Information on EC 5.4.99.9 - UDP-galactopyranose mutase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
5.4.99.9
-
RECOMMENDED NAME
GeneOntology No.
UDP-galactopyranose mutase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose
show the reaction diagram
-
-
-
-
UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose
show the reaction diagram
catalytic mechanism, overview
-
UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose
show the reaction diagram
mobile loop of enzyme must move in order for enzyme to bind UDP-galactose substrate
-
UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose
show the reaction diagram
chemical reaction mechanism, overview
-
UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose
show the reaction diagram
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
show the reaction diagram
chemical reaction mechanism, overview
-
-
UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose
show the reaction diagram
catalytic mechanism, overview
Campylobacter jejuni 11168
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
group transfer
-
-
intramolecular
-
isomerization
-
-
-
-
isomerization
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Galactose metabolism
-
-
mycolyl-arabinogalactan-peptidoglycan complex biosynthesis
-
-
O-antigen building blocks biosynthesis (E. coli)
-
-
superpathway of UDP-glucose-derived O-antigen building blocks biosynthesis
-
-
UDP-galactofuranose biosynthesis
-
-
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.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
galactopyranose mutase
Q9RYF1
-
GLF gene product
-
-
GLF gene product
Q5KEL8
-
GLF gene product
Q5EEK0
-
GLF gene product
Q5EEK1
-
GLF-1
Caenorhabditis elegans N2
-
-
-
Mutase, uridine diphosphogalactopyranose
-
-
-
-
UDP-D-galactopyranose mutase
-
-
UDP-Gal mutase
-
-
UDP-galactopyranose mutase
-
-
-
-
UDP-galactopyranose mutase
Q4W1X2
-
UDP-galactopyranose mutase
-
-
UDP-galactopyranose mutase
Q5KEL8
-
UDP-galactopyranose mutase
-
-
UDP-galactopyranose mutase
-
-
UDP-galactopyranose mutase
Q5EEK0
-
UDP-galactopyranose mutase
-
-
UDP-galactopyranose mutase
Q5EEK1
-
UDP-Galp mutase
-
-
UGM
Q4W1X2
the key enzyme of galactofuranose metabolism controls the biosynthesis of galactomannan and galactofuranose containing glycoconjugates
UGM
Caenorhabditis elegans N2
-
-
-
UGM
Campylobacter jejuni 11168
-
-
-
UGM
Q5EEK1
-
UgmA
Aspergillus niger RD6.13
-
-
-
UNGM
-
Campylobacter jejuni UNGM has UGM activity in Escherichia coli
UNGM
Campylobacter jejuni 11168
-
; Campylobacter jejuni UNGM has UGM activity in Escherichia coli
-
uridine 5'-diphosphate galactopyranose mutase
-
-
uridine 5'-diphosphate galactopyranosemutase
Q48485
-
CAS REGISTRY NUMBER
COMMENTARY
174632-18-9
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain RD6.13
-
-
Manually annotated by BRENDA team
Aspergillus niger RD6.13
strain RD6.13
-
-
Manually annotated by BRENDA team
strain N2 variant Bristol
-
-
Manually annotated by BRENDA team
Caenorhabditis elegans N2
strain N2 variant Bristol
-
-
Manually annotated by BRENDA team
strain 11168
-
-
Manually annotated by BRENDA team
Campylobacter jejuni 11168
-
-
-
Manually annotated by BRENDA team
Campylobacter jejuni 11168
strain 11168
-
-
Manually annotated by BRENDA team
no activity in Homo sapiens
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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 pyrophosphate
evolution
-
the enzyme is a member of the UGM family
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
Campylobacter jejuni 11168
-
the enzyme is a member of the UGM family
-
malfunction
-
glf-1 mutants display significant late embryonic and larval lethality, and other phenotypes indicative of defective surface coat synthesis, the glycan-rich outermost layer of the nematode cuticle
malfunction
-
Aspergillus nidulans strains deleted for UgmA lack immunolocalizable UDP-D-galactofuranose, have growth and sporulation defects, abnormal wall architecture, and significantly larger hyphal surface subunits and lower cell wall viscoelastic moduli
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
Caenorhabditis elegans N2
-
glf-1 is required for normal post-embryonic development
-
physiological function
Campylobacter jejuni 11168
-
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
-
malfunction
Caenorhabditis elegans N2
-
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
-
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
-
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
Campylobacter jejuni 11168
-
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
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-(6-deoxy-6-fluoro)-D-galactofuranose
UDP-(6-deoxy-6-fluoro)-D-galactopyranose
show the reaction diagram
-
-
-
-
r
UDP-(6-deoxy-6-fluoro)-D-galactofuranose
?
show the reaction diagram
-
-
-
-
?
UDP-2-amino-2-deoxy-D-galactopyranose
?
show the reaction diagram
-
-
-
-
?
UDP-2-deoxy-2-fluoro-D-galactofuranose
?
show the reaction diagram
-
-
-
-
?
UDP-2-deoxy-2-fluoro-D-galactopyranose
?
show the reaction diagram
-
-
-
-
?
UDP-2-fluoro-galactofuranose
?
show the reaction diagram
-
-
-
-
?
UDP-3''-deoxy-3''-fluoro-D-galactopyranose
UDP-3''-deoxy-3''-fluoro-D-galactofuranose
show the reaction diagram
-
-
-
-
r
UDP-3-deoxy-3-fluoro-D-galactofuranose
?
show the reaction diagram
-
-
-
-
?
UDP-3-deoxy-3-fluoro-D-galactofuranose
?
show the reaction diagram
-
-
-
-
?
UDP-3-deoxy-3-fluoro-D-galactopyranose
?
show the reaction diagram
-
-
-
-
?
UDP-6-deoxy-6-fluoro-D-galactopyranose
?
show the reaction diagram
-
-
-
-
?
UDP-6-deoxy-D-galactopyranose
?
show the reaction diagram
-
-
-
-
?
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
show the reaction diagram
-
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
show the reaction diagram
-
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
show the reaction diagram
-
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
show the reaction diagram
-
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
show the reaction diagram
-
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
show the reaction diagram
-
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
show the reaction diagram
-
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
show the reaction diagram
-
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
show the reaction diagram
-
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
show the reaction diagram
Q9RYF1
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
Campylobacter jejuni 11168
-
-
-
-
r
UDP-beta-L-arabinofuranose
?
show the reaction diagram
-
-
-
-
?
UDP-D-galactofuranose
UDP-D-galactopyranose
show the reaction diagram
-
-
-
-
r
UDP-D-galactofuranose
UDP-D-galactopyranose
show the reaction diagram
-
-
-
-
r
UDP-D-galactofuranose
UDP-D-galactopyranose
show the reaction diagram
-
-
-
-
r
UDP-D-galactopyranose
UDP-D-galactofuranose
show the reaction diagram
-
-
-
r
UDP-D-galactopyranose
UDP-D-galactofuranose
show the reaction diagram
-
-
-
-
r
UDP-D-galactopyranose
UDP-D-galactofuranose
show the reaction diagram
-
-
-
?
UDP-D-galactopyranose
UDP-D-galactofuranose
show the reaction diagram
Q48485
-
-
-
?
UDP-D-galactopyranose
UDP-D-galactofuranose
show the reaction diagram
-
-
-
-
?
UDP-D-galactopyranose
UDP-D-galactofuranose
show the reaction diagram
-
-
-
-
r
UDP-D-galactopyranose
UDP-D-galactofuranose
show the reaction diagram
-
-
-
-
?
UDP-D-galactopyranose
UDP-D-galactofuranose
show the reaction diagram
-
-
-
-
r
UDP-D-galactopyranose
UDP-D-galactofuranose
show the reaction diagram
-
-
-
-
r
UDP-D-galactopyranose
UDP-D-galactofuranose
show the reaction diagram
-
-
-
-
r
UDP-D-galactopyranose
UDP-D-galactofuranose
show the reaction diagram
-
-
-
-
?
UDP-galactofuranose
UDP-galactopyranose
show the reaction diagram
-
-
8-5% product yield, 92-95% product yield
-
r
UDP-galactofuranose
UDP-galactopyranose
show the reaction diagram
Caenorhabditis elegans N2
-
-
8-5% product yield, 92-95% product yield
-
r
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
-
-
-
-
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
-
-
-
?
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
P37747
-
-
?
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
-
-
-
-
?
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
-
-
-
-
r
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
-
-
-
-
r
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
-
-
-
-
?
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
-
-
-
-
?
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
-
-
-
-
r
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
-
-
-
?
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
-
-
-
-
?
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
-
-
-
-
r
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
-
-
-
-
?
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
-
-
-
-
r
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
-
-
-
-
r
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
-
-
-
-
?
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
Q5KEL8
-
-
-
r
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
Q5EEK0
-
-
-
r
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
-
-
-
-
r
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
-
-
-
-
?
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
Q4W1X2
-
-
-
r
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
Q5EEK1
-
-
-
r
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
Q48485
-
-
-
r
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
-
-
-
-
r
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
-
essential step of mycobacterial cell wall biosynthesis
-
-
r
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
-
pH 7.1, 30C
-
-
r
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
Q5KEL8
pH 7.1, 30C
-
-
r
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
-
pH 7.1, 30C
-
-
r
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
Q5EEK1
pH 7.1, 30C
-
-
r
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
Aspergillus niger RD6.13
-
-
-
-
?
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
Campylobacter jejuni 11168
-
-
-
-
?
UDP-L-arabinofuranose
?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-2-deoxy-2-amino-alpha-D-galactopyranose
UDP-N-acetyl-2-deoxy-2-amino-alpha-D-galactofuranose
show the reaction diagram
Campylobacter jejuni, Campylobacter jejuni 11168
-
-
-
-
r
Uridine 5'-(trihydrogen diphosphate) P'-alpha-D-galactopyranosyl ester
Uridine 5'-(trihydrogen diphosphate) P'-alpha-D-galactofuranosyl ester
show the reaction diagram
-
-
-
-
2-fluoro-deoxy-UDP-galactopyranose
2-fluoro-deoxy-UDP-galactofuranose
show the reaction diagram
-
-
-
?
additional information
?
-
-
1,4-anhydrogalactopyranose does not react with UGM and UDP to form UDP-galactopyranose or UDP-galactofuranose
-
-
-
additional information
?
-
-
UDP-galactopyranose mutase as an important protein in fungal cell wall biosynthesis
-
-
-
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
?
-
-
UGM does not interconvert UDP-GalpNAc and UDP-GalfNAc
-
-
-
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
?
-
-
the enzyme is active only in the reduced state
-
-
-
additional information
?
-
-
development of a fluorescence polarization binding assay for the Aspergillus fumigatus enzyme, evaluation, overview
-
-
-
additional information
?
-
-
the bifunctional pyranose-furanose mutase recognizes both UDP-Gal and UDP-GalNAc
-
-
-
additional information
?
-
Aspergillus niger RD6.13
-
UDP-galactopyranose mutase as an important protein in fungal cell wall biosynthesis
-
-
-
additional information
?
-
Campylobacter jejuni 11168
-
the bifunctional pyranose-furanose mutase recognizes both UDP-Gal and UDP-GalNAc
-
-
-
additional information
?
-
Campylobacter jejuni 11168
-
UGM does not interconvert UDP-GalpNAc and UDP-GalfNAc
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
show the reaction diagram
-
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
show the reaction diagram
-
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
show the reaction diagram
-
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
show the reaction diagram
-
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
show the reaction diagram
-
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
show the reaction diagram
-
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
show the reaction diagram
-
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
show the reaction diagram
-
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
show the reaction diagram
-
-
-
-
r
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
show the reaction diagram
Campylobacter jejuni 11168
-
-
-
-
r
UDP-D-galactopyranose
UDP-D-galactofuranose
show the reaction diagram
-
-
-
-
r
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
P37747
-
-
?
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
-
-
-
-
r
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
-
-
-
?
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
-
-
-
-
r
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
-
-
-
-
r
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
Q5KEL8
-
-
-
r
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
Q5EEK0
-
-
-
r
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
-
-
-
-
r
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
Q4W1X2
-
-
-
r
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
Q5EEK1
-
-
-
r
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
-
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
show the reaction diagram
Campylobacter jejuni, Campylobacter jejuni 11168
-
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
0.52 mol bound FAD per monomer
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
Q48485
FAD-containing enzyme
FAD
-
flavoenzyme
FAD
-
contains FAD
FAD
-
flavoenzyme, activity depends on FAD redox state
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
flavin
-
flavoenzyme, reduction of AfUGM also changes the conformation of the flavin itself, enzyme conformational changes induced by flavin reduction, overview
flavin
-
flavoenzyme
flavin
-
flavoenzyme, required for enzyme activation mechanism, overview
flavin
-
flavoenzyme, conformational changes induced by flavin reduction, overview
flavin
-
flavoenzyme
flavin
-
the flavin needs to be reduced for the enzyme to be active
NAD(P)+
-
-
NAD(P)H
P37747
or other reductants
NAD(P)H
-
or other reductants
NADH
-
or NADPH required
NADPH
-
or NADH required
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-propylpyrrolidine-3,4-diol
-
-
(2S,3S,4S,5R)-2-[(1S)-1,2-dihydroxyethyl]-5-[(1E)-prop-1-en-1-yl]pyrrolidine-3,4-diol
-
-
(2Z)-2-(2-chloro-4-hydroxy-5-nitrobenzylidene)[1,3]thiazolo[3,2-a]benzimidazol-3(2H)-one
-
comparison with inhibition of Mycobacterium tuberculosis enzyme; dissociation constant 0.0053 mM, comparison with inhibition of Klebsiella pneumoniae enzyme
(4-chlorophenyl)-[1-(4-chlorophenyl)-3-hydroxy-5-methyl-1H-pyrazol-4-yl]-methanone
-
-
(4E)-4-(4-chloro-3-nitrobenzylidene)-1-(3,4-dichlorophenyl)pyrazolidine-3,5-dione
-
comparison with inhibition of Mycobacterium tuberculosis enzyme; dissociation constant 0.0049 mM, comparison with inhibition of Klebsiella pneumoniae enzyme
(Z)-N-((E)-5-(5-nitro-2-oxoindolin-3-ylidene)-4-oxothiazolidin-2-ylidene) benzenesulfonamide
-
-
-
1(R)-1,4-dideoxy-1-C-3-[(ethyl)(uridin-5'-yl)phosphono]-2-propen-1-yl-1,4-imino-D-galactitol
-
25 mM, 52% residual activity
1(R)-1,4-dideoxy-1-C-3-[(uridin-5'-yl)phosphono]-2-propen-1-yl-1,4-imino-D-galactitol
-
2.5 mM, 43% residual activity
1(R)-1-C-allyl-1,4-dideoxy-1,4-imino-D-galactitol
-
25 mM, 61% residual activity
1,4-anhydro-beta-D-galactopyranose (1,5-anhydro-alpha-D-galactofuranose)
-
15% inhibition at 4 mM
1,4-bis-[1(R)-1,4-dideoxy-1,4-imino-D-galactit-1-yl]-2-butene
-
2.5 mM, 50% residual activity
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
-
-
3-(4-iodophenyl)-2-[4-(3,4-dichlorophenyl)-thiazol-2-ylamino]-propionic 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
-
-
Sodium borohydride
-
-
Sodium cyanoborohydride
-
-
UDP
-
competitive
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-C-alpha-D-galactofuranose
-
91% inhibition at 1 mM
UDP-C-alpha-D-galactopyranose
-
36% inhibition at 1 mM
UDP-C-beta-D-galactopyranose
-
8% inhibition at 1 mM
UDP-CH2-Galp
Q9RYF1
moderate inhibition of UGM
UDP-CH2-Galp
-
moderate inhibition of UGM
UDP-D-glucose
-
poor inhibitor of UGM
UDP-[1(1')Z]-exo-glycal-D-galactopyranose
-
42% inhibition at 1 mM
uridine diphosphate
-
-
uridine-5'-diphospho-(N-fluoresceinisothiocyano)hexanolamine
-
-
additional information
-
fluorinated substrate analogues under non-reducing conditions
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD(P)H
-
enzyme activation mechanism, overview
NADP(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
Sodium dithionite
-
20 mM
5-Deazariboflavin
-
specific activity 29fold higher than of control without illumination
additional information
-
enzyme activation mechanism, overview
-
additional information
-
enzme activation mechanism, overview
-
additional information
-
enzyme activation mechanism, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
24
UDP-(6-deoxy-6-fluoro)-D-galactofuranose
-
-
24
UDP-(6-deoxy-6-fluoro)-D-galactofuranose
-
-
1.14
UDP-2-amino-2-deoxy-D-galactopyranose
-
in 50 mM MOPS, 10 mM sodium dithionite, 2 mM MgCl2 pH 7.4, at 37C
0.065
UDP-2-deoxy-2-fluoro-D-galactofuranose
-
-
0.203
UDP-2-deoxy-2-fluoro-D-galactopyranose
-
in 50 mM MOPS, 10 mM sodium dithionite, 2 mM MgCl2 pH 7.4, at 37C
0.065
UDP-2-fluoro-galactofuranose
-
-
0.861
UDP-3-deoxy-3-fluoro-D-galactofuranose
-
-
0.861
UDP-3-deoxy-3-fluoro-D-galactofuranose
-
-
0.28
UDP-3-deoxy-3-fluoro-D-galactopyranose
-
in 50 mM MOPS, 10 mM sodium dithionite, 2 mM MgCl2 pH 7.4, at 37C
0.2
UDP-6-deoxy-6-fluoro-D-galactopyranose
-
in 50 mM MOPS, 10 mM sodium dithionite, 2 mM MgCl2 pH 7.4, at 37C
3.15
UDP-6-deoxy-D-galactopyranose
-
in 50 mM MOPS, 10 mM sodium dithionite, 2 mM MgCl2 pH 7.4, at 37C
0.022
UDP-alpha-D-galactopyranose
-
pH 7.0, 37C, mutant R182K
0.0334
UDP-alpha-D-galactopyranose
-
mutant Y317F, pH 7.5, 37C
0.0425
UDP-alpha-D-galactopyranose
-
pH 7.0, 37C, wild-type enzyme
0.0429
UDP-alpha-D-galactopyranose
-
pH 7.0, 37C, mutant R327K
0.09
UDP-alpha-D-galactopyranose
-
mutant R327A, pH 7.5, 37C
0.091
UDP-alpha-D-galactopyranose
-
mutant Y395F, pH 7.5, 37C
0.1
UDP-alpha-D-galactopyranose
-
mutant Y429F, pH 7.5, 37C
0.134
UDP-alpha-D-galactopyranose
-
mutant R176A, pH 7.5, 37C
0.14
UDP-alpha-D-galactopyranose
-
wild-type enzyme, pH 7.5, 37C
0.607
UDP-alpha-D-galactopyranose
-
pH 7.0, 37C, mutant R182A
0.016
UDP-D-galactofuranose
-
in 50 mM MOPS, 10 mM sodium dithionite, 2 mM MgCl2 pH 7.4, at 37C
0.022
UDP-D-galactofuranose
-
37C, 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 37C
0.11
UDP-D-galactofuranose
-
in 25 mM HEPES, 125 mM NaCl, 20 mM dithionite, pH 7.5, at 37C
0.194
UDP-D-galactofuranose
-
37C, pH 7.5
0.043
UDP-D-galactopyranose
-
wild-type, pH 8.0
0.205
UDP-D-galactopyranose
-
mutant E301A, pH 8.0
0.386
UDP-D-galactopyranose
-
mutant Y185F, pH 8.0
0.619
UDP-D-galactopyranose
-
mutant Y155F, pH 8.0
0.739
UDP-D-galactopyranose
-
mutant Y349F, pH 8.0
0.805
UDP-D-galactopyranose
-
in 50 mM MOPS, 10 mM sodium dithionite, 2 mM MgCl2 pH 7.4, at 37C
0.819
UDP-D-galactopyranose
-
mutant Y314F, pH 8.0
1.002
UDP-D-galactopyranose
-
mutant D351A, pH 8.0
0.02
UDP-galactofuranose
-
under reducing conditions
0.022
UDP-galactofuranose
-
-
0.19
UDP-galactofuranose
-
under non-reducing (native) conditions
0.022
UDP-galactopyranose
-
-
0.055
UDP-galactopyranose
-
wild type enzyme, in 50 mM sodium phosphate buffer pH 7.0
0.6
UDP-L-arabinofuranose
-
-
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
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7.4
UDP-(6-deoxy-6-fluoro)-D-galactofuranose
-
-
7.4
UDP-(6-deoxy-6-fluoro)-D-galactofuranose
-
-
1.4
UDP-2-amino-2-deoxy-D-galactopyranose
-
in 50 mM MOPS, 10 mM sodium dithionite, 2 mM MgCl2 pH 7.4, at 37C
0.033
UDP-2-deoxy-2-fluoro-D-galactofuranose
-
-
0.0007
UDP-2-deoxy-2-fluoro-D-galactopyranose
-
in 50 mM MOPS, 10 mM sodium dithionite, 2 mM MgCl2 pH 7.4, at 37C
0.033
UDP-2-fluoro-galactofuranose
-
-
5.7
UDP-3-deoxy-3-fluoro-D-galactofuranose
-
-
5.7
UDP-3-deoxy-3-fluoro-D-galactofuranose
-
-
0.9
UDP-3-deoxy-3-fluoro-D-galactopyranose
-
in 50 mM MOPS, 10 mM sodium dithionite, 2 mM MgCl2 pH 7.4, at 37C
3.5
UDP-6-deoxy-6-fluoro-D-galactopyranose
-
in 50 mM MOPS, 10 mM sodium dithionite, 2 mM MgCl2 pH 7.4, at 37C
42.2
UDP-6-deoxy-D-galactopyranose
-
in 50 mM MOPS, 10 mM sodium dithionite, 2 mM MgCl2 pH 7.4, at 37C
0.0224
UDP-alpha-D-galactopyranose
-
mutant R176A, pH 7.5, 37C
0.079
UDP-alpha-D-galactopyranose
-
pH 7.0, 37C, mutant R182A
0.12
UDP-alpha-D-galactopyranose
-
pH 7.0, 37C, mutant R327K
0.248
UDP-alpha-D-galactopyranose
-
mutant Y395F, pH 7.5, 37C
0.291
UDP-alpha-D-galactopyranose
-
mutant Y317F, pH 7.5, 37C
0.44
UDP-alpha-D-galactopyranose
-
pH 7.0, 37C, mutant R182K
4.26
UDP-alpha-D-galactopyranose
-
mutant R327A, pH 7.5, 37C
6.296
UDP-alpha-D-galactopyranose
-
mutant Y429F, pH 7.5, 37C
8.72
UDP-alpha-D-galactopyranose
-
pH 7.0, 37C, wild-type enzyme
13.4
UDP-alpha-D-galactopyranose
-
wild-type enzyme, pH 7.5, 37C
1.5
UDP-D-galactofuranose
-
37C, pH 7.5
5
UDP-D-galactofuranose
-
in 25 mM HEPES, 125 mM NaCl, 20 mM dithionite, pH 7.5, at 37C
27
UDP-D-galactofuranose
-
37C, 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 37C
72
UDP-D-galactofuranose
-
in 25 mM HEPES, 125 mM NaCl, 20 mM dithionite, pH 7.5, at 37C
0.13
UDP-D-galactopyranose
-
mutant D351A, pH 8.0
0.3
UDP-D-galactopyranose
-
mutant E301A, pH 8.0
1.3
UDP-D-galactopyranose
-
mutant Y185F, pH 8.0
1.7
UDP-D-galactopyranose
-
mutant Y349F, pH 8.0
3.6
UDP-D-galactopyranose
-
mutant Y155F, pH 8.0
5.2
UDP-D-galactopyranose
-
mutant Y314F, pH 8.0
5.5
UDP-D-galactopyranose
-
wild-type, pH 8.0
35.3
UDP-D-galactopyranose
-
in 50 mM MOPS, 10 mM sodium dithionite, 2 mM MgCl2 pH 7.4, at 37C
27
UDP-galactofuranose
-
-
27
UDP-galactopyranose
-
-
66
UDP-galactopyranose
-
wild type enzyme, in 50 mM sodium phosphate buffer pH 7.0
12
UDP-L-arabinofuranose
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.34
UDP-(6-deoxy-6-fluoro)-D-galactofuranose
-
-
14473
0.41
UDP-2-fluoro-galactofuranose
-
-
40133
0.00013
UDP-alpha-D-galactopyranose
-
pH 7.0, 37C, mutant R182A
85662
0.00017
UDP-alpha-D-galactopyranose
-
mutant R176A, pH 7.5, 37C
85662
0.00087
UDP-alpha-D-galactopyranose
-
mutant Y317F, pH 7.5, 37C
85662
0.0027
UDP-alpha-D-galactopyranose
-
mutant Y395F, pH 7.5, 37C
85662
0.003
UDP-alpha-D-galactopyranose
-
pH 7.0, 37C, mutant R327K
85662
0.02
UDP-alpha-D-galactopyranose
-
pH 7.0, 37C, mutant R182K
85662
0.047
UDP-alpha-D-galactopyranose
-
mutant R327A, pH 7.5, 37C
85662
0.063
UDP-alpha-D-galactopyranose
-
mutant Y429F, pH 7.5, 37C
85662
0.093
UDP-alpha-D-galactopyranose
-
wild-type enzyme, pH 7.5, 37C
85662
0.205
UDP-alpha-D-galactopyranose
-
pH 7.0, 37C, wild-type enzyme
85662
57
UDP-D-galactofuranose
-
in 25 mM HEPES, 125 mM NaCl, 20 mM dithionite, pH 7.5, at 37C
6212
650
UDP-D-galactofuranose
-
in 25 mM HEPES, 125 mM NaCl, 20 mM dithionite, pH 7.5, at 37C
6212
1230
UDP-galactofuranose
-
-
12721
1180
UDP-galactopyranose
-
wild type enzyme, in 50 mM sodium phosphate buffer pH 7.0
12722
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0016
2-[5-(3-bromo-benzylidene)-4-oxo-2-thioxo-thiazolidin-3-yl]-3-phenyl-propionic acid
-
-
0.0046
2-[[2-(4-bromo-phenyl)-1,3-dioxo-2,3-dihydro-1H-isoindole-5-carbonyl]-amino]-benzoic acid
-
-
0.017
N-[4-oxo-5-(2-oxo-1,2-dihydro-indol-3-ylidene)-thiazolidin-2-ylidene]-benzenesulfonamide
-
-
0.0013
uridine-5'-diphospho-(N-fluoresceinisothiocyano)hexanolamine
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.004
(2Z)-2-(2-chloro-4-hydroxy-5-nitrobenzylidene)[1,3]thiazolo[3,2-a]benzimidazol-3(2H)-one
-
pH 7.0, 37C
0.035
(2Z)-2-(2-chloro-4-hydroxy-5-nitrobenzylidene)[1,3]thiazolo[3,2-a]benzimidazol-3(2H)-one
-
pH 7.0, 37C
0.044
(4-chlorophenyl)-[1-(4-chlorophenyl)-3-hydroxy-5-methyl-1H-pyrazol-4-yl]-methanone
-
pH and temperature not specified in the publication
0.062
(4-chlorophenyl)-[1-(4-chlorophenyl)-3-hydroxy-5-methyl-1H-pyrazol-4-yl]-methanone
-
pH and temperature not specified in the publication
0.004
(4E)-4-(4-chloro-3-nitrobenzylidene)-1-(3,4-dichlorophenyl)pyrazolidine-3,5-dione
-
pH 7.0, 37C
0.041
(4E)-4-(4-chloro-3-nitrobenzylidene)-1-(3,4-dichlorophenyl)pyrazolidine-3,5-dione
-
pH 7.0, 37C
0.0046
2-(([2-(4-bromophenyl)-1,3-dioxo-2,3-dihydro-1H-isoindol-5-yl]carbonyl)amino)benzoic acid
-
pH 7.0, 37C
0.0016
2-[(5E)-5-(3-bromobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
-
pH 7.0, 37C
0.065
2-[(5E)-5-(3-bromobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
-
pH 7.0, 37C
0.0072
3-(4-iodophenyl)-2-[4-(3,4-dichlorophenyl)-thiazol-2-ylamino]-propionic acid
-
pH and temperature not specified in the publication
0.037
3-(4-iodophenyl)-2-[4-(3,4-dichlorophenyl)-thiazol-2-ylamino]-propionic acid
-
pH and temperature not specified in the publication
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
-
-
0.411
UDP-CH2-Galp
Q9RYF1
in 50 mM sodium phosphate buffer (pH 7.0), at 22C
0.479
UDP-CH2-Galp
-
in 50 mM sodium phosphate buffer (pH 7.0), at 22C
0.495
UDP-CH2-Galp
-
in 50 mM sodium phosphate buffer (pH 7.0), at 22C
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
assay at
PDB
SCOP
CATH
ORGANISM
Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
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)
Escherichia coli (strain K12)
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)
Neosartorya fumigata
Neosartorya fumigata
Neosartorya fumigata
Neosartorya fumigata
Neosartorya fumigata
Neosartorya fumigata
Neosartorya fumigata
Neosartorya fumigata
Neosartorya fumigata
Neosartorya fumigata
Neosartorya fumigata
Neosartorya fumigata
Neosartorya fumigata
Neosartorya fumigata
Neosartorya fumigata
Neosartorya fumigata
Neosartorya fumigata
Neosartorya fumigata
Neosartorya fumigata
Neosartorya fumigata
Neosartorya fumigata
Neosartorya fumigata
Neosartorya fumigata
Trypanosoma cruzi (strain CL Brener)
Trypanosoma cruzi (strain CL Brener)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
72000
-
gel filtration
651570
92000
-
gel filtration
3633
228600
-
calculated from amino acid sequence
713950
275000
-
gel filtration
713950
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 57200, about, sequence calculation
decamer
-
pentamer-of-dimers, in crystals
decamer
-
pentamer-of-dimers, in crystals
-
dimer
-
2 * 45000, SDS-PAGE
dimer
P37747
solution scattering experiments
dimer
-
in solution
dimer
-
alpha2, crystal structure
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
-
in solution
-
homodimer
-
alpha2, 2 * 43000, crystallization
homodimer
-
alpha2, 2 * 44000, calculated from translated peptide sequence
homotetramer
-
4 * 55000, SDS-PAGE, 4 * 57152, calculated from amino acid sequence
monomer
-
1 * 55000, SDS-PAGE, 1 * 54960, calculated from amino acid sequence
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
monomer
-
the unique fold-level variations exhibited by TcUGM are responsible for the monomeric state
additional information
-
oligomeric state and quaternary structure, overview
additional information
-
the tertiary structure dictates the oligomeric state, oligomeric state and quaternary structure, overview
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
-
crystal structure analysis
-
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
Q9RYF1
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
-
crystal structure analysis
-
FAD is located in a cleft lined with conserved residues
P37747
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
-
crystal structure analysis
-
in complex with UDP-D-glucose
-
in the (active) reduced state, with FAD, crystal structure at 2.2 A resolution, with FADH-, crystal structure at 2.25 A resolution
-
crystal structure analysis
-
in the oxidized state, with FAD, crystal structure at 2.25 A resolution
-
substrate-bound enzyme in oxidized and reduced forms
Q48485
crystal structure analysis
-
crystal structure analysis, molecular dynamics simulations and modeling, overview
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
nickel immobilized affinity chromatography and DEAE column chromatography
-
recombinant GST-tagged enzyme from Escherichia coli strain BL21 (DE3) pLysS or B893 (DE3) pLysS by glutathione affinity chroatography and gel filtration
-
HQ20 column chromatography and HP-20 column chromatography
-
HQ20 column chromatography and HP-20 hydrophobic interaction chromatography column
-
Protino Ni-IDA 1000 column chromatography
Q9RYF1
Protino Ni-IDA 1000 column chromatography
-
the recombinant enzyme
-
the recombinant enzyme from Escherichia coli
-
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
-
the recombinant enzyme from Escherichia coli
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
expressed in Escherichia coli BL21T1 cells
-
expression 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
-
expressed in Escherichia coli DH5alpha cell
-
expression in Escherichia coli
-
expressed in Escherichia coli strain strain MFF1
-
expression in Escherichia coli
Q5KEL8
expressed in Escherichia coli C43 cells
Q9RYF1
expressed in Escherichia coli Tuner cells
-
expression in Escherichia coli with a His-tag
-
overexpression in Escherichia coli
P37747
expressed in Escherichia coli
-
expressed in Escherichia coli C43 cells
-
expression in Escherichia coli (ER2566)
-
expression in Escherichia coli with a His-tag
-
expression in Escherichia coli, His-tagged protein
-
expression with His-tag in Escherichai coli
-
overexpression in Escherichia coli
-
expressed in Escherichia coli BL21T1 and BL21(DE3) cells
-
expression in Escherichia coli
Q5EEK0
expressed in Escherichia coli C43 cells
-
expression in Escherichia coli (BL21(DE3))
-
gene glf, overexpression of C-terminally His6-tagged enzyme in Escherichia coi strain BL21 StarTM (DE3)
-
expression in Escherichia coli
Q5EEK1
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R182A
-
site-directed mutagenesis, the mutant is almost inactive
R182K
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R327A
-
site-directed mutagenesis, inactive mutant
D351A
-
mutation of conserved residue of putative active site cleft. 4% of wild-type activity
E301A
-
mutation of conserved residue of putative active site cleft. 21% of wild-type activity
R174A
-
no catalytic activity
R280A
-
mutation of conserved residue of putative active site cleft. No catalytic activity
W156A
-
lower activity than wild-type enzyme
W156Y
-
lower activity than wild-type enzyme
W160A
-
catalytically inert
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%)
Y151F
-
lower activity than wild-type enzyme
Y155F
-
7% of wild-type activity
Y181F
-
lower activity than wild-type enzyme
Y185F
-
11% of wild-type activity
Y311F
-
lower activity than wild-type enzyme
Y314F
-
5% of wild-type activity
Y346F
-
lower activity than wild-type enzyme
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
R327K
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
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
Y349F
-
6% of wild-type activity
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
-
the product galactofuranose is valued as an important target for the development of new antituberculosis drugs
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
-
the enzyme is a potential drug target involved in the synthesis of the cell wall of this fungal pathogen
medicine
-
the UDP-galactopyranose mutase is an appealing adjunct therapeutic target in combination with other drugs against Aspergillus fumigatus
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
Q5KEL8
UGM inhibition may provide an attractive drug target in those eukaryotes where galactofuranose plays a critical role in cellular viability and virulence
analysis
-
high-throughput fluorescence polarization assay for indentification of inhibitors of enzyme and homologues
drug development
-
blocking the incorporation of the product galactofuranose into polysaccharides essential for pathogen viability or virulence may lead to novel therapeutics
synthesis
-
production of uridine 5'-(trihydrogen diphosphate) P'-alpha-D-galactofuranosyl ester, a precursor required for the formation of the lipopolysaccharide O-antigen of Klebsiella pneumoniae serotype O1
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
Q5EEK1
UGM inhibition may provide an attractive drug target in those eukaryotes where galactofuranose plays a critical role in cellular viability and virulence
drug development
-
since the enzyme does not exist in Homo sapiens, the parasite enzyme is a target for drug design