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Information on EC 2.7.7.12 - UDP-glucose-hexose-1-phosphate uridylyltransferase and Organism(s) Escherichia coli and UniProt Accession P09148

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Escherichia coli
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
uridyltransferase, galt enzyme, uridyl transferase, hexose-1-phosphate uridylyltransferase, udp-glucose-hexose-1-phosphate uridylyltransferase, galactose-1-phosphate:uridyltransferase, udp-glucose:alpha-d-galactose-1-phosphate uridylyltransferase, udpglucose:alpha-d-galactose-1-phosphate uridylyltransferase, hexose 1-phosphate uridylyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
galactose 1-phosphate uridylyltransferase
-
-
hexose 1-phosphate uridyltransferase
-
-
-
-
hexose 1-phosphate uridylyltransferase
-
-
-
-
hexose-1-phosphate uridylyltransferase
-
-
-
-
UDPGlc:Gal-1-P uridylyltransferase
-
-
UDPglucose-hexose-1-phosphate uridylyltransferase
-
-
UDPglucose:alpha-D-galactose-1-phosphate uridylyltransferase
-
-
-
-
uridyl transferase
-
-
-
-
uridyltransferase
-
-
-
-
uridylylgalactose-1-P uridylyltransferase
-
-
uridylyltransferase, hexose 1-phosphate
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
show the reaction diagram
UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
UDP-glucose:alpha-D-galactose-1-phosphate uridylyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9026-21-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
show the reaction diagram
TDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + TDP-galactose
show the reaction diagram
-
no activity
-
-
?
UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
show the reaction diagram
-
-
-
-
r
UDP-alphaS-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-alphaS-galactose
show the reaction diagram
UDP-glucose + 2-methylimidazole
uridine 5'-phospho-2-methylimidazole + alpha-D-glucose 1-phosphate
show the reaction diagram
UDP-glucose + 4-methylimidazole
uridine 5'-phospho-4-methylimidazole + alpha-D-glucose 1-phosphate
show the reaction diagram
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
show the reaction diagram
UDP-glucose + imidazole
uridine 5'-phosphoimidazole + alpha-D-glucose 1-phosphate
show the reaction diagram
uridine 5'-phospho-2,4,5-trimethylimidazole + alpha-D-glucose 1-phosphate
UDP-glucose + 2,4,5-trimethylimidazole
show the reaction diagram
uridine 5'-phospho-2-methylimidazole + alpha-D-glucose 1-phosphate
UDP-glucose + 2-methylimidazole
show the reaction diagram
uridine 5'-phospho-3-methylimidazole + alpha-D-glucose 1-phosphate
UDP-glucose + 3-methylimidazole
show the reaction diagram
uridine 5'-phospho-4-methylimidazole + alpha-D-glucose 1-phosphate
UDP-glucose + 4-methylimidazole
show the reaction diagram
uridine 5'-phospho-5-methylimidazole + alpha-D-glucose 1-phosphate
UDP-glucose + 5-methylimidazole
show the reaction diagram
additional information
?
-
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-alpha-D-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
show the reaction diagram
-
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
mutant E182A
1,10-phenanthroline
-
inactivation of the enzyme by chelation of Zn2+ and Fe2+ ions, UDP-glucose protects, but alpha-D-glucose 1-phosphate does not
2,2'-bipyridyl
-
inactivation of the enzyme by chelation of Zn2+ and Fe2+ ions
8-hydroxyquinoline
-
inactivation of the enzyme by chelation of Zn2+ and Fe2+ ions
8-Hydroxyquinoline sulfonate
-
inactivation of the enzyme by chelation of Zn2+ and Fe2+ ions
alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate
-
product/substrate inhibition
diethyl dicarbonate
-
inactivates the enzyme, reversable by hydroxylamine
DTNB
-
binds to SH-group in the active center
NEM
-
complete inhibition at 0.05 mM
UDP-galactose
UDP-glucose
-
product/substrate inhibition
additional information
-
product inhibition study, wild-type and mutants H166G and H166A
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
2fold at 10 mM
cysteine
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.125 - 0.77
alpha-D-galactose 1-phosphate
0.14 - 0.2
alpha-D-glucose 1-phosphate
0.048 - 0.12
UDP-galactose
0.072 - 0.39
UDP-glucose
0.125 - 1.54
alpha-D-galactose 1-phosphate
0.14 - 0.5
alpha-D-glucose 1-phosphate
0.12 - 0.31
UDP-galactose
0.072 - 0.41
UDP-glucose
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0533 - 780
alpha-D-galactose 1-phosphate
0.0967 - 283
UDP-galactose
0.0533 - 780
alpha-D-galactose 1-phosphate
0.0167 - 5.52
imidazole
0.0217 - 13.5
uridine 5'-phosphoimidazolate
additional information
additional information
-
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
product/substrate inhibition pattern and kinetics
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00093
recombinant mutant S161A, cell extract
0.018
purified recombinant mutant H164N
0.023
purified recombinant mutant S161A
0.06
purified recombinant mutant C52S
0.3
purified recombinant mutant C55S
14.9
recombinant mutant C160S, cell extract
16.3
recombinant wild-type, cell extract
180
purified recombinant wild-type enzyme
2.9
purified recombinant mutant H115N
79.5
purified recombinant mutant C160A
88.5
purified recombinant mutant E182A
9.9
recombinant mutant C160A, cell extract
0.00066
-
purified recombinant mutant Q168R
0.00093
-
recombinant mutant S161A, cell extract
0.023
-
purified recombinant mutant S161A
0.1
-
recombinant mutant Q168G and Q168H, cell extract
0.19
-
recombinant mutant Q168N, cell extract
1080
-
purified recombinant bifunctional chimeric fusion protein
14.9
-
recombinant mutant C160S, cell extract
16.3
-
recombinant wild-type, cell extract
170 - 190
-
purified recombinant enzyme
180
-
purified recombinant wild-type enzyme
209
-
purified enzyme
238
-
purified enzyme
3.4
-
purified recombinant mutant Q168N
79.5
-
purified recombinant mutant C160A
9.9
-
recombinant mutant C160A, cell extract
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5 - 9
-
-
additional information
-
mutant H166G
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2 - 9.8
-
about half-maximal activity at pH 7.2 and about 70% of maximal activity at pH 9.8
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
activation energy, temperature profile
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
GALT belongs to the histidine triad family of transferases
metabolism
-
the enzyme catalyzes a critical step in the Leloir pathway, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41000
79290
-
amino acid sequence determination
80000
additional information
-
the recombinant chimeric fusion protein exists as monomer, dimer and tetramer, all are active
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
homodimer
-
-
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
H166G mutant enzyme/UDP-glucose or UDP-galactose complexes, X-ray diffraction structure determination and analysis
uridyl/enzyme complex, X-ray diffraction structure determination and analysis
17.5-23 mg/ml recombinant protein, hanging drop vapour diffusion method in the presence of 4 mM substrate analog phenyl-UDP, 277 K, 0.1 M sodium succinate, pH 5.9, 0.25 M NaCl, 0.4 M Li2SO4, over 14.5% w/w polyethylene glycol 10000, 1 mM NaN3, 5-6 days, X-ray diffraction structure determination and analysis
-
crystal structure determination and analysis
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C160A
site-directed mutagenesis, 18fold reduced activity
C160S
site-directed mutagenesis, 12fold reduced activity
C52S
site-directed mutagenesis, 3000fold less active than the wild-type, no formation of reaction intermediate UMP-enzyme, low metal content, low expression level
C55S
site-directed mutagenesis, 600fold less active than the wild-type, no formation of reaction intermediate UMP-enzyme, low metal content, low expression level
E182A
site-directed mutagenesis, 50% activity compared to wild-type, normal formation of reaction intermediate UMP-enzyme, contains reduced zinc content and no iron
H115N
site-directed mutagenesis, 2.9% activity compared to wild-type, slightly reduced formation of reaction intermediate UMP-enzyme, retention of zinc and iron
H164N
site-directed mutagenesis, 10000fold less active than the wild-type, no formation of reaction intermediate UMP-enzyme, low metal content, low expression level
H166G
S161A
site-directed mutagenesis, 7000fold reduced activity compared to wild-type
H166 A
-
site-directed mutagenesis, point mutation leads to shift of the enzyme activity to UDP-hexose synthase activity, formation of uridine 5'-phosphoimidazolate and alpha-D-glucose 1-phosphate from UDP-glucose and imidazole, highly reduced activity compared to H166G mutant
H166G
Q168G
-
site-directed mutagenesis, reduced activity
Q168H
-
site-directed mutagenesis, reduced activity
Q168N
Q168R
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freeze-thawing inactivates purified enzyme
-
PMSF, EDTA and 2-mercaptoethanol stabilize during purification
-
purified enzyme has tendency to undergo transition to a lower specific activity form
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0°C, 10% loss of activity per week
-
0°C, 5 mM potassium phosphate buffer, pH 7, 20 mg/ml bovine serum albumin, 5 h stable
-
metal ions or/and substrates do not protect from oxidation or proteolysis during prolonged storage
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutants from strain BL21(DE3)pLysS to near homogeneity
over 200fold
-
recombinant bifunctional fusion protein from strain BL21(DE3), pLysS, pT7ET to near homogeneity, 9fold
-
recombinant from overexpressing strain BL21(DE3)
-
recombinant mutants H166G and H166A
-
recombinant wild-type and mutants Q168R and Q168N
-
to homogeneity
-
wild-type and mutant H166G
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression of wild-type and mutants in strain BL21(DE3)pLysS
3 to 4fold overexpression in strain BL21(DE3)
-
construction and overexpression of bifunctional fusion protein composed of galactose-2-phosphate uridylyltransferase and UDP-galactose 4-epimerase with an intervening linker of 3 Ala residues
-
expression of mutant H166G in strain CA13, expression of mutant H166A in strain BL21(DE3)pLysS
-
expression of wild-type and mutant H166G in strain BL21(DE3)
-
overexpression in strain BL21
-
overexpression of mutants Q168N and Q168R in strain Bl21(DE3)
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
enzyme reconstitution with different metal ions after denaturation with urea to eliminate the natively bound metal ions
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tamada, Y.; Swanson, B.A.; Arabshahi, A.; Frey, P.A.
Preparation and characterization of a bifunctional fusion enzyme composed of UDP-galactose 4-epimerase and galactose-1-P uridylyltransferase
Bioconjug. Chem.
5
660-665
1994
Escherichia coli
Manually annotated by BRENDA team
Saito, S.; Ozutsumi, M.; Kurahashi, K.
Galactose 1-phosphate uridylyltransferase of Escherichia coli. II. Further purification and characterization
J. Biol. Chem.
242
2362-2368
1967
Escherichia coli
Manually annotated by BRENDA team
Arabshahi, A.; Brody, R.S.; Smallwood, A.; Tsai, T.C.; Frey, P.A.
Galactose-1-phosphate uridylyltransferase. Purification of the enzyme and stereochemical course of each step of the double-displacement mechanism
Biochemistry
25
5583-5589
1986
Escherichia coli
Manually annotated by BRENDA team
Wedekind, J.E.; Frey, P.A.; Rayment, I.
Crystallization and preliminary crystallographic analysis of galactose-1-phosphate uridylyltransferase from Escherichia coli
Acta Crystallogr. Sect. D
50
329-331
1994
Escherichia coli
Manually annotated by BRENDA team
Chowdhury, R.R.
Purification & some properties of galactose-1-phosphate uridylyl transferase from E. coli
Indian J. Biochem. Biophys.
16
273-277
1979
Escherichia coli
Manually annotated by BRENDA team
Frey, P.A.; Wong, L.J.; Sheu, K.F.; Yang, S.L.
Galactose-1-phosphate uridylyltransferase: detection, isolation, and characterization of the uridylyl enzyme
Methods Enzymol.
87
20-36
1982
Saccharomyces cerevisiae, Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Arabshahi, A.; Ruzicka, F.J.; Geeganage, S.; Frey, P.A.
Standard free energies for uridylyl group transfer by hexose-1-P uridylyltransferase and UDP-hexose synthase and for the hydrolysis of uridine 5'-phosphoimidazolate
Biochemistry
35
3426-3428
1996
Escherichia coli
Manually annotated by BRENDA team
Ruzicka, F.J.; Geeganage, S.; Frey, P.A.
Kinetic mechanism of UDP-hexose synthase, a point variant of hexose-1-phosphate uridylyltransferase from Escherichia coli
Biochemistry
37
11385-11392
1998
Escherichia coli
Manually annotated by BRENDA team
Lai, K.; Willis, A.C.; Elsas, L.J.
The biochemical role of glutamine 188 in human galactose-1-phosphate uridyltransferase
J. Biol. Chem.
274
6559-6566
1999
Escherichia coli (P09148), Homo sapiens
Manually annotated by BRENDA team
Thoden, J.B.; Ruzicka, F.J.; Frey, P.A.; Rayment, I.; Holden, H.M.
Structural analysis of the H166G site-directed mutant of galactose 1-phosphate uridylyltransferase complexed with either UDP-glucose or UDP-galactose: detailed description of the nucleotide sugar binding site
Biochemistry
36
1212-1222
1997
Escherichia coli (P09148)
Manually annotated by BRENDA team
Wedekind, J.E.; Frey, P.A.; Rayment, I.
The structure of nucleotidylated histidine-166 of galactose-1-phosphate uridylyltransferase provides insight into phosphoryl group transfer
Biochemistry
35
11560-11569
1996
Escherichia coli (P09148)
Manually annotated by BRENDA team
Ruzicka, F.J.; Wedekind, J.E.; Kim, J.; Rayment, I.; Frey, P.A.
Galactose-1-phosphate uridylyltransferase from Escherichia coli, a zinc and iron metalloenzyme
Biochemistry
34
5610-5617
1995
Escherichia coli
Manually annotated by BRENDA team
Quimby, B.B.; Wells, L.; Wilkinson, K.D.; Fridovich-Keil, J.L.
Functional requirements of the active site position 185 in the human enzyme galactose-1-phosphate uridylyltransferase
J. Biol. Chem.
271
26835-26842
1996
Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Geeganage, S.; Frey, P.A.
Transient kinetics of formation and reaction of the uridylyl-enzyme form of galactose-1-P uridylyltransferase and its Q168R-variant: insight into the molecular basis of galactosemia
Biochemistry
37
14500-14507
1998
Escherichia coli
Manually annotated by BRENDA team
Geeganage, S.; Frey, P.A.
Significance of metal ions in galactose-1-phosphate uridylyltransferase: an essential structural zinc and a nonessential structural iron
Biochemistry
38
13398-13406
1999
Escherichia coli (P09148)
Manually annotated by BRENDA team
Geeganage, S.; Ling, V.W.; Frey, P.A.
Roles of two conserved amino acid residues in the active site of galactose-1-phosphate uridylyltransferase: an essential serine and a nonessential cysteine
Biochemistry
39
5397-5404
2000
Escherichia coli (P09148)
Manually annotated by BRENDA team
Geeganage, S.; Frey, P.A.
Galactose-1-phosphate uridylyltransferase: kinetics of formation and reaction of uridylyl-enzyme intermediate in wild-type and specifically mutated uridylyltransferases
Methods Enzymol.
354
134-148
2002
Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
McCorvie, T.J.; Timson, D.J.
The structural and molecular biology of type I galactosemia: enzymology of galactose 1-phosphate uridylyltransferase
IUBMB Life
63
694-700
2011
Escherichia coli, Homo sapiens
Manually annotated by BRENDA team