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Information on EC 2.7.7.12 - UDP-glucose-hexose-1-phosphate uridylyltransferase and Organism(s) Homo sapiens and UniProt Accession P07902

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The taxonomic range for the selected organisms is: Homo sapiens
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
-
galactose-1-phosphate uridyl transferase
-
galactose-1-phosphate uridyltransferase
-
galactose-1-phosphate uridylyltransferase
-
galactose 1-phosphate uridylyltransferase
-
-
galactose-1-phosphate uridyl transferase
-
-
galactose-1-phosphate uridyltransferase
-
-
galactose-1-phosphate uridylyltransferase
-
-
galactose-1-phosphate:uridyltransferase
-
-
GALT enzyme
-
-
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
-
-
-
-
uridine diphosphoglucose:alpha-D-galactose-1-phosphate uridilyltransferase
-
-
uridyl transferase
-
-
-
-
uridyltransferase
-
-
-
-
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
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
alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate
show the reaction diagram
-
-
-
r
UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
show the reaction diagram
-
-
-
r
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
UDP-glucose + D-galactose 1-phosphate
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
-
-
-
-
?
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
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-alpha-D-galactose
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zinc
zinc binding stabilizes the enzyme
Zn2+
-
the zinc co-orientating residues are not conserved and therefore, it may only bind one metal ion per monomer
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-fluoro-galactose-1-phosphate
competitively inhibit recombinant enzyme
-
alpha-D-glucose 1-phosphate
-
UDP-alpha-D-glucose
-
ADP-glucose
-
-
alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate
CDP-glucose
-
-
cycloheximide
D-galactose
D-glucose 6-phosphate
-
erythrocytes
diethyldicarbonate
-
erythrocytes
GDP-glucose
-
-
iodoacetate
-
erythrocytes
PCMB
-
erythrocytes
TDP-glucose
-
-
UDP-galactose
-
the product of the forward reaction is a competitive inhibitor with respect to UDP-glucose and a mixed inhibitor with respect to galactose 1-phosphate
UDP-glucose
UDP-glucuronic acid
-
-
UDP-mannose
-
-
UDP-xylose
-
-
Uracil
-
-
uridine
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-galactose
-
galactose growth medium induces enzyme activity, not expression, and increases Vmax by about 50% compared to glucose medium
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0459 - 1.184
alpha-D-galactose 1-phosphate
0.118 - 0.202
alpha-D-glucose 1-phosphate
0.0897 - 0.324
UDP-alpha-D-galactose
0.0608 - 0.4487
UDP-alpha-D-glucose
0.011 - 0.64
alpha-D-galactose 1-phosphate
0.015 - 0.4
UDP-glucose
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.5 - 17.7
alpha-D-glucose 1-phosphate
0.98 - 13.6
UDP-alpha-D-glucose
3.6 - 98
alpha-D-galactose 1-phosphate
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
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.9
2-fluoro-galactose-1-phosphate
pH and temperature not specified in the publication
-
2.3 - 5.9
alpha-D-glucose 1-phosphate
0.094 - 0.85
UDP-alpha-D-glucose
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0006
-
partially purified recombinant mutant Q188R
0.008
-
HepG2 cells grown on glucose medium
0.012
-
HepG2 cells grown on galactose medium
0.03
-
partially purified recombinant mutant Q188N
0.058
-
purified enzyme
0.08
-
partially purified recombinant wild-type enzyme
1.6
-
purified recombinant mutant P185E
12
-
purified recombinant enzyme mutant S135L
122
-
purified recombinant wild-type enzyme
15.1
-
purified enzyme
16.8
-
purified enzyme
2.6
-
purified recombinant mutant P185Q
40
-
purified enzyme
44
-
erythrocytes
56.1
-
purified enzyme
6.14
-
purified recombinant mutant P185S
6.9
-
purified recombinant mutant P185G
9.3
-
purified recombinant mutant P185A
92.2
-
purified enzyme from placenta
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33
-
recombinant mutants P185G and P185A
35
-
recombinant mutant P185S
37
-
assay at
40
-
recombinant mutants P185E, and P185Q
42 - 48
-
recombinant wild-type and mutant S135L
45
-
recombinant wild-type
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
activation energy, temperature profile
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
hepatoblastoma cell line, grown on glucose or galactose
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
evolution
-
GALT belongs to the histidine triad family of transferases
malfunction
-
reduced galactose 1-phosphate uridylyltransferase activity is associated with the genetic disease type I galactosemia. Enzyme-deficiency results in an increase in the cellular concentration of galactose 1-phosphate. The accumulation of this toxic metabolite, combined with aberrant glycoprotein and glycolipid biosynthesis, is likely to be the major factor in molecular pathology
metabolism
-
the enzyme catalyzes a critical step in the Leloir pathway, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GALT_HUMAN
379
0
43363
Swiss-Prot
other Location (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
44000
-
2 * 44000, SDS-PAGE
45000
-
x * 45000, SDS-PAGE
46000
-
2 * 46000, SDS-PAGE
48000
-
x * 48000, SDS-PAGE
67000
-
gel filtration
86000
-
nondenaturing PAGE
88000
-
sucrose density gradient centrifugation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
sitting-drop vapour diffusion at 20°C. 1.9 A resolution crystal structure of human GALT 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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
F171S
variant associated with type I galactosemia, residue is strictly conserved across species. No residual activity
F194L
variant associated with type I galactosemia. 11.9% of wild-type activity
K285N
L74P
variant associated with type I galactosemia, residue is strictly conserved across species. No residual activity
N314D
P257T
mutation identified in a in patient with classic galactosemia
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
Q188R
R333G
variant associated with type I galactosemia, residue is strictly conserved across species. 0.6% of wild.type activtiy
S135L
Y165H
mutation identified in a in patient with classic galactosemia
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
F171S
F171W
-
site-directed mutagenesis, severely reduced abundance
F171Y
-
site-directed mutagenesis, 4% activity compared to wild-type, no inhibition by excess UDP-glucose
K285N
-
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
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
N314D
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
Q188N
-
site-directed mutagenesis, reduced activity
Q188R
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
R333G
-
native mutant, 20% activity compared to wild-type, no clinical symptoms
R333W
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
S135L
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
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
44
-
t1/2: 2 min, 2 mg/ml serum albumin stabilizes considerably
48
-
t1/2: 1 min, 2 mg/ml serum albumin stabilizes considerably
50
-
15 min, 30% loss of activity for the wild-type enzyme, over 55% loss of activity for the homozygous N314D mutant
additional information
-
increased thermal lability of the mutant N314D compared to the wild-type
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
-
sulfhydryl reagents restore activity of partially denatured enzyme and protect against inactivation
-
UDP-glucose stabilizes during gel filtration
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, partially purified, 10% loss of activity per month
-
0°C, 10% loss of activity per week
-
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
-
freezing inactivates purified enzyme
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
4190fold
-
45000fold
-
70600fold from erythrocytes
-
about 500fold
-
His-tagged recombinant wild-type and mutants F171Y and F171L to near homogeneity
-
partial from erythrocyte, several isozymes
-
placental enzyme to homogeneity, coelutes with a 67 kDa glycoprotein
-
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)
-
tagged mutant heterodimers from yeast
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Sacchaormyces cerevisiae
cloning in Escherichia coli and coexpression in yeast of mutant heterodimers derived from galactosemic patients, use of different tags
-
expression as fusion protein with glutathione-S-transferase from Schistosoma japonicum in a bacterial expression system
-
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 N314D mutants in human lymphoblasts
-
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
-
overexpression of wild-type and mutant S135L as His-tagged proteins, 2fold lower expression than the wild-type, in a null-background yeast
-
the GALT gene is located on chromosome 9p13
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mayes, J.S.; Hansen, R.G.
Galactose 1-phosphate uridyl transferase
Methods Enzymol.
9
708-713
1966
Bos taurus, Homo sapiens
-
Manually annotated by BRENDA team
Helmer, G.R.; Williams, V.P.
Purification of galactose-1-phosphate uridylyltransferase from human placenta
Arch. Biochem. Biophys.
210
573-580
1981
Homo sapiens
Manually annotated by BRENDA team
Williams, V.P.; Helmer, G.R.; Fried, C.
Human galactose-1-phosphate uridylyltransferase: purification and comparison of the red blood cell and placental enzymes
Arch. Biochem. Biophys.
216
503-511
1982
Homo sapiens
Manually annotated by BRENDA team
Williams, V.P.
Purification and some properties of galactose 1-phosphate uridylyltransferase from human red cells
Arch. Biochem. Biophys.
191
182-191
1978
Homo sapiens
Manually annotated by BRENDA team
Kelly, S.; Sweeney, P.; Schedlbauer, L.
Galactose-l-phosphate uridyl transferase activity in red cells of various animal species
Experientia
37
550-553
1981
Bos taurus, Capra hircus, Cavia porcellus, Cavia porcellus Hartley, Chlorocebus aethiops, Equus caballus, Homo sapiens, Oryctolagus cuniculus, Ovis aries, Rattus norvegicus
Manually annotated by BRENDA team
Ellis, G.; Goldberg, D.M.
Galactose-1-phosphate uridylytransferase. UDPglucose:alpha-D-galactose-1-phosphate uridylyltransferase, EC 2.7.7.12
Methods Enzym. Anal. , 3rd. Ed. (Bergmeyer, H. U. , ed. )
3
560-571
1983
Bos taurus, Homo sapiens
-
Manually annotated by BRENDA team
Banroques, J.; Gregori, C.; Schapira, F.
Purification and characterization of human erythrocyte uridylyl transferase
Biochim. Biophys. Acta
657
374-382
1981
Homo sapiens
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
Daude, N.; Lestage, J.; Reichardt, J.K.; Petry, K.G.
Expression of galactose-1-phosphate uridyltransferase in the anterior pituitary of rat during the estrous cycle
Neuroendocrinology
64
42-48
1996
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Podskarbi, T.; Kohlmetz, T.; Gathof, B.S.; Kleinlein, B.; Bieger, W.P.; Gresser, U.; Shin, Y.S.
Molecular characterization of Duarte-1 and Duarte-2 variants of galactose-1-phosphate uridyltransferase
J. Inherit. Metab. Dis.
19
638-644
1996
Homo sapiens
Manually annotated by BRENDA team
Wells, L.; Fridovich-Keil, J.L.
Biochemical characterization of the S135L allele of galactose-1-phosphate uridylyltransferase associated with galactosaemia
J. Inherit. Metab. Dis.
20
633-642
1997
Homo sapiens
Manually annotated by BRENDA team
Lai, K.; Langley, S.D.; Dembure, P.P.; Hjelm, L.N.; Elsas, L.J.2nd.
Duarte allele impairs biostability of galactose-1-phosphate uridyltransferase in human lymphoblasts
Hum. Mutat.
11
28-38
1998
Homo sapiens
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
Davit-Spraul, A.; Pourci, M.L.; Ng, K.H.; Soni, T.; Lemonnier, A.
Regulatory effects of galactose on galactose-1-phosphate uridyltransferase activity on human hepatoblastoma HepG2 cells
FEBS Lett.
354
232-236
1994
Homo sapiens
Manually annotated by BRENDA team
Shin, Y.S.; Zschocke, J.; Das, A.M.; Podskarbi, T.
Molecular and biochemical basis for variants and deficiency forms of galactose-1-phosphate uridyltransferase
J. Inherit. Metab. Dis.
22
327-329
1999
Homo sapiens
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
Elsevier, J.P.; Wells, L.; Quimby, B.B.; Fridovich-Keil, J.L.
Heterodimer formation and activity in the human enzyme galactose-1-phosphate uridylyltransferase
Proc. Natl. Acad. Sci. USA
93
7166-7171
1996
Homo sapiens
Manually annotated by BRENDA team
Crews, C.; Wilkinson, K.D.; Wells, L.; Perkins, C.; Fridovich-Keil, J.L.
Functional consequence of substitutions at residue 171 in human galactose-1-phosphate uridylyltransferase
J. Biol. Chem.
275
22847-22853
2000
Homo sapiens
Manually annotated by BRENDA team
Riehman, K.; Crews, C.; Fridovich-Keil, J.L.
Relationship between genotype, activity, and galactose sensitivity in yeast expressing patient alleles of human galactose-1-phosphate uridylyltransferase
J. Biol. Chem.
276
10634-10640
2001
Homo sapiens
Manually annotated by BRENDA team
Christacos, N.C.; Fridovich-Keil, J.L.
Impact of patient mutations on heterodimer formation and function in human galactose-1-P uridylyltransferase
Mol. Genet. Metab.
76
319-326
2002
Homo sapiens
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
Coffee, B.; Hjelm, L.N.; DeLorenzo, A.; Courtney, E.M.; Yu, C.; Muralidharan, K.
Characterization of an unusual deletion of the galactose-1-phosphate uridyl transferase (GALT) gene
Genet. Med.
8
635-640
2006
Homo sapiens
Manually annotated by BRENDA team
Karas-Kuzelicki, N.; Pfeifer, V.; Lukac-Bajalo, J.
Synergistic effect of high lactase activity genotype and galactose-1-phosphate uridyl transferase (GALT) mutations on idiopathic presenile cataract formation
Clin. Biochem.
41
869-874
2008
Homo sapiens (P07902)
Manually annotated by BRENDA team
Prodan-Zitnik, I.; Karas-Kuzelicki, N.; Lukac-Bajalo, J.
Positive correlation between galactose-1-phosphate uridyltransferase (GALT) and UDP-galactose-4-epimerase (GALE) activities
Clin. Biochem.
42
1561-1564
2009
Homo sapiens
Manually annotated by BRENDA team
Carney, A.E.; Sanders, R.D.; Garza, K.R.; McGaha, L.A.; Bean, L.J.; Coffee, B.W.; Thomas, J.W.; Cutler, D.J.; Kurtkaya, N.L.; Fridovich-Keil, J.L.
Origins, distribution and expression of the Duarte-2 (D2) allele of galactose-1-phosphate uridylyltransferase
Hum. Mol. Genet.
18
1624-1632
2009
Homo sapiens (P07902)
Manually annotated by BRENDA team
Lindhout, M.; Rubio-Gozalbo, M.E.; Bakker, J.A.; Bierau, J.
Direct non-radioactive assay of galactose-1-phosphate:uridyltransferase activity using high performance liquid chromatography
Clin. Chim. Acta
411
980-983
2010
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
McCorvie, T.J.; Gleason, T.J.; Fridovich-Keil, J.L.; Timson, D.J.
Misfolding of galactose 1-phosphate uridylyltransferase can result in type I galactosemia
Biochim. Biophys. Acta
1832
1279-1293
2013
Homo sapiens (P07902), Homo sapiens
Manually annotated by BRENDA team
Choi, R.; Jo, K.I.; Ko, D.H.; Lee, D.H.; Song, J.; Jin, D.K.; Ki, C.S.; Lee, S.Y.; Kim, J.W.; Lee, Y.W.; Park, H.D.
Novel GALT variations and mutation spectrum in the Korean population with decreased galactose-1-phosphate uridyltransferase activity
BMC Med. Genet.
15
94
2014
Homo sapiens (P07902), Homo sapiens
Manually annotated by BRENDA team
McCorvie, T.J.; Kopec, J.; Pey, A.L.; Fitzpatrick, F.; Patel, D.; Chalk, R.; Shrestha, L.; Yue, W.W.
Molecular basis of classic galactosemia from the structure of human galactose 1-phosphate uridylyltransferase
Hum. Mol. Genet.
25
2234-2244
2016
Homo sapiens (P07902)
Manually annotated by BRENDA team
Papachristoforou, R.; Petrou, P.P.; Sawyer, H.; Williams, M.; Drousiotou, A.
A novel large deletion encompassing the whole of the galactose-1-phosphate uridyltransferase (GALT) gene and extending into the adjacent interleukin 11 receptor alpha (IL11RA) gene causes classic galactosemia associated with additional phenotypic abnormalities
JIMD Rep.
12
91-98
2014
Homo sapiens (P07902), Homo sapiens
Manually annotated by BRENDA team
Tran, T.T.; Liu, Y.; Zwick, M.E.; Ramachandran, D.; Cutler, D.J.; Huang, X.; Berry, G.T.; Fridovich-Keil, J.L.
A de novo variant in galactose-1-P uridylyltransferase (GALT) leading to classic galactosemia
JIMD Rep.
19
1-6
2015
Homo sapiens (P07902), Homo sapiens
Manually annotated by BRENDA team
Janes, V.; Grabany, S.; Delbrouck, J.; Vincent, S.P.; Gottschalk, J.; Elling, L.; Hanisch, F.G.
Fluorinated galactoses inhibit galactose-1-phosphate uridyltransferase and metabolically induce galactosemia-like phenotypes in HEK-293 cells
Cells
9
607
2020
Homo sapiens (P07902)
Manually annotated by BRENDA team
Kumar S, U.; Kumar D, T.; R, S.; Doss C, G.P.; Zayed, H.
An extensive computational approach to analyze and characterize the functional mutations in the galactose-1-phosphate uridyl transferase (GALT) protein responsible for classical galactosemia
Comput. Biol. Med.
117
103583
2020
Homo sapiens (P07902)
Manually annotated by BRENDA team
McCorvie, T.J.; Kopec, J.; Pey, A.L.; Fitzpatrick, F.; Patel, D.; Chalk, R.; Shrestha, L.; Yue, W.W.
Molecular basis of classic galactosemia from the structure of human galactose 1-phosphate uridylyltransferase
Hum. Mol. Genet.
25
2234-2244
2016
Homo sapiens (P07902)
Manually annotated by BRENDA team
De Lucca, M.; Casique, L.; Cornejo, V.
Alterations of galactose metabolism caused by deficit of galactose-1-phosphate uridylyltransferase activity An overview of galactosemia type I
Molecular Nutrition: Carbohydrates (ed. Patel V.B.)
2019
369-395
2019
Homo sapiens (P07902)
-
Manually annotated by BRENDA team