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Enzyme Nomenclature
Information on EC 5.4.99.9 - UDP-galactopyranose mutase
for references in articles please use BRENDA:EC5.4.99.9
Word Map on EC 5.4.99.9
- 5.4.99.9
- phosphoglycerate
- methylmalonyl-coa
-
methylmalonic
- udp-galactofuranose
-
galactofuranose
- chorismate
-
udp-galf
-
urogenital
-
sinus
-
galf
-
methylmalonyl-coenzyme
- prephenate
- adenosylcobalamin
- acidemia
- succinyl-coa
- acidurias
-
flavoenzyme
-
bisphosphoglycerate
-
b12-dependent
- 2,3-bisphosphoglycerate
-
adenosylcobalamin-dependent
-
adocbl
- propionyl-coa
-
cobalamin-dependent
-
cofactor-dependent
- shermanii
-
cytodifferentiation
- drug development
-
phosphoenzyme
- methylcobalamin
- isobutyryl-coa
-
furanose
-
cobiialamin
- analysis
- synthesis
- medicine
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
5.4.99.9
-
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RECOMMENDED NAME
GeneOntology No.
UDP-galactopyranose mutase
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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
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
catalytic 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 mechanism, overview
-
-
UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose
chemical reaction mechanism, overview
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
group transfer
-
-
intramolecular
-
isomerization
isomerization
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
3633, 650202, 653321, 661926, 662649, 662936, 679168, 692768, 694527, 695049, 706033, 706049, 706635, 715191, 715919, 726820
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-
-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
physiological function
additional information
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
-
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
-
conserved active site residues in Aspegillus fumigatus UGM compared to prokaryotic UGMs, 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
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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
-
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
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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 synthesis of the cell wall
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
-
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
-
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
-
glf-1 is required for normal post-embryonic development
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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
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additional information
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substrate recognition mechanism, overview. Molecular dynamics studies of active site flexibility, overview
additional information
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substrate recognition mechanism, overview. Molecular dynamics studies of active site flexibility, overview
additional information
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molecular dynamics studies of active site flexibility, overview
additional information
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molecular dynamics studies of active site flexibility, overview
additional information
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molecular dynamics studies of active site flexibility, overview
additional information
-
molecular dynamics studies of active site flexibility, overview
additional information
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molecular dynamics studies of active site flexibility, overview
additional information
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molecular dynamics studies of active site flexibility, overview
additional information
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molecular dynamics studies of active site flexibility, overview
additional information
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enzyme-substrate binding analysis by combination of UV/visible spectroscopy, X-ray crystallography, saturation transfer difference NMR spectroscopy, molecular dynamics, and CORCEMA-ST calculations. Two arginines in the enzyme, Arg59 and Arg168, play critical roles in the catalytic mechanism of the enzyme and in controlling its specificity to ultimately lead to an N-acetyl-alpha-D-galactofuranose-containing capsular polysaccharides. Substrate-recognition patterns compared to the Eschericia coli enzyme, overview
additional information
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Arg182 and Arg327 play important roles in stabilizing the position of the diphosphates of the nucleotide sugar and help to facilitate the positioning of the galactose moiety for catalysis. Substrate recognition and structural changes observed upon substrate binding involving the mobile loops and the critical arginine residues Arg182 and Arg327, overview. The Aspergillus fumigatus enzyme contains a third flexible loop (loop III) above the si-face of the isoalloxazine ring that changes position depending on the redox state of the flavin cofactor
additional information
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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
-
enzyme-substrate binding analysis by combination of UV/visible spectroscopy, X-ray crystallography, saturation transfer difference NMR spectroscopy, molecular dynamics, and CORCEMA-ST calculations. Two arginines in the enzyme, Arg59 and Arg168, play critical roles in the catalytic mechanism of the enzyme and in controlling its specificity to ultimately lead to an N-acetyl-alpha-D-galactofuranose-containing capsular polysaccharides. Substrate-recognition patterns compared to the Eschericia coli enzyme, overview
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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
-
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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-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-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
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-
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
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-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539
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-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539
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the equilibrium of the UGM-catalyzed reaction favors UDP-Galp by the ratio of 11:1
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-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
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the equilibrium of the UGM-catalyzed reaction favors UDP-Galp by the ratio of 11:1
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-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
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-
-
-
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
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-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
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the equilibrium of the UGM-catalyzed reaction favors UDP-Galp by the ratio of 11:1
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-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
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the equilibrium of the UGM-catalyzed reaction favors UDP-Galp by the ratio of 11:1
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-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
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the equilibrium of the UGM-catalyzed reaction favors UDP-Galp by the ratio of 11:1
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r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
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-
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r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
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the equilibrium of the UGM-catalyzed reaction favors UDP-Galp by the ratio of 11:1
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-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
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the equilibrium of the UGM-catalyzed reaction favors UDP-Galp by the ratio of 11:1
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-
r
UDP-galactofuranose
UDP-galactopyranose
-
-
8-5% product yield, 92-95% product yield
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r
UDP-galactofuranose
UDP-galactopyranose
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8-5% product yield, 92-95% product yield
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r
UDP-galactopyranose
UDP-galactofuranose
-
-
-
-
r
UDP-galactopyranose
UDP-galactofuranose
-
essential step of mycobacterial cell wall biosynthesis
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-
r
UDP-N-acetyl-2-deoxy-2-amino-alpha-D-galactopyranose
UDP-N-acetyl-2-deoxy-2-amino-alpha-D-galactofuranose
-
-
-
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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
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-
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additional information
?
-
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development of a fluorescence polarization binding assay for the Aspergillus fumigatus enzyme, evaluation, overview
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-
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additional information
?
-
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UDP-galactopyranose mutase as an important protein in fungal cell wall biosynthesis
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-
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additional information
?
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UDP-galactopyranose mutase as an important protein in fungal cell wall biosynthesis
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-
-
additional information
?
-
-
UGM does not interconvert UDP-GalpNAc and UDP-GalfNAc
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-
-
additional information
?
-
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the bifunctional pyranose-furanose mutase recognizes both UDP-Gal and UDP-GalNAc
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-
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additional information
?
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the bifunctional pyranose-furanose mutase recognizes both UDP-Gal and UDP-GalNAc
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-
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additional information
?
-
-
UGM does not interconvert UDP-GalpNAc and UDP-GalfNAc
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-
-
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
?
-
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UDP-D-glucose is not a substrate for UGM
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-
-
additional information
?
-
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the enzyme is active only in the reduced state
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-
-
additional information
?
-
-
1,4-anhydrogalactopyranose does not react with UGM and UDP to form UDP-galactopyranose or UDP-galactofuranose
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-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539
-
-
-
-
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
flavin
-
flavoenzyme, reduction of AfUGM also changes the conformation of the flavin itself, enzyme conformational changes induced by flavin reduction, overview
flavin
-
flavoenzyme, conformational changes induced by flavin reduction, overview
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INHIBITORS
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,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
(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
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-[(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
-
-
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
additional information
-
fluorinated substrate analogues under non-reducing conditions
-
(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
-
-
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
-
-
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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
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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
0.022
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
-
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
-
steady-state kinetics of wild-type and mutant enzymes, overview
-
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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
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
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
0.0016
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
-
-
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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
Q9RYF1
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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PDB
SCOP
CATH
ORGANISM
UNIPROT
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
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 smegmatis (strain ATCC 700084 / mc(2)155)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
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)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decamer
dimer
homodimer
homotetramer
-
4 * 55000, SDS-PAGE; 4 * 57152, calculated from amino acid sequence
monomer
tetramer
-
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
-
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
-
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
-
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
-
1 * 54960, calculated from amino acid sequence; 1 * 55000, SDS-PAGE
monomer
-
the unique fold-level variations exhibited by TcUGM are responsible for the monomeric state
additional information
-
the tertiary structure dictates the oligomeric state, oligomeric state and quaternary structure, overview
additional information
-
oligomeric state and quaternary structure, overview
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis, two crystal forms, hexagonal and triclinic
-
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
-
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
-
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
-
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
-
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°
-
in the (active) reduced state, with FAD, crystal structure at 2.2 A resolution, with FADH-, crystal structure at 2.25 A resolution
-
in the oxidized state, with FAD, crystal structure at 2.25 A resolution
-
crystal structure analysis, molecular dynamics simulations and modeling, overview
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
HQ20 column chromatography and HP-20 hydrophobic interaction chromatography column
-
nickel immobilized affinity chromatography and DEAE column chromatography
-
nickel immobilized metal affinity chromatography, DEAE column chromatography, and purification with HaloLink resin
-
Protino Ni-IDA 1000 column chromatography
recombinant C-terminally His6-tagged enzyme from Escherichia coi strain BL21 StarTM (DE3) by nickel affinity chromatography
-
recombinant GST-tagged enzyme from Escherichia coli strain BL21 (DE3) pLysS or B893 (DE3) pLysS by glutathione affinity chroatography and gel filtration
-
the recombinant enzyme from Escherichia coli
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli C43 cells
expression in Escherichia coli
expression in Escherichia coli with a His-tag
gene glf, overexpression of C-terminally His6-tagged enzyme in Escherichia coi strain BL21 StarTM (DE3)
-
overexpression in Escherichia coli
recombinant expression of GST-tagged enzyme in Escherichia coli strain BL21 (DE3) pLysS, and in strain B893 (DE3) pLysS for the selnomethionine-labeled enzyme
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R182K
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R327K
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
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
R176A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R327A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y317F
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Y395F
-
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
W160A
-
mutation of conserved residue on edge putative active site cleft, defective in binding of substrate
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%)
additional information
-
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
-
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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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
high-throughput fluorescence polarization assay for indentification of inhibitors of enzyme and homologues
drug development
medicine
-
the UDP-galactopyranose mutase is an appealing adjunct therapeutic target in combination with other drugs against Aspergillus fumigatus
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
drug development
-
the product galactofuranose is valued as an important target for the development of new antituberculosis drugs
drug development
-
the product galactofuranose is valued as an important target for the development of new antituberculosis drugs
drug development
-
UGM inhibition may provide an attractive drug target in those eukaryotes where galactofuranose plays a critical role in cellular viability and virulence
drug development
UGM inhibition may provide an attractive drug target in those eukaryotes where galactofuranose plays a critical role in cellular viability and virulence
drug development
-
UGM inhibition may provide an attractive drug target in those eukaryotes where galactofuranose plays a critical role in cellular viability and virulence
drug development
UGM inhibition may provide an attractive drug target in those eukaryotes where galactofuranose plays a critical role in cellular viability and virulence
drug development
-
blocking the incorporation of the product galactofuranose into polysaccharides essential for pathogen viability or virulence may lead to novel therapeutics
drug development
-
the enzyme is a potential drug target involved in the synthesis of the cell wall of this fungal pathogen
drug development
-
inhibitors of the enzyme that block the biosynthesis of UDP-galactofuranose can lead to novel chemotherapeutics for treating Aspergillus fumigatus-related diseases
drug development
-
since the enzyme does not exist in Homo sapiens, the parasite enzyme is a target for drug design
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LINKS TO OTHER DATABASES (specific for EC-Number 5.4.99.9)
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