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

for references in articles please use BRENDA:EC2.7.7.12
Word Map on EC 2.7.7.12
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)


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

top print hide
EC NUMBER
COMMENTARY hide
2.7.7.12
-
top print hide
RECOMMENDED NAME
GeneOntology No.
UDP-glucose-hexose-1-phosphate uridylyltransferase
top print hide
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
top print hide
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
-
-
-
-
top print hide
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
-
-
top print hide
SYSTEMATIC NAME
IUBMB Comments
UDP-glucose:alpha-D-galactose-1-phosphate uridylyltransferase
-
top
top print hide
CAS REGISTRY NUMBER
COMMENTARY hide
9026-21-5
-
top print hide
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
top print hide
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
-
homology modeling of the three-dimensional protein structure, overview
top print hide
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
?
-
top print hide
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
-
-
-
-
?
top print hide
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
required
additional information
top print hide
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
-
top print hide
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
-
-
top print hide
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
-
top print hide
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
-
-
-
top print hide
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
top print hide
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
-
top print hide
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
top print hide
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
-
assay at
8.5 - 9
-
-
additional information
-
mutant H166G
top print hide
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
top print hide
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
top print hide
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
top print hide
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
top print hide
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
top print hide
PDB
SCOP
CATH
UNIPROT
ORGANISM
Escherichia coli (strain K12);
Homo sapiens;
top print hide
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
top print hide
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
additional information
top print hide
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
top print hide
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
top print hide
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
top print hide
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
-
top print hide
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
-
top print hide
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
top print hide
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
top print hide
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
-
site-directed mutagenesis, no remaining activity, highly reduced expression level compared to wild-type
P185M
-
site-directed mutagenesis, no remaining activity, reduced expression level compared to wild-type
P185N
-
site-directed mutagenesis, no remaining activity, reduced expression level compared to wild-type
P185Q
-
site-directed mutagenesis, reduced activity, increased expression level compared to wild-type
P185R
-
site-directed mutagenesis, no remaining activity, same expression level compared to wild-type
P185S
-
site-directed mutagenesis, reduced activity, reduced expression level compared to wild-type
P185T
-
site-directed mutagenesis, no remaining activity, reduced expression level compared to wild-type
P185V
-
site-directed mutagenesis, no remaining activity, highly reduced expression level compared to wild-type
P185W
-
site-directed mutagenesis, no remaining activity, highly reduced expression level compared to wild-type
P185Y
-
site-directed mutagenesis, no remaining activity, reduced expression level compared to wild-type
P257T
-
mutation identified in a in patient with classic galactosemia
Q188N
-
site-directed mutagenesis, reduced activity
Q188P
-
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
-
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
-
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
-
native mutant, 15-20% activity compared to wild-type, some clinical symptoms
R259W
-
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
-
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
-
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
-
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
-
native mutant, nearly no enzyme activity, galactosemia phenotype
Y165H
-
mutation identified in a in patient with classic galactosemia
Y323D
-
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
top print hide
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme reconstitution with different metal ions after denaturation with urea to eliminate the natively bound metal ions
-
top print hide
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
-
the enzyme activity is measured for determination of galactosaemia using erythrocyte from blood samples, HPLC-based method development, overview
drug development
-
the enzyme might be a target for inhibitor design in galactosemia treatment
medicine
top
Show AA Sequence (8880 entries)
Longer loading times are possible. Please use the Sequence Search for a specific query.
top
top
top
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)