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Information on EC 5.4.99.9 - UDP-galactopyranose mutase
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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
- methylmalonyl-coa
-
methylmalonic
- udp-galactofuranose
-
galactofuranose
- chorismate
-
urogenital
-
udp-galf
-
methylmalonyl-coenzyme
- acidemia
-
sinus
-
galf
- adenosylcobalamin
- prephenate
- succinyl-coa
- acidurias
-
b12-dependent
-
flavoenzyme
-
bisphosphoglycerate
- propionyl-coa
- drug development
-
adocbl
- 2,3-bisphosphoglycerate
-
adenosylcobalamin-dependent
-
cobalamin-dependent
-
cofactor-dependent
-
cytodifferentiation
- phosphoenzyme
- methylcobalamin
- isobutyryl-coa
- shermanii
-
cobiialamin
-
furanose
- galactan
- medicine
- synthesis
- analysis
The enzyme appears in viruses and cellular organisms
Synonyms
mutase, ugm, udp-galactopyranose mutase, udp-galp mutase, afugm, glf-1, mtugm, galactopyranose mutase, tcugm, udp-gal mutase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ANIA_03112
galactopyranose mutase
Glf
GLF gene product
GLF-1
MtUGM
mutase
UDP-galactopyranose mutase
UDP-Galp mutase
UGM
UgmA
UNGM
uridine 5'-diphosphate galactopyranose mutase
uridine 5'-diphosphate-galactopyranose mutase
UGM
-
UGM
the key enzyme of galactofuranose metabolism controls the biosynthesis of galactomannan and galactofuranose containing glycoconjugates
UGM
-
-
UGM
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose
-
-
-
-
UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose
catalytic mechanism, overview
-
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
-
UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose
chemical reaction mechanism, overview
-
UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose
chemical reaction mechanism, overview
-
UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose
chemical reaction mechanism, overview
-
UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose
chemical reaction mechanism, overview
-
UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose
reaction mechanism, overview. FAD-UDP-alpha-D-galactopyranose/UDP-alpha-D-galactofuranose adduct as an intermediate in the catalytic cycle, the chemical mechanism for UGM involves an SN2-type displacement of UDP from UDP-alpha-D-galactopyranose/UDP-alpha-D-galactofuranose by N5 of FADred
-
UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose
catalytic reaction mechanism, detailed overview. A covalent adduct is formed between the substrate and the FADH cofactor, temporarily breaking the glycosidic bond, followed by an internal proton transfer between N5FADH and O6FADH. The next step involves linearization of the sugar and formation of the iminium ion species. In the next step, the sugar cyclizes into its five-membered ring form. This step is isotope sensitive and is considered to be the chemical rate-limiting step of the mechanism. Once the furanose form of the sugar is reached, another internal proton transfer takes place, and the glycosidic bond to UDP is formed. Finally, the product of the reaction exits the active site of the enzyme
UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose
detailed reaction mechanism involving SN2-type steps, overview
-
UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose
enzyme-substrate binding structure and mechanism
UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose
quantum mechanics-molecular mechanics (QM/MM) molecular dynamics study and reaction mechanism, characterization of the structures of reactants, products, intermediate species and transitions states, overview
-
UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose
reaction mechanism including FAD cofactor, overview. Role of a covalent flavin N5 intermediate in the isomerization, non-redox reaction, of UDP-galactopyranose (UDP-Galp) to UDP-galactofuranose (UDP-Galf) by UDP-galactopyranose mutase (UGM). The flavin is required to be in the reduced state and functions as a nucleophile. The flavin must cycle back to the oxidized state for sustained catalysis. Formation of a N5-iminium ion intermediate, Fformation of N5-adducts in non-redox reactions involving the flavin in the oxidized or reduced forms
UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose
chemical reaction mechanism, overview
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539
-
UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose
catalytic mechanism, overview
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
isomerization
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PATHWAY SOURCE
PATHWAYS
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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.
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CAS REGISTRY NUMBER
COMMENTARY
174632-18-9
-
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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
2-fluoro-deoxy-UDP-galactopyranose
2-fluoro-deoxy-UDP-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-3''-deoxy-3''-fluoro-D-galactopyranose
UDP-3''-deoxy-3''-fluoro-D-galactofuranose
-
-
r
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
-
-
-
?
UDP-alpha-D-galactofuranose
UDP-alpha-D-galactopyranose
-
-
r
UDP-alpha-D-galactofuranose
UDP-alpha-D-galactopyranose
-
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
-
-
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
Aspergillus nidulans FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
-
-
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
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539
-
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
-
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
-
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
-
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
-
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
-
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-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
-
-
-
r
UDP-galactopyranose
UDP-galactofuranose
-
essential step of mycobacterial cell wall biosynthesis
-
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
-
?
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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
UDP-N-acetyl-2-deoxy-2-amino-alpha-D-galactopyranose
UDP-N-acetyl-2-deoxy-2-amino-alpha-D-galactofuranose
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
Aspergillus nidulans FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
-
-
-
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
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539
-
-
-
-
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-galactopyranose
UDP-galactofuranose
-
essential step of mycobacterial cell wall biosynthesis
-
-
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
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FADH2
-
reduced FAD is required for activity. Reconstitution of apoenzyme with other FAD analogues, e.g. with methoxy-FAD, trifluoromethyl-FAD, or chloro-FAD, which are less effective than FAD, overview
FAD
-
exists in a reduced state when the enzyme is catalytically active
FAD
-
UGM is only catalytically active when the flavin is in the reduced form
FAD
a flavoenzyme, FAD is tightly bound, binding kinetics and mechanism
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
-
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
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
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
-
involved in the catalyzed reaction, formation of a flavin-substrate/flavin-product adduct
FAD
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
FAD
the flavin functions as a catalytic center in a non-redox reaction, catalytic function, overview. The flavin is required to be in the reduced state and functions as a nucleophile. The flavin must cycle back to the oxidized state for sustained catalysis
flavin
-
flavoenzyme, conformational changes induced by flavin reduction, overview
flavin
-
flavoenzyme, reduction of AfUGM also changes the conformation of the flavin itself, enzyme conformational changes induced by flavin reduction, overview
flavin
the flavin needs to be reduced for the enzyme to be active
additional information
-
UGMs are active only in the reduced form
-
additional information
UGMs are active only in the reduced form. Kinetic parameters for the reduction of AfUGM mutant enzymes by NADPH compared to wild-type enzyme, overview
-
additional information
-
UGMs are active only in the reduced form. Kinetic parameters for the reduction of AfUGM mutant enzymes by NADPH compared to wild-type enzyme, overview
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
citrate
the citrate ion is identified on the basis of its shape and bonding partners and is located in the active site cavity adjacent to the FAD cofactor. Citrate is anionic like the UDP-alpha-D-galactopyranose substrate. 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
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(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-[(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
(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-(([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-(thiophen-2-yl)-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-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-(4-bromobenzyl)-6-(4-chlorophenyl)-7H-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazine-7-carboxylic 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
-
-
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
(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
-
-
UDP
enzyme binding structure analysis and binding mode, overview
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5-Deazariboflavin
-
specific activity 29fold higher than of control without illumination
NAD(P)H
-
kinetic parameters for the reduction of eukaryotic UGMs by NAD(P)H, NAD(P)H site structure and conformational changes associated with enzyme activation, overview
NAD(P)H
-
kinetic parameters for the reduction of eukaryotic UGMs by NAD(P)H, NAD(P)H site structure and conformational changes associated with enzyme activation, overview
NAD(P)H
-
kinetic parameters for the reduction of eukaryotic UGMs by NAD(P)H, NAD(P)H site structure and conformational changes associated with enzyme activation, overview
NAD(P)H
-
kinetic parameters for the reduction of eukaryotic UGMs by NAD(P)H, NAD(P)H site structure and conformational changes associated with enzyme activation, overview
NAD(P)H
-
kinetic parameters for the reduction of eukaryotic UGMs by NAD(P)H, NAD(P)H site structure and conformational changes associated with enzyme activation, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.203
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
0.032
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
0.0425
UDP-alpha-D-galactopyranose
pH 7.0, 37°C, wild-type enzyme
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
0.805
UDP-D-galactopyranose
-
in 50 mM MOPS, 10 mM sodium dithionite, 2 mM MgCl2 pH 7.4, at 37°C
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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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
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
0.14
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
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
35.3
UDP-D-galactopyranose
-
in 50 mM MOPS, 10 mM sodium dithionite, 2 mM MgCl2 pH 7.4, at 37°C
66
UDP-galactopyranose
-
wild type enzyme, in 50 mM sodium phosphate buffer pH 7.0
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1180
UDP-galactopyranose
-
wild type enzyme, in 50 mM sodium phosphate buffer pH 7.0
0.06
UDP-alpha-D-galactofuranose
pH and temperature not specified in the publication, recombinant mutant N201A
0.29
UDP-alpha-D-galactofuranose
pH and temperature not specified in the publication, recombinant mutant Q103A
0.7
UDP-alpha-D-galactofuranose
pH and temperature not specified in the publication, recombinant mutant Y317A
0.8
UDP-alpha-D-galactofuranose
pH and temperature not specified in the publication, recombinant mutant N207A
0.9
UDP-alpha-D-galactofuranose
pH and temperature not specified in the publication, recombinant mutant Y317A
0.94
UDP-alpha-D-galactofuranose
pH and temperature not specified in the publication, recombinant mutant Y100A
1.4
UDP-alpha-D-galactofuranose
pH 7.0, 37°C, recombinant mutant W315A
2
UDP-alpha-D-galactofuranose
pH and temperature not specified in the publication, recombinant mutant Q107A
3
UDP-alpha-D-galactofuranose
pH and temperature not specified in the publication, recombinant mutant Y104A
3.5
UDP-alpha-D-galactofuranose
pH and temperature not specified in the publication, recombinant mutant F66A
95.7
UDP-alpha-D-galactofuranose
pH and temperature not specified in the publication, recombinant wild-type enzyme
222.22
UDP-alpha-D-galactofuranose
pH 7.0, 37°C, recombinant wild-type enzyme
654.5
UDP-alpha-D-galactofuranose
pH and temperature not specified in the publication, recombinant wild-type enzyme
1048.6
UDP-alpha-D-galactofuranose
-
pH and temperature not specified in the publication, recombinant wild-type enzyme
0.205
UDP-alpha-D-galactopyranose
pH 7.0, 37°C, wild-type enzyme
0.33
UDP-beta-L-arabinofuranose
pH 7.0, 37°C, recombinant mutant W315A
1.489
UDP-beta-L-arabinofuranose
pH 7.0, 37°C, recombinant wild-type enzyme
57
UDP-D-galactofuranose
-
in 25 mM HEPES, 125 mM NaCl, 20 mM dithionite, pH 7.5, at 37°C
650
UDP-D-galactofuranose
-
in 25 mM HEPES, 125 mM NaCl, 20 mM dithionite, pH 7.5, at 37°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0049
2-((4-(3,4-dichlorophenyl)thiazol-2-yl)amino)-3-(4-iodophenyl)propanoic acid
pH 7.0, temperature not specified in the publication
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
-
-
additional information
additional information
-
inhibition kinetic analysis
-
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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 - 0.062
(4-chlorophenyl)-[1-(4-chlorophenyl)-3-hydroxy-5-methyl-1H-pyrazol-4-yl]-methanone
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 - 0.037
3-(4-iodophenyl)-2-[4-(3,4-dichlorophenyl)-thiazol-2-ylamino]-propionic acid
0.0035
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
Mycobacterium tuberculosis
-
-
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
0.044
(4-chlorophenyl)-[1-(4-chlorophenyl)-3-hydroxy-5-methyl-1H-pyrazol-4-yl]-methanone
Klebsiella pneumoniae
-
pH and temperature not specified in the publication
0.062
(4-chlorophenyl)-[1-(4-chlorophenyl)-3-hydroxy-5-methyl-1H-pyrazol-4-yl]-methanone
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
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
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
0.037
3-(4-iodophenyl)-2-[4-(3,4-dichlorophenyl)-thiazol-2-ylamino]-propionic acid
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
0.411
UDP-CH2-Galp
Deinococcus radiodurans
in 50 mM sodium phosphate buffer (pH 7.0), at 22°C
0.479
UDP-CH2-Galp
Klebsiella pneumoniae
-
in 50 mM sodium phosphate buffer (pH 7.0), at 22°C
0.495
UDP-CH2-Galp
Mycobacterium tuberculosis
-
in 50 mM sodium phosphate buffer (pH 7.0), at 22°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Aspergillus nidulans FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
i.e. Emericella nidulans
UniProt
brenda
i.e. Neosartorya fumigata
SwissProt
brenda
-
-
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
physiological function
additional information
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
-
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
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539
-
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
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
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
Aspergillus nidulans FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
-
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
-
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
-
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
-
glf-1 is required for normal post-embryonic development
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
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
-
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
-
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
-
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
-
molecular dynamics studies of active site flexibility, overview
additional information
-
molecular dynamics studies of active site flexibility, overview
additional information
-
molecular dynamics studies of active site flexibility, overview
additional information
-
molecular dynamics studies of active site flexibility, overview
additional information
-
molecular dynamics studies of active site flexibility, overview
additional information
-
molecular dynamics studies of active site flexibility, overview
additional information
-
molecular dynamics studies of active site flexibility, overview
additional information
-
substrate recognition mechanism, overview. Molecular dynamics studies of active site flexibility, overview
additional information
-
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
-
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
-
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
molecular dynamics simulations. Binding modes of substrates in the active site of enzyme AfUGM
additional information
-
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
-
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
-
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
-
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
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539
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substrate recognition mechanism, overview. Molecular dynamics studies of active site flexibility, overview
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
Show AA Sequence and Transmembrane Helices (5057 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis)
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
Trypanosoma cruzi (strain CL Brener)
Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis)
Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis)
Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis)
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decamer
dimer
homodimer
homotetramer
monomer
tetramer
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dimer-of-dimers tetramer in solution, the C-terminal helix of domain 1 and residue Arg133 in AfUGM form intersubunit hydrogen bonds in the AfUGM tetramer, while long side chains protruding from a helix of domain 2 likely prevent formation of the intersubunit 4-helix bundle that stabilizes the AfUGM tetramer
additional information
dimer
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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
dimer
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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
dimer
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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
monomer
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the unique fold-level variations exhibited by TcUGM are responsible for the monomeric state
additional information
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the tertiary structure dictates the oligomeric state, oligomeric state and quaternary structure, overview
additional information
structure of dimeric recombinant GSG-CdUGM
additional information
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structure of dimeric recombinant GSG-CdUGM
additional information
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oligomeric state and quaternary structure, overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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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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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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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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
crystal structure analysis, molecular dynamics simulations and modeling, overview
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F66A
H63N
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
R182A
R182K
R327A
R327K
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
R280A
mutation of conserved residue of putative active site cleft. No catalytic activity
W160A
W70F/W290F
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
-
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
Y317F
Y395F
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y429F
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
additional information
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 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, 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
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
Aspergillus nidulans FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
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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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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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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE