-3(2H)-one
0.044
(4-chlorophenyl)-[1-(4-chlorophenyl)-3-hydroxy-5-methyl-1H-pyrazol-4-yl]-methanone
Klebsiella pneumoniae
-
pH and temperature not specified in the publication
0.004 - 0.041
(4E)-4-(4-chloro-3-nitrobenzylidene)-1-(3,4-dichlorophenyl)pyrazolidine-3,5-dione
0.0046
2-(([2-(4-bromophenyl)-1,3-dioxo-2,3-dihydro-1H-isoindol-5-yl]carbonyl)amino)benzoic acid
Klebsiella pneumoniae
-
pH 7.0, 37°C
0.0016 - 0.065
2-[(5E)-5-(3-bromobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
0.0072
3-(4-iodophenyl)-2-[4-(3,4-dichlorophenyl)-thiazol-2-ylamino]-propionic acid
Klebsiella pneumoniae
-
pH and temperature not specified in the publication
0.479
UDP-CH2-Galp
Klebsiella pneumoniae
-
in 50 mM sodium phosphate buffer (pH 7.0), at 22°C
0.004
(2Z)-2-(2-chloro-4-hydroxy-5-nitrobenzylidene)[1,3]thiazolo[3,2-a]benzimidazol-3(2H)-one
Klebsiella pneumoniae
-
pH 7.0, 37°C
0.035
(2Z)-2-(2-chloro-4-hydroxy-5-nitrobenzylidene)[1,3]thiazolo[3,2-a]benzimidazol-3(2H)-one
Klebsiella pneumoniae
-
pH 7.0, 37°C
0.004
(4E)-4-(4-chloro-3-nitrobenzylidene)-1-(3,4-dichlorophenyl)pyrazolidine-3,5-dione
Klebsiella pneumoniae
-
pH 7.0, 37°C
0.041
(4E)-4-(4-chloro-3-nitrobenzylidene)-1-(3,4-dichlorophenyl)pyrazolidine-3,5-dione
Klebsiella pneumoniae
-
pH 7.0, 37°C
0.0016
2-[(5E)-5-(3-bromobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
Klebsiella pneumoniae
-
pH 7.0, 37°C
0.065
2-[(5E)-5-(3-bromobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
Klebsiella pneumoniae
-
pH 7.0, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
all organisms that generate Galf-containing glycans encode a UGM homologue
physiological function
the enzyme catalyzes the formation of UDP-galactofuranose (UDP-Galf), which is required to produce Galf-containing glycoconjugates
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
additional information
-
molecular dynamics studies of active site flexibility, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
-
the dimer is a semicircular particle with the interface formed by domain 2 of one protomer packing against the beta-sheet of domain 3 of another protomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in the (active) reduced state, with FAD, crystal structure at 2.2 A resolution, with FADH-, crystal structure at 2.25 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
R280A
mutation of conserved residue of putative active site cleft. No catalytic activity
W160A
mutation of conserved residue on edge putative active site cleft, defective in binding of substrate
W160A
W70F/W290F
W160A
-
redox-switched binding affinity of substrate reverses in the W160A mutant where it only binds when oxidized
W70F/W290F
-
wild type UGM and the W70F/W290F double mutant show competition of UDP and UDP-galactopyranose for the same site
W70F/W290F
-
the double mutant binds substrate in a similar manner to wild type and has comparable enzyme activity (90%)
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ugmA, recombinant expression in Escherichia coli strain BL21(DE3)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
high-throughput fluorescence polarization assay for indentification of inhibitors of enzyme and homologues
drug development
-
blocking the incorporation of the product galactofuranose into polysaccharides essential for pathogen viability or virulence may lead to novel therapeutics
synthesis
-
production of uridine 5'-(trihydrogen diphosphate) P'-alpha-D-galactofuranosyl ester, a precursor required for the formation of the lipopolysaccharide O-antigen of Klebsiella pneumoniae serotype O1
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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
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
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
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
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
Carlson, E.E.; May, J.F.; Kiessling, L.L.
Chemical probes of UDP-galactopyranose mutase
Chem. Biol.
13
825-837
2006
Klebsiella pneumoniae
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
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
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
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
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
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
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
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
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
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
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
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)
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