Information on EC 2.7.7.12 - UDP-glucose-hexose-1-phosphate uridylyltransferase

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

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EC NUMBER
COMMENTARY hide
2.7.7.12
-
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RECOMMENDED NAME
GeneOntology No.
UDP-glucose-hexose-1-phosphate uridylyltransferase
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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
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
D-galactose degradation I (Leloir pathway)
-
-
D-galactose degradation V (Leloir pathway)
-
-
stachyose degradation
-
-
degradation of hexoses
-
-
Galactose metabolism
-
-
Amino sugar and nucleotide sugar metabolism
-
-
Metabolic pathways
-
-
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SYSTEMATIC NAME
IUBMB Comments
UDP-glucose:alpha-D-galactose-1-phosphate uridylyltransferase
-
top
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CAS REGISTRY NUMBER
COMMENTARY hide
9026-21-5
-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
male Hartley
-
-
Manually annotated by BRENDA team
male Hartley
-
-
Manually annotated by BRENDA team
cv. Burpee's Hybrid
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
gene galt
-
-
Manually annotated by BRENDA team
female
-
-
Manually annotated by BRENDA team
male castrated
-
-
Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
-
homology modeling of the three-dimensional protein structure, overview
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate
show the reaction diagram
CDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + CDP-galactose
show the reaction diagram
TDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + TDP-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
UDP-alpha-D-glucose + N-acetyl-alpha-D-galactosamine 1-phosphate
alpha-D-glucose 1-phosphate + UDP-N-acetyl-alpha-D-galactosamine
show the reaction diagram
UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosamine 1-phosphate
alpha-D-glucose 1-phosphate + UDP-N-acetyl-alpha-D-glucosamine
show the reaction diagram
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 + D-galactose 1-phosphate
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
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-alpha-D-galactose
show the reaction diagram
-
-
-
-
?
additional information
?
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
show the reaction diagram
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-alpha-D-galactose
show the reaction diagram
-
-
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
required
additional information
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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
ADP-glucose
-
-
alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate
CDP-glucose
-
-
Cu2+
-
-
cycloheximide
-
i.e. 3-[2-(3,5-dimethyl-2-oxocyclohexyl)-2-hydroxyethyl]glutarimide; inhibition of de novo enzyme synthesis; mutant N314D is more sensitive than the wild-type
D-galactose
D-glucose 6-phosphate
-
erythrocytes
diethyl dicarbonate
-
inactivates the enzyme, reversable by hydroxylamine
diethyldicarbonate
-
erythrocytes
DTNB
-
binds to SH-group in the active center
GDP-glucose
-
-
HgCl2
-
94% inhibition at 0.2 mM
iodoacetate
p-hydroxymercuribenzoate
-
complete inhibition at 0.001 mM
TDP-glucose
-
-
UDP-alpha-D-glucose
-
-
UDP-galactose
UDP-glucose
UDP-glucuronic acid
-
-
UDP-mannose
-
-
UDP-xylose
-
-
Uracil
-
-
uridine
-
-
additional information
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
cysteine
D-galactose
-
galactose growth medium induces enzyme activity, not expression, and increases Vmax by about 50% compared to glucose medium
DTT
-
most effective in activation
glutathione
-
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.011 - 6.66
alpha-D-galactose 1-phosphate
0.092 - 0.5
alpha-D-glucose 1-phosphate
0.051 - 0.324
UDP-alpha-D-galactose
0.0608 - 0.4487
UDP-alpha-D-glucose
0.03 - 0.31
UDP-galactose
0.015 - 0.41
UDP-glucose
additional information
additional information
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0533 - 987
alpha-D-galactose 1-phosphate
5.5 - 17.7
alpha-D-glucose 1-phosphate
0.0167 - 5.52
imidazole
0.98 - 13.6
UDP-alpha-D-glucose
0.0967 - 283
UDP-galactose
0.0217 - 13.5
uridine 5'-phosphoimidazolate
additional information
additional information
-
-
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.8 - 54
alpha-D-galactose 1-phosphate
27 - 111
alpha-D-glucose 1-phosphate
16 - 126
UDP-alpha-D-galactose
3 - 167
UDP-alpha-D-glucose
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.3 - 5.9
alpha-D-glucose 1-phosphate
0.094 - 0.85
UDP-alpha-D-glucose
additional information
additional information
-
product/substrate inhibition pattern and kinetics
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0006
-
partially purified recombinant mutant Q188R
0.00066
-
purified recombinant mutant Q168R
0.00093
0.008
-
HepG2 cells grown on glucose medium
0.012
-
HepG2 cells grown on galactose medium
0.018
-
purified recombinant mutant H164N
0.03
-
partially purified recombinant mutant Q188N
0.058
-
purified enzyme
0.06
-
purified recombinant mutant C52S
0.08
-
partially purified recombinant wild-type enzyme
0.1
-
recombinant mutant Q168G and Q168H, cell extract
0.19
-
recombinant mutant Q168N, cell extract
0.235
substrate N-acetyl-alpha-D-glucose 1-phosphate, pH 7.0, 37°C
0.261
substrate alpha-D-galactose 1-phosphate, pH 7.0, 37°C
0.3
-
purified recombinant mutant C55S
0.334
substrate N-acetyl-alpha-D-galactose 1-phosphate, pH 7.0, 37°C
1.6
-
purified recombinant mutant P185E
2.6
-
purified recombinant mutant P185Q
2.9
-
purified recombinant mutant H115N
3.4
-
purified recombinant mutant Q168N
5.53
-
purified enzyme
6.14
-
purified recombinant mutant P185S
6.9
-
purified recombinant mutant P185G
9.3
-
purified recombinant mutant P185A
12
-
purified recombinant enzyme mutant S135L
12.4
-
purified enzyme
15.1
-
purified nezyme
16.8
-
purified enzyme
25.7
-
purified enzyme
40
-
purified enzyme
44
-
erythrocytes
54.1
-
purified enzyme
56.1
-
purified enzyme
88.5
-
purified recombinant mutant E182A
92.2
-
purified enzyme from placenta
122
-
purified recombinant wild-type enzyme
137
-
purified enzyme
170 - 190
-
purified recombinant enzyme
209
-
purified enzyme
238
-
purified enzyme
1080
-
purified recombinant bifunctional chimeric fusion protein
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
-
assay at
8.5 - 9
-
-
additional information
-
mutant H166G
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.4 - 9
-
about half-maximal activity at pH 4.4 and pH 9.0
7.1 - 9.4
-
56% of maximal activity at pH 7.1 and 83% of maximal activity at pH 9.4
7.2 - 9.8
-
about half-maximal activity at pH 7.2 and about 70% of maximal activity at pH 9.8
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33
-
recombinant mutants P185G and P185A
35
-
recombinant mutant P185S
40
-
recombinant mutants P185E, and P185Q
42 - 48
-
recombinant wild-type and mutant S135L
45
-
recombinant wild-type
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
3 isozymes
5.72 - 5.86
-
3 placental isozymes
additional information
-
different isozymic pattern in cells grown in glucose, galactose or inosine media
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
derived from anterior pituitary gland gonadotropin-producing cells in different stages of the estrous cycle: proestrus, estrus, metestrus, and diestrus
Manually annotated by BRENDA team
-
hepatoblastoma cell line, grown on glucose or galactose
Manually annotated by BRENDA team
additional information
-
expression level of the enzyme changes during the estrous cycle in the anterior pituitary gland
Manually annotated by BRENDA team
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36000
2 * 36000, SDS-PAGE
38000
-
2 * 38000, SDS-PAGE
42000
-
2 * 42000, SDS-PAGE
44000
-
2 * 44000, SDS-PAGE
45000
-
x * 45000, SDS-PAGE
46000
-
2 * 46000, SDS-PAGE
48000
-
x * 48000, SDS-PAGE
55000
x * 55000, calculated; x * 55000, calculated
59000
gel filtration
60000
-
gel filtration
67000
-
gel filtration
79290
-
amino acid sequence determination
82000
-
sedimentation equilibrium centrifugation
86000
-
nondenaturing PAGE
86100
-
sedimentation equilibrium centrifugation
88000
-
sucrose density gradient centrifugation
110000
-
gel filtration
additional information
-
the recombinant chimeric fusion protein exists as monomer, dimer and tetramer, all are active
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
additional information
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
-
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
-
crystal structure of ternary complex reveals a homodimer arrangement that contains a covalent uridylylated intermediate and glucose 1-phosphate in the active site, as well as a structural zinc-binding site, per monomer. Both uridylylation and zinc binding influence the stability and aggregation tendency of human GALT. Q188R, the most commonly detected disease-associated variant, increases the rate of aggregation in the absence of zinc likely due to its reduced ability to form the uridylylated intermediate
-
purified recombinant enzyme, sitting-drop vapour-diffusion method, 10mg/ml protein, 4°C, X-ray diffraction structure determination and analysis at 2.73 A resolution
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5
-
and below, very unstable
642826
6 - 9
-
stable
642826
6
-
t1/2: 18 h, sulfhydryl compounds stabilize
642828
7 - 8
-
fairly stable
642828
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
10 min, 20% loss of activity
44
-
t1/2: 2 min, 2 mg/ml serum albumin stabilizes considerably
48
-
t1/2: 1 min, 2 mg/ml serum albumin stabilizes considerably
additional information
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dithioerythritol stabilizes during purification
-
freeze-thawing inactivates purified enzyme
freezing of dilute enzyme solution inactivates, concentration procedures lead to considerable loss of activity
-
glycerol 20% stabilizes
-
PMSF, EDTA and 2-mercaptoethanol stabilize during purification
-
purified enzyme has tendency to undergo transition to a lower specific activity form
-
SH-reagents stabilize
-
stable to freezing and thawing, purified and crude
-
sulfhydryl reagents restore activity of partially denatured enzyme and protect against inactivation
-
UDP-glucose stabilizes during gel filtration
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, in 0.01 M phosphate buffer, pH 7.5: 40% loss of activity within 2 weeks and 60% within a month, with 20% glycerol: 15% loss of activity within 2 months
-
-20°C, partially purified, 10% loss of activity per month
-
-20°C, stable
-
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
-
0°C, purified enzyme, 10% loss of activity within 2 weeks
-
0°C, purified in the presence of dithioerythritol, 2 weeks
-
4°C, adsorbed to DEAE-cellulose, about 2 months
-
4°C, in 0.01 M potassium phosphate buffer, pH 7.5, inactivation within 2 weeks, 2-mercaptoethanol, DTT and 20% glycerol slightly stabilize
-
freezing inactivates purified enzyme
-
metal ions or/and substrates do not protect from oxidation or proteolysis during prolonged storage
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
213fold to homogeneity
-
4190fold; placental enzyme to homogeneity, coelutes with a 67 kDa glycoprotein
-
45000fold
-
70600fold from erythrocytes
-
about 1800fold to homogeneity
-
about 2000fold
-
about 500fold
His-tagged recombinant wild-type and mutants F171Y and F171L to near homogeneity
-
over 200fold
-
partial from erythrocyte, several isozymes; placental enzyme to homogeneity, coelutes with a 67 kDa glycoprotein
-
recombinant bifunctional fusion protein from strain BL21(DE3), pLysS, pT7ET to near homogeneity, 9fold
-
recombinant enzyme from Escherichia coli strain BL21 (DE3) Codon Plus RIL by heat treatment at 80°C for 10 min, followed by anion exchange and cation exchange chromatography
recombinant enzyme from Escherichia coli strain BL21(DE3) plysS
-
recombinant from overexpressing strain BL21(DE3)
-
recombinant from overexpressing strain BL21(DE3); recombinant wild-type and mutants Q168R and Q168N
-
recombinant from overexpressing strain BL21(DE3); to homogeneity
-
recombinant from overexpressing strain BL21(DE3); wild-type and mutant H166G
-
recombinant His-tagged wild-type and mutant S135L from yeast, to near homogeneity
-
recombinant His-tagged wild-type and mutants P185A, P185S, P185G, P185E, and P185Q to near homogeneity
-
recombinant His-tagged wild-type, partial 67fold, and mutants from Escherichia coli Bl21(DE3)
-
recombinant mutants H166G and H166A
-
recombinant wild-type and mutants from strain BL21(DE3)pLysS to near homogeneity
-
tagged mutant heterodimers from yeast
-
to homogeneity
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3 to 4fold overexpression in strain BL21(DE3)
-
cloning in Escherichia coli and coexpression in yeast of mutant heterodimers derived from galactosemic patients, use of different tags
-
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 as fusion protein with glutathione-S-transferase from Schistosoma japonicum in a bacterial expression system
-
expression in Escherichia coli; expression in Escherichia coli
expression in Sacchaormyces cerevisiae
-
expression of His- and 12CA5 epitope-tagged subunits of mutants R333W and Q188R in yeast, analysis of homo- and heterodimer formation of wild-type and mutant subunits
-
expression of mutant H166G in strain CA13, expression of mutant H166A in strain BL21(DE3)pLysS
-
expression of N314D mutants in human lymphoblasts
-
expression of wild-type and mutant H166G in strain BL21(DE3)
-
expression of wild-type and mutants as His-tagged proteins in Escherichia coli Bl21(DE3)
-
expression of wild-type and mutants in Saccharomyces cerevisiae
-
expression of wild-type and mutants in yeast
-
gene galt, DNA and amino acid sequence determination and analysis
-
gene GALT, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree, expression in Escherichia coli strain BL21(DE3) plysS
-
gene PAE1184, DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli strain BL21 (DE3) Codon Plus RIL
overexpression in strain BL21
-
overexpression of mutants Q168N and Q168R in strain Bl21(DE3)
-
overexpression of wild-type and mutant S135L as His-tagged proteins, 2fold lower expression than the wild-type, in a null-background yeast
-
overexpression of wild-type and mutants in strain BL21(DE3)pLysS
-
the GALT gene is located on chromosome 9p13
-
transient expression of reporter plasmids in HepG2 cells and NS20Y mouse neuroblastoma cells carrying varying fragments of the gene sequence, functional promotor search and analysis, DNA sequencing
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
Q168G
-
site-directed mutagenesis, reduced activity
Q168H
-
site-directed mutagenesis, reduced activity
A101D
-
mutation identified in a in patient with classic galactosemia
A276N
-
mutation identified in a in patient with classic galactosemia
D28Y
-
variant associated with type I galactosemia. 13.5% of wild-type activity
E203K
-
native heterozygous mutant, reduced activity by about 50% in erythrocytes
E291K
-
site-directed mutagenesis for construction of the naturally occuring mutation, 62.8% of wild-type activity, accumulation of alpha-D-galactose 1-phosphate, UDP-galactose and UDP-glucose
E340X/L218L/N314D
-
native mutant, no or nearly no enzyme activity, L218L is a silent mutation, galactosemia phenotype
F171L
-
site-directed mutagenesis, 10fold decreased activity
F171W
-
site-directed mutagenesis, severely reduced abundance
F171Y
-
site-directed mutagenesis, 4% activity compared to wild-type, no inhibition by excess UDP-glucose
F194L
-
variant associated with type I galactosemia. 11.9% of wild-type activity
L139P
-
site-directed mutagenesis for construction of the naturally occuring mutation, 1.9% of wild-type activity, accumulation of alpha-D-galactose 1-phosphate, UDP-galactose and UDP-glucose
L218L/N314D
-
native Duarte-1 D1 variant, L218L is a silent mutation, N314D leads to 110-130% activity compared to the wild-type
L74P
-
variant associated with type I galactosemia, residue is strictly conserved across species. No residual activity
N314D/E203K
-
homozygous N314D mutant with introduced cis mutation E203K does no longer show the reduced, but the full activity and increased thermolablity of mutant without E203K
N314D/G1105C/G1391A
P183T
-
site-directed mutagenesis for construction of the naturally occuring mutation, 45.2% of wild-type activity, accumulation of alpha-D-galactose 1-phosphate, UDP-galactose and UDP-glucose
P185A
-
site-directed mutagenesis, reduced activity and reduced expression level compared to wild-type
P185C
-
site-directed mutagenesis, no remaining activity, same expression level compared to wild-type
P185D
-
site-directed mutagenesis, no remaining activity, same expression level compared to wild-type
P185E
-
site-directed mutagenesis, reduced activity, same expression level compared to wild-type
P185F
-
site-directed mutagenesis, no remaining activity, highly reduced expression level compared to wild-type
P185G
-
site-directed mutagenesis, reduced activity and expression level compared to wild-type
P185H
-
site-directed mutagenesis, no remaining activity, reduced expression level compared to wild-type
P185I
-
site-directed mutagenesis, no remaining activity, highly reduced expression level compared to wild-type
P185K
-
site-directed mutagenesis, no remaining activity, reduced expression level compared to wild-type
P185L
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site-directed mutagenesis, no remaining activity, highly reduced expression level compared to wild-type
P185M
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site-directed mutagenesis, no remaining activity, reduced expression level compared to wild-type
P185N
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site-directed mutagenesis, no remaining activity, reduced expression level compared to wild-type
P185Q
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site-directed mutagenesis, reduced activity, increased expression level compared to wild-type
P185R
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site-directed mutagenesis, no remaining activity, same expression level compared to wild-type
P185S
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site-directed mutagenesis, reduced activity, reduced expression level compared to wild-type
P185T
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site-directed mutagenesis, no remaining activity, reduced expression level compared to wild-type
P185V
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site-directed mutagenesis, no remaining activity, highly reduced expression level compared to wild-type
P185W
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site-directed mutagenesis, no remaining activity, highly reduced expression level compared to wild-type
P185Y
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site-directed mutagenesis, no remaining activity, reduced expression level compared to wild-type
P257T
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mutation identified in a in patient with classic galactosemia
Q188N
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site-directed mutagenesis, reduced activity
Q188P
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variant identified in a patient with classic galactosemia, introduces a missense substitution near the active site of the GALT enzyme. The variant is found in the compound heterozygous state in a child with classic galactosemia, but not in either of her parents. The patient inherited a common Q188R GALT mutation from the mother
R201H
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site-directed mutagenesis for construction of the naturally occuring mutation, 62.8% of wild-type activity, accumulation of alpha-D-galactose 1-phosphate, UDP-galactose and UDP-glucose
R231H
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site-directed mutagenesis for construction of the naturally occuring mutation, below 0.2% of wild-type activity, accumulation of alpha-D-galactose 1-phosphate, UDP-galactose and UDP-glucose
R258C
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native mutant, 15-20% activity compared to wild-type, some clinical symptoms
R259W
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site-directed mutagenesis for construction of the naturally occuring mutation, below 0.2% of wild-type activity, accumulation of alpha-D-galactose 1-phosphate, UDP-galactose and UDP-glucose
R67C
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site-directed mutagenesis for construction of the naturally occuring mutation, 2.3% of wild-type activity, accumulation of alpha-D-galactose 1-phosphate, UDP-galactose and UDP-glucose
T350A
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site-directed mutagenesis for construction of the naturally occuring mutation, 9.9% of wild-type activity, accumulation of alpha-D-galactose 1-phosphate, UDP-galactose and UDP-glucose
V151A
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site-directed mutagenesis for construction of the naturally occuring mutation, 4.6% of wild-type activity, accumulation of alpha-D-galactose 1-phosphate, UDP-galactose and UDP-glucosey
W316X/N314D/G1105C/G1391A
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native mutant, nearly no enzyme activity, galactosemia phenotype
Y165H
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mutation identified in a in patient with classic galactosemia
Y323D
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site-directed mutagenesis for construction of the naturally occuring mutation, 9.6% of wild-type activity, accumulation of alpha-D-galactose 1-phosphate, UDP-galactose and UDP-glucose
additional information
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme reconstitution with different metal ions after denaturation with urea to eliminate the natively bound metal ions
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
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the enzyme activity is measured for determination of galactosaemia using erythrocyte from blood samples, HPLC-based method development, overview
drug development
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the enzyme might be a target for inhibitor design in galactosemia treatment
medicine
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Show AA Sequence (8926 entries)
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LINKS TO OTHER DATABASES (specific for EC-Number 2.7.7.12)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)