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Information on EC 5.4.99.9 - UDP-galactopyranose mutase and Organism(s) Escherichia coli and UniProt Accession P37747

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     5 Isomerases
         5.4 Intramolecular transferases
             5.4.99 Transferring other groups
                5.4.99.9 UDP-galactopyranose mutase
IUBMB Comments
A flavoenzyme which generates UDP-alpha-D-glactofuranose required for cell wall formation in bacteria, fungi, and protozoa.
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This record set is specific for:
Escherichia coli
UNIPROT: P37747
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
mutase, ugm, udp-galactopyranose mutase, udp-galp mutase, afugm, glf-1, mtugm, galactopyranose mutase, tcugm, udp-gal mutase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
UDP-galactopyranose mutase
-
Mutase, uridine diphosphogalactopyranose
-
-
-
-
UDP-Gal mutase
-
-
UDP-galactopyranose mutase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose
show the reaction diagram
chemical reaction mechanism, overview
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isomerization
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
UDP-D-galactopyranose furanomutase
A flavoenzyme which generates UDP-alpha-D-glactofuranose required for cell wall formation in bacteria, fungi, and protozoa.
CAS REGISTRY NUMBER
COMMENTARY hide
174632-18-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
-
-
?
UDP-(6-deoxy-6-fluoro)-D-galactofuranose
UDP-(6-deoxy-6-fluoro)-D-galactopyranose
show the reaction diagram
-
-
-
-
r
UDP-2-deoxy-2-fluoro-D-galactofuranose
?
show the reaction diagram
-
-
-
-
?
UDP-3-deoxy-3-fluoro-D-galactofuranose
?
show the reaction diagram
-
-
-
-
?
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
show the reaction diagram
UDP-D-galactopyranose
UDP-D-galactofuranose
show the reaction diagram
-
-
-
r
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
UDP-L-arabinofuranose
?
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-galactopyranose
UDP-galactofuranose
show the reaction diagram
-
-
?
UDP-alpha-D-galactopyranose
UDP-alpha-D-galactofuranose
show the reaction diagram
-
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD(P)H
or other reductants
flavin
-
flavoenzyme, required for enzyme activation mechanism, overview
NAD(P)+
-
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(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
-
-
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-bis-[1(R)-1,4-dideoxy-1,4-imino-D-galactit-1-yl]-2-butene
-
2.5 mM, 50% residual activity
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-[1(1')Z]-exo-glycal-D-galactopyranose
-
42% inhibition at 1 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5-Deazariboflavin
-
specific activity 29fold higher than of control without illumination
NAD(P)H
-
enzyme activation mechanism, overview
Sodium dithionite
-
20 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
24
UDP-(6-deoxy-6-fluoro)-D-galactofuranose
-
-
0.065
UDP-2-deoxy-2-fluoro-D-galactofuranose
-
-
0.861
UDP-3-deoxy-3-fluoro-D-galactofuranose
-
-
0.022 - 0.194
UDP-D-galactofuranose
0.022
UDP-galactopyranose
-
-
0.6
UDP-L-arabinofuranose
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.4
UDP-(6-deoxy-6-fluoro)-D-galactofuranose
-
-
0.033
UDP-2-deoxy-2-fluoro-D-galactofuranose
-
-
5.7
UDP-3-deoxy-3-fluoro-D-galactofuranose
-
-
1.5 - 27
UDP-D-galactofuranose
27
UDP-galactopyranose
-
-
12
UDP-L-arabinofuranose
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
additional information
-
molecular dynamics studies of active site flexibility, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43000
-
alpha2, 2 * 43000, crystallization
44000
-
alpha2, 2 * 44000, calculated from translated peptide sequence
72000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
solution scattering experiments
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
homodimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
FAD is located in a cleft lined with conserved residues
crystal structure analysis
-
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°
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli
expression in Escherichia coli with a His-tag
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lee, R.; Monsey, D.; Weston, A.; Duncan, K.; Rithner, C.; McNeil, M.
Enzymic synthesis of UDP-galactofuranose and an assay for UDP-galactopyranose mutase based on high-performance liquid chromatography
Anal. Biochem.
242
1-7
1996
Escherichia coli
Manually annotated by BRENDA team
McMahon, S.A.; Leonard, G.A.; Buchanan, L.V.; Giraud, M.F.; Naismith, J.H.
Initiating a crystallographic study of UDP-galactopyranose mutase from Escherichia coli
Acta Crystallogr. Sect. D
55
399-402
1999
Escherichia coli
-
Manually annotated by BRENDA team
Zhang, Q.; Liu, H.w.
Studies of UDP-galactopyranose mutase from Escherichia coli: An unusual role of reduced FAD in its catalysis
J. Am. Chem. Soc.
122
9065-9070
2000
Escherichia coli
-
Manually annotated by BRENDA team
Sanders, D.A.; Staines, A.G.; McMahon, S.A.; McNeil, M.R.; Whitfield, C.; Naismith, J.H.
UDP-galactopyranose mutase has a novel structure and mechanism
Nat. Struct. Biol.
8
858-863
2001
Klebsiella pneumoniae, Escherichia coli (P37747), Escherichia coli
Manually annotated by BRENDA team
Caravano, A.; Dohi, H.; Sinay, P.; Vincent, S.P.
A new methodology for the synthesis of fluorinated exo-glycals and their time-dependent inhibition of UDP-galactopyranose mutase
Chemistry
12
3114-3123
2006
Escherichia coli
Manually annotated by BRENDA team
Eppe, G.; Peltier, P.; Daniellou, R.; Nugier-Chauvin, C.; Ferrieres, V.; Vincent, S.P.
Probing UDP-galactopyranose mutase binding pocket: A dramatic effect on substitution of the 6-position of UDP-galactofuranose
Bioorg. Med. Chem. Lett.
19
814-816
2008
Escherichia coli, Mycobacterium tuberculosis
Manually annotated by BRENDA team
Liautard, V.; Desvergnes, V.; Itoh, K.; Liu, H.W.; Martin, O.R.
Convergent and stereoselective synthesis of iminosugar-containing Galf and UDP-Galf mimicks: evaluation as inhibitors of UDP-Gal mutase
J. Org. Chem.
73
3103-3115
2008
Escherichia coli
Manually annotated by BRENDA team
Caravano, A.; Vincent, S.
Synthesis of three C-glycoside analogues of UDP-galactopyranose as conformational probes for the mutase-catalyzed furanose/pyranose interconversion
Eur. J. Org. Chem.
2009
1771-1780
2009
Escherichia coli
-
Manually annotated by BRENDA team
Tanner, J.J.; Boechi, L.; Andrew McCammon, J.; Sobrado, P.
Structure, mechanism, and dynamics of UDP-galactopyranose mutase
Arch. Biochem. Biophys.
544
128-141
2014
Aspergillus fumigatus, Deinococcus radiodurans, Escherichia coli, Klebsiella pneumoniae, Leishmania infantum, Leishmania major, Leishmania mexicana, Mycobacterium tuberculosis, Trypanosoma cruzi, Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539
Manually annotated by BRENDA team