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Information on EC 2.7.7.12 - UDP-glucose-hexose-1-phosphate uridylyltransferase
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EC Tree
2.7.7.12 UDP-glucose-hexose-1-phosphate uridylyltransferaseSpecify your search results
Word Map
- 2.7.7.12
- galactosemia
- galactokinase
-
duarte
- n-acetylglucosamine-1-phosphate
- udp-glcnac
-
leloir
- glucose-1-phosphate
-
4-epimerase
- medicine
- drug development
- diagnostics
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
galactose 1-phosphate uridylyltransferase, galactose-1-phosphate uridyl transferase, galactose-1-phosphate uridyl trensferase, galactose-1-phosphate uridyltransferase, galactose-1-phosphate uridylyltransferase, galactose-1-phosphate:uridyltransferase, GALT, GALT enzyme, GalT1, GalT2, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
galactose 1-phosphate uridylyltransferase
galactose-1-phosphate uridylyltransferase
GALT
GalT1
GalT2
hexose 1-phosphate uridyltransferase
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hexose 1-phosphate uridylyltransferase
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-
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hexose-1-phosphate uridylyltransferase
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UDPGlc:Gal-1-P uridylyltransferase
UDPglucose-hexose-1-phosphate uridylyltransferase
UDPglucose:alpha-D-galactose-1-phosphate uridylyltransferase
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uridine diphosphoglucose:alpha-D-galactose-1-phosphate uridilyltransferase
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uridyl transferase
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uridyltransferase
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uridylyltransferase, hexose 1-phosphate
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GALT
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
double-displacement mechanism
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UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
SH-group in the active site
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UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
double-displacement mechanism; ping pong bi bi kinetic model
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UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
mutant H166G, random equilibrium, intrinsically ordered substrate binding mechanism, ping pong kinetics
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UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
reaction mechanism of Duarte mutant N314D
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UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
mechanism, modeling
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UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
active site nucleophil H166; amino acid residues of both subunits contribute to the active site
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UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
double-displacement mechanism; formation of a stable nucleotidylated histidine intermediate; Gln168 engages hydrogen bonding with the phosphoryl oxygen of the UMP moiety in the covalently formed reaction intermediate UMP-enzyme, UMP is bound to His166; mechanism model
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UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
Pro185 has a critical role in facilitating the transferase reaction
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UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
Pro185 has a critical role in facilitating the transferase reaction
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UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
Gln168 engages hydrogen bonding with the phosphoryl oxygen of the UMP moiety in the covalently formed reaction intermediate UMP-enzyme, UMP is bound to His166
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UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
active site triad: His164, His165, and His166, with His166 as nulceophilic catalyst, highly conserved; double-displacement mechanism
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UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
active site structure, enzyme complexed with UDP-galactose; double-displacement mechanism
UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
active site: C160SNPHP165; active site nucleophil H166; active site structure, enzyme complexed with UDP-galactose; active site triad: His164, His165, and His166, with His166 as nulceophilic catalyst, highly conserved; formation of a stable nucleotidylated histidine intermediate; Gln168 engages hydrogen bonding with the phosphoryl oxygen of the UMP moiety in the covalently formed reaction intermediate UMP-enzyme, UMP is bound to His166; ping pong bi bi kinetic model
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UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
active site nucleophil H166
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UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
ping-pong catalytic mechanism, overview. A UMP group is transferred from UDP-glucose to His166 in the active site of the enzyme
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UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
ping-pong catalytic mechanism, a UMP group is transferred from UDP-glucose to His186 in the active site of the enzyme, overview
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UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleotidyl group transfer
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
UDP-glucose:alpha-D-galactose-1-phosphate uridylyltransferase
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CAS REGISTRY NUMBER
COMMENTARY
9026-21-5
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate
UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
UDP-alpha-D-glucose + N-acetyl-alpha-D-galactosamine 1-phosphate
alpha-D-glucose 1-phosphate + UDP-N-acetyl-alpha-D-galactosamine
UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosamine 1-phosphate
alpha-D-glucose 1-phosphate + UDP-N-acetyl-alpha-D-glucosamine
UDP-alphaS-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-alphaS-galactose
UDP-glucose + 2-methylimidazole
uridine 5'-phospho-2-methylimidazole + alpha-D-glucose 1-phosphate
UDP-glucose + 4-methylimidazole
uridine 5'-phospho-4-methylimidazole + alpha-D-glucose 1-phosphate
UDP-glucose + D-galactose 1-phosphate
D-glucose 1-phosphate + UDP-galactose
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-
-
-
?
uridine 5'-phospho-2,4,5-trimethylimidazole + alpha-D-glucose 1-phosphate
UDP-glucose + 2,4,5-trimethylimidazole
uridine 5'-phospho-2-methylimidazole + alpha-D-glucose 1-phosphate
UDP-glucose + 2-methylimidazole
uridine 5'-phospho-3-methylimidazole + alpha-D-glucose 1-phosphate
UDP-glucose + 3-methylimidazole
uridine 5'-phospho-4-methylimidazole + alpha-D-glucose 1-phosphate
UDP-glucose + 4-methylimidazole
uridine 5'-phospho-5-methylimidazole + alpha-D-glucose 1-phosphate
UDP-glucose + 5-methylimidazole
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-alpha-D-galactose
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-
-
-
?
alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate
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-
-
-
r
alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate
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-
-
-
r
CDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + CDP-galactose
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no activity
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-
-
CDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + CDP-galactose
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low activity
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-
?
TDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + TDP-galactose
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reaction at 60% the rate of UDP-glucose
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r
TDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + TDP-galactose
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8.7% activity compared to UDP-glucose
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r
TDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + TDP-galactose
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no activity
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-
UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
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-
-
?
UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
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-
-
?
UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
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-
-
-
r
UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
-
-
-
-
r
UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
-
-
-
-
r
UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
-
-
-
-
r
UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
-
-
-
r
UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
-
-
-
r
UDP-alpha-D-glucose + N-acetyl-alpha-D-galactosamine 1-phosphate
alpha-D-glucose 1-phosphate + UDP-N-acetyl-alpha-D-galactosamine
-
-
-
?
UDP-alpha-D-glucose + N-acetyl-alpha-D-galactosamine 1-phosphate
alpha-D-glucose 1-phosphate + UDP-N-acetyl-alpha-D-galactosamine
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-
-
?
UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosamine 1-phosphate
alpha-D-glucose 1-phosphate + UDP-N-acetyl-alpha-D-glucosamine
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-
-
?
UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosamine 1-phosphate
alpha-D-glucose 1-phosphate + UDP-N-acetyl-alpha-D-glucosamine
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-
-
?
UDP-alphaS-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-alphaS-galactose
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stereochemistry: enzyme accepts (Rp)-UDP-alphaS-glucose converting it to (Rp)-UDP-alphaS-galactose, the overall retention of configuration arises from inversion in each of the two steps
(Rp1)-UDP-alphaS-galactose, i.e. uridine 5'-(1-thiodiphosphate) galactose
r
UDP-alphaS-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-alphaS-galactose
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i.e. uridine 5'-(1-thiodiphosphate) glucose
(Rp1)-UDP-alphaS-galactose, i.e. uridine 5'-(1-thiodiphosphate) galactose
r
UDP-alphaS-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-alphaS-galactose
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(Rp1)-UDP-alphaS-glucose
(Rp1)-UDP-alphaS-galactose, i.e. uridine 5'-(1-thiodiphosphate) galactose
r
UDP-glucose + 2-methylimidazole
uridine 5'-phospho-2-methylimidazole + alpha-D-glucose 1-phosphate
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kinetic study
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r
UDP-glucose + 2-methylimidazole
uridine 5'-phospho-2-methylimidazole + alpha-D-glucose 1-phosphate
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mutant H166G, i.e. UDP-hexose synthase
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r
UDP-glucose + 4-methylimidazole
uridine 5'-phospho-4-methylimidazole + alpha-D-glucose 1-phosphate
-
kinetic study
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r
UDP-glucose + 4-methylimidazole
uridine 5'-phospho-4-methylimidazole + alpha-D-glucose 1-phosphate
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mutant H166G, i.e. UDP-hexose synthase
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r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
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highly specific for the substrates
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r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
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involved in conversion of galactose into alpha-D-glucose 1-phosphate, Leloir pathway
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r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
important step in galactose metabolism
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-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
central enzyme in the classical Lelior pathway, but not in galactose metabolsim
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r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
stereochemistry: enzyme accepts (Rp)-UDP-alphaS-glucose converting it to (Rp)-UDP-alphaS-galactose, the overall retention of configuration arises from inversion in each of the two steps
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
formation of a covalent uridylyl-enzyme intermediate, i.e. UMP-enzyme
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
formation of a covalent uridylyl-enzyme intermediate, i.e. UMP-enzyme
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
formation of a covalent uridylyl-enzyme intermediate, i.e. UMP-enzyme
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
highly specific for the substrates
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
recombinant bifunctional chimeric fusion protein
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r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
2nd step of Leloir pathway
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
involved in conversion of galactose into alpha-D-glucose 1-phosphate, Leloir pathway
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
highly specific for the substrates
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
involved in conversion of galactose into alpha-D-glucose 1-phosphate, Leloir pathway
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
2-step mechanism
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
galactosemia with altered activity of the follicle-stimulating hormone FSH
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
important step in galactose metabolism
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
essential enzyme in galactose metabolism, deficiency causes genetic disorder galactosemia, e.g. mutant Duarte variant
-
-
-
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
essential enzyme in galactose metabolism, deficiency causes genetic disorder galactosemia, e.g. mutant Duarte variant
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
essential enzyme in galactose metabolism, deficiency causes genetic disorder galactosemia, e.g. mutant Duarte variant
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
essential enzyme in galactose metabolism, deficiency causes genetic disorder galactosemia, e.g. mutant Duarte variant
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
essential enzyme in galactose metabolism, deficiency causes genetic disorder galactosemia, e.g. mutant Duarte variant
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
2nd step of Leloir pathway
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
2nd step of Leloir pathway
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
involved in the biosynthesis of follicle-stimulating hormone FSH
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
transcriptional regulation is complex and not directly induced by substrate levels
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
2nd step of Leloir pathway
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + imidazole
uridine 5'-phosphoimidazole + alpha-D-glucose 1-phosphate
-
wild-type, 800fold reduced activity compared to normal reaction intermediate uridylyl-enzyme as substrate, pH-dependent
-
r
UDP-glucose + imidazole
uridine 5'-phosphoimidazole + alpha-D-glucose 1-phosphate
-
mutant H166A
-
r
UDP-glucose + imidazole
uridine 5'-phosphoimidazole + alpha-D-glucose 1-phosphate
-
mutant H166G, i.e. UDP-hexose synthase
-
r
UDP-glucose + imidazole
uridine 5'-phosphoimidazole + alpha-D-glucose 1-phosphate
-
mutant H166G, i.e. UDP-hexose synthase
-
r
UDP-glucose + imidazole
uridine 5'-phosphoimidazole + alpha-D-glucose 1-phosphate
-
equilibrium study and constants
-
r
UDP-glucose + imidazole
uridine 5'-phosphoimidazole + alpha-D-glucose 1-phosphate
-
equilibrium study and constants
-
r
uridine 5'-phospho-2,4,5-trimethylimidazole + alpha-D-glucose 1-phosphate
UDP-glucose + 2,4,5-trimethylimidazole
-
kinetic study
-
r
uridine 5'-phospho-2,4,5-trimethylimidazole + alpha-D-glucose 1-phosphate
UDP-glucose + 2,4,5-trimethylimidazole
-
mutant H166G, i.e. UDP-hexose synthase
-
r
uridine 5'-phospho-2-methylimidazole + alpha-D-glucose 1-phosphate
UDP-glucose + 2-methylimidazole
-
kinetic study
-
r
uridine 5'-phospho-2-methylimidazole + alpha-D-glucose 1-phosphate
UDP-glucose + 2-methylimidazole
-
mutant H166G, i.e. UDP-hexose synthase
-
r
uridine 5'-phospho-3-methylimidazole + alpha-D-glucose 1-phosphate
UDP-glucose + 3-methylimidazole
-
kinetic study
-
r
uridine 5'-phospho-3-methylimidazole + alpha-D-glucose 1-phosphate
UDP-glucose + 3-methylimidazole
-
mutant H166G, i.e. UDP-hexose synthase
-
r
uridine 5'-phospho-4-methylimidazole + alpha-D-glucose 1-phosphate
UDP-glucose + 4-methylimidazole
-
kinetic study
-
r
uridine 5'-phospho-4-methylimidazole + alpha-D-glucose 1-phosphate
UDP-glucose + 4-methylimidazole
-
mutant H166G, i.e. UDP-hexose synthase
-
r
uridine 5'-phospho-5-methylimidazole + alpha-D-glucose 1-phosphate
UDP-glucose + 5-methylimidazole
-
kinetic study
-
r
uridine 5'-phospho-5-methylimidazole + alpha-D-glucose 1-phosphate
UDP-glucose + 5-methylimidazole
-
mutant H166G, i.e. UDP-hexose synthase
-
r
additional information
?
-
-
no activity with ADP-glucose or GDP-glucose
-
-
-
additional information
?
-
-
no substrates: N-acetyl-alpha-D-galactose 1-phosphate, N-acetyl-alpha-D-glucose 1-phosphate
-
-
-
additional information
?
-
no substrates: N-acetyl-alpha-D-galactose 1-phosphate, N-acetyl-alpha-D-glucose 1-phosphate
-
-
-
additional information
?
-
no substrates: N-acetyl-alpha-D-galactose 1-phosphate, N-acetyl-alpha-D-glucose 1-phosphate
-
-
-
additional information
?
-
no substrates: N-acetyl-alpha-D-galactose 1-phosphate, N-acetyl-alpha-D-glucose 1-phosphate
-
-
-
additional information
?
-
no substrates: N-acetyl-alpha-D-galactose 1-phosphate, N-acetyl-alpha-D-glucose 1-phosphate
-
-
-
additional information
?
-
-
no activity with fructose 1-phosphate and galactose 6-phosphate
-
-
-
additional information
?
-
-
no activity with xylose 1-phosphate, and IDP-glucose
-
-
-
additional information
?
-
-
no activity with fructose 1-phosphate and galactose 6-phosphate
-
-
-
additional information
?
-
-
no activity with ADP-glucose or GDP-glucose
-
-
-
additional information
?
-
-
no activity with ribose 1-phosphate and mannose 6-phosphate
-
-
-
additional information
?
-
-
the enzyme has a strict requirement for UDP-glucose or UDP-galactose as substrates, while GDP-glucose, ADP-glucose, TDP-glucose, CDP-glucose, UDPxylose, and UDP-mannose are all unable to support activity
-
-
-
additional information
?
-
-
no activity with UDP-xylose, ADP-glucose, and galactose 6-phosphate
-
-
-
additional information
?
-
-
inverse relationship between enzyme activity and galactose sensitivity
-
-
-
additional information
?
-
-
the enzyme has a strict requirement for UDP-glucose or UDP-galactose as substrates, while GDP-glucose, ADP-glucose, TDP-glucose, CDP-glucose, UDPxylose, and UDP-mannose are all unable to support activity
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
UTP + alpha-D-galactose 1-phosphate
diphosphate + UDP-alpha-D-galactose
-
-
-
-
?
UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
-
-
-
-
r
UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
-
-
-
-
r
UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
-
-
-
-
r
UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
-
-
-
-
r
UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
Q8ZXN7
-
-
-
r
UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
Q8ZXN7
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
involved in conversion of galactose into alpha-D-glucose 1-phosphate, Leloir pathway
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
important step in galactose metabolism
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
central enzyme in the classical Lelior pathway, but not in galactose metabolsim
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
2nd step of Leloir pathway
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
involved in conversion of galactose into alpha-D-glucose 1-phosphate, Leloir pathway
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
involved in conversion of galactose into alpha-D-glucose 1-phosphate, Leloir pathway
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
galactosemia with altered activity of the follicle-stimulating hormone FSH
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
important step in galactose metabolism
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
essential enzyme in galactose metabolism, deficiency causes genetic disorder galactosemia, e.g. mutant Duarte variant
-
-
-
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
essential enzyme in galactose metabolism, deficiency causes genetic disorder galactosemia, e.g. mutant Duarte variant
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
essential enzyme in galactose metabolism, deficiency causes genetic disorder galactosemia, e.g. mutant Duarte variant
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
essential enzyme in galactose metabolism, deficiency causes genetic disorder galactosemia, e.g. mutant Duarte variant
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
essential enzyme in galactose metabolism, deficiency causes genetic disorder galactosemia, e.g. mutant Duarte variant
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
2nd step of Leloir pathway
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
2nd step of Leloir pathway
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
involved in the biosynthesis of follicle-stimulating hormone FSH
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
Q03249
transcriptional regulation is complex and not directly induced by substrate levels
-
-
r
UDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-galactose
-
2nd step of Leloir pathway
-
r
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Zn2+
additional information
Fe2+
-
contains 0.67 mol per mol of wild-type enzyme, 0.59 mol per mol of mutant H166A enzyme, and 0.7-0.76 mol per mol of mutant H166G enzyme
Fe2+
-
contains 0.67 mol per mol of wild-type enzyme subunit, 0.44 mol per mol of mutant Q168R subunit; required
Fe2+
-
0.7 mol per mol of subunit; coordinated in a square pyramidal geometry with His296, His298, and Glu182 in a bidentate coordination providing the base ligands and His281 providing the axial ligand; not essential
Fe2+
0.7 mol per mol of subunit; mutant C160A: 0.5 mol per mol of subunit, mutant S161A: 0.4 mol per mol of subunit
Fe2+
-
can be replaced by other metal ions; coordinated in a square pyramidal geometry with His296, His298, and Glu182 in a bidentate coordination providing the base ligands and His281 providing the axial ligand; not essential
Fe2+
-
the enzyme homodimer contains one zinc (II) and one iron (II) ion per subunit, pyramidial iron-binding site, structure, overview
Fe2+
-
the iron-binding site involves residues H338, H360, H360 and G229
Zn2+
-
contains 1.21 mol per mol of wild-type enzyme, 1.33 mol per mol of mutant H166A enzyme, and 0.99-1.16 mol per mol of mutant H166G enzyme
Zn2+
-
0.91 mol per mol of mutant Q168R subunit; 1.2 mol tightly bound per mol of subunit; required
Zn2+
-
1.2 mol tightly bound per mol of subunit; coordinated in a tetrahedral geometry by Cys52, Cys55, His115, and His164; required
Zn2+
1.2 mol tightly bound per mol of subunit; mutant C160A: 1.3 mol per mol of subunit, mutant S161A: 1.2 mol per mol of subunit like the wild-type
Zn2+
-
can be replaced by other metal ions; coordinated in a tetrahedral geometry by Cys52, Cys55, His115, and His164; required
Zn2+
-
the enzyme homodimer contains one zinc (II) and one iron (II) ion per subunit, tetrahedral zinc binding site, structure, overview
Zn2+
-
the zinc co-orientating residues are not conserved and therefore, it may only bind one metal ion per monomer
additional information
-
enzyme contains no Ca, Cd, Cu, Mo, Ni, Co, Mn, As, Pb, or Se
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
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
alpha-D-galactose 1-phosphate
-
competitive substrate inhibition in the forward reaction
alpha-D-galactose 1-phosphate
-
substrate inhibition at concentrations above 1.5 mM
alpha-D-galactose 1-phosphate
-
competitive substrate inhibition in the forward reaction
D-galactose
-
wild-type and mutants, inverse relationship between enzyme activity and galactose sensitivity
D-galactose
-
galactosemia, disease caused by genetic disorder, is characterized by a galactose sensitivity
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-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
-
at high concentrations, wild-type and mutants F171L and F171S, not F171Y
additional information
-
product inhibition study, wild-type and mutants H166G and H166A
-
additional information
-
no inhibition by NADH, NAD+, sodium diphosphate
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-galactose
-
galactose growth medium induces enzyme activity, not expression, and increases Vmax by about 50% compared to glucose medium
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Carcinoma, Ovarian Epithelial
Galactose-1-phosphate uridyl transferase (GALT) genotype and phenotype, galactose consumption, and the risk of borderline and invasive ovarian cancer (United States).
Cataract
Association of presenile cataract with galactose-1-phosphate uridyl transferase gene mutations.
Cataract
[Activity of enzymes of galactose metabolism in so-called congenital cataract (author's transl)]
Congenital Disorders of Glycosylation
Hypoglycosylation with increased fucosylation and branching of serum transferrin N-glycans in untreated galactosemia.
Congenital, Hereditary, and Neonatal Diseases and Abnormalities
Hypoglycosylation with increased fucosylation and branching of serum transferrin N-glycans in untreated galactosemia.
Craniosynostoses
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.
Endometriosis
Mutation of galactose-1-phosphate uridyl transferase and its association with ovarian cancer and endometriosis.
Fanconi Syndrome
Defective galactose oxidation in a patient with glycogen storage disease and Fanconi syndrome.
galactokinase deficiency
Biokinetics of galactose in the homozygotes and heterozygotes of both forms of galactosemia.
galactokinase deficiency
Hemoglobin A1 in galactosemia, a possible role in monitoring dietary compliance.
galactokinase deficiency
Recommendations for newborn screening for galactokinase deficiency: A systematic review and evaluation of Dutch newborn screening data.
galactokinase deficiency
Simultaneous quantitative estimation of galactose-1-phosphate and galactose in blood for the diagnosis of galactosemia.
Galactosemias
A Case of Classical Galactosemia: Identification and Characterization of 3 Distinct Mutations in Galactose-1-Phosphate Uridyl Transferase (GALT) Gene in a Single Family.
Galactosemias
A De Novo Variant in Galactose-1-P Uridylyltransferase (GALT) Leading to Classic Galactosemia.
Galactosemias
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.
Galactosemias
Analysis of common mutations in the galactose-1-phosphate uridyl transferase gene: new assays to increase the sensitivity and specificity of newborn screening for galactosemia.
Galactosemias
Biokinetics of galactose in the homozygotes and heterozygotes of both forms of galactosemia.
Galactosemias
Clinical significance of plasma galactose and erythrocyte galactose-1-phosphate measurements in transferase-deficient galactosemia and in individuals with below-normal transferase activity.
Galactosemias
Duarte (DG) galactosemia: a pilot study of biochemical and neurodevelopmental assessment in children detected by newborn screening.
Galactosemias
Hemoglobin A1 in galactosemia, a possible role in monitoring dietary compliance.
Galactosemias
Heterozygosity for the classical galactosemia mutation does not affect ovarian reserve and menopausal age.
Galactosemias
Hypoglycosylation with increased fucosylation and branching of serum transferrin N-glycans in untreated galactosemia.
Galactosemias
Isoelectrofocusing of erythrocyte galactose 1 phospho uridyl transferase in a family with both galactosemia and Duarte variants.
Galactosemias
Neonatal screening for galactosemia by quantitative analysis of hexose monophosphates using tandem mass spectrometry: a retrospective study.
Galactosemias
Prenatal diagnosis of galactosemia and properties of galactose-1-phosphate uridyltransferase in erythrocytes of galactosemic variants as well as in human fetal and adult organs.
Galactosemias
Problems in the diagnosis of transferase and galactokinase deficient galactosemia.
Galactosemias
Quantification of galactose-1-phosphate uridyltransferase enzyme activity by liquid chromatography-tandem mass spectrometry.
Galactosemias
Recommendations for newborn screening for galactokinase deficiency: A systematic review and evaluation of Dutch newborn screening data.
Galactosemias
Simultaneous quantitative estimation of galactose-1-phosphate and galactose in blood for the diagnosis of galactosemia.
Galactosemias
The ability of an LC-MS/MS-based erythrocyte GALT enzyme assay to predict the phenotype in subjects with GALT deficiency.
Galactosemias
The molecular relationship between deficient UDP-galactose uridyl transferase (GALT) and ceramide galactosyltransferase (CGT) enzyme function: a possible cause for poor long-term prognosis in classic galactosemia.
Galactosemias
[Association of thrombopenia due to platelet alloimmunization with galactosemia in the neonatal period]
Galactosemias
[Effectiveness of the screening programme for galactosemia. New strategy in Poland]
Hepatomegaly
Negative screening tests in classical galactosaemia caused by S135L homozygosity.
Neoplasms
Mouse monoclonal antibodies which recognize a human (beta 1-4)galactosyl-transferase associated with tumor in body fluids.
Ovarian Neoplasms
Mutation of galactose-1-phosphate uridyl transferase and its association with ovarian cancer and endometriosis.
Primary Ovarian Insufficiency
Heterozygosity for the classical galactosemia mutation does not affect ovarian reserve and menopausal age.
Tuberculosis
Identification of amino acids involved in catalytic process of M. tuberculosis GlmU acetyltransferase.
Tuberculosis
Mycobacterium tuberculosis AtsG (Rv0296c), GlmU (Rv1018c) and SahH (Rv3248c) Proteins Function as the Human IL-8-Binding Effectors and Contribute to Pathogen Entry into Human Neutrophils.
udp-glucose-hexose-1-phosphate uridylyltransferase deficiency
Diagnosis and management of galactosemia: an Egyptian experience.
udp-glucose-hexose-1-phosphate uridylyltransferase deficiency
Duarte (DG) galactosemia: a pilot study of biochemical and neurodevelopmental assessment in children detected by newborn screening.
udp-glucose-hexose-1-phosphate uridylyltransferase deficiency
Functional analysis of GALT variants found in classic galactosemia patients using a novel cell-free translation method.
udp-glucose-hexose-1-phosphate uridylyltransferase deficiency
Galactose-1 phosphate uridyl transferase deficiency in the western grey kangaroo (Macropus fuliginosus; marsupialia): a model system for gene therapy studies.
udp-glucose-hexose-1-phosphate uridylyltransferase deficiency
GALT Deficiency Galactosemia.
udp-glucose-hexose-1-phosphate uridylyltransferase deficiency
Hemoglobin A1 in galactosemia, a possible role in monitoring dietary compliance.
udp-glucose-hexose-1-phosphate uridylyltransferase deficiency
[Efficacy of dietetic treatment in a case of galactosemia diagnosed late]
udp-glucose-hexose-1-phosphate uridylyltransferase deficiency
[The frequency of uridyl transferase deficiency in patients with galactose intolerance]
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.125
alpha-D-galactose 1-phosphate
recombinant mutant C160A, pH 8.5, 27°C
0.125
alpha-D-galactose 1-phosphate
-
recombinant mutant C160A, pH 8.5, 27°C
0.223
alpha-D-galactose 1-phosphate
recombinant mutant S161A, pH 8.5, 27°C
0.223
alpha-D-galactose 1-phosphate
-
recombinant mutant S161A, pH 8.5, 27°C
0.29
alpha-D-galactose 1-phosphate
-
purified recombinant bifunctional chimeric fusion protein, pH 8.5, 27°C
0.3
alpha-D-galactose 1-phosphate
recombinant wild-type, pH 8.5, 27°C
0.3
alpha-D-galactose 1-phosphate
-
recombinant mutant Q168N, pH 8.5, 27°C; recombinant wild-type, pH 8.5, 27°C
0.14
alpha-D-glucose 1-phosphate
recombinant mutant C160A, pH 8.5, 27°C
0.2
alpha-D-glucose 1-phosphate
recombinant mutant S161A, pH 8.5, 27°C
0.08
UDP-glucose
-
purified recombinant bifunctional chimeric fusion protein, pH 8.5, 27°C
0.2
UDP-glucose
-
recombinant wild-type and mutants P185E and P185A, pH 8.7, 37°C
0.2
UDP-glucose
-
recombinant mutant Q168N, pH 8.5, 27°C; recombinant wild-type, pH 8.5, 27°C
additional information
additional information
-
kinetics; mutant H166A; mutant H166G
-
additional information
additional information
-
kinetics; wild-type and mutants in the 2-step reaction
-
additional information
additional information
-
kinetics; wild-type and mutants in the 2-step reaction
-
additional information
additional information
-
kinetics; wild-type and mutants in the 2-step reaction
-
additional information
additional information
-
kinetics; kinetics at 4°C, wild-type and mutants; wild-type and mutants in the 2-step reaction
-
additional information
additional information
kinetics at 4°C, wild-type and mutants
-
additional information
additional information
-
kinetics at 4°C, wild-type and mutants
-
additional information
additional information
-
steady-state kinetics of G, overview
-
additional information
additional information
-
kinetics forward and reverse reaction, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0533
alpha-D-galactose 1-phosphate
-
recombinant mutant S161A, forward reaction, pH 8.5, 27°C
19
alpha-D-galactose 1-phosphate
-
recombinant mutant Q168N, forward reaction, pH 8.5, 27°C
24
alpha-D-galactose 1-phosphate
-
purified recombinant bifunctional chimeric fusion protein, pH 8.5, 27°C
265
alpha-D-galactose 1-phosphate
-
recombinant mutant C160A, forward reaction, pH 8.5, 27°C
653
alpha-D-galactose 1-phosphate
-
recombinant mutant E182A, forward reaction, pH 8.5, 27°C
780
alpha-D-galactose 1-phosphate
-
recombinant wild-type, forward reaction, pH 8.5, 27°C
780
alpha-D-galactose 1-phosphate
recombinant wild-type, forward reaction, pH 8.5, 27°C
780
alpha-D-galactose 1-phosphate
-
recombinant wild-type, forward reaction, pH 8.5, 27°C
5.5
alpha-D-glucose 1-phosphate
-
mutant F194L, pH 8.8, 37°C; mutant R333G, pH 8.8, 37°C
0.0167
imidazole
-
mutant H166A, forward reaction with UDP-glucose, pH 8.5, 27°C
5.52
imidazole
-
mutant H166G, forward reaction with UDP-glucose, pH 8.5, 27°C
0.0967
UDP-galactose
-
recombinant mutant S161A, reverse reaction, pH 8.5, 27°C
177
UDP-galactose
-
recombinant mutant E182A, reverse reaction, pH 8.5, 27°C
283
UDP-galactose
recombinant wild-type, reverse reaction, pH 8.5, 27°C
0.0217
uridine 5'-phosphoimidazolate
-
mutant H166A, forward reaction with D-glucose 1-phosphate, pH 8.5, 27°C
13.5
uridine 5'-phosphoimidazolate
-
mutant H166G, forward reaction with D-glucose 1-phosphate, pH 8.5, 27°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
product/substrate inhibition pattern and kinetics
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00093
0.023
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
0.334
substrate N-acetyl-alpha-D-galactose 1-phosphate, pH 7.0, 37°C
9.9
14.9
16.3
79.5
180
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
8.5
8.7
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
LITERATURE
25
27
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
different isozymic pattern in cells grown in glucose, galactose or inosine media
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
Protein Data Base: 1HXQ, three-dimensional model of the Escherichia coli enzyme-UMP-crystal
SwissProt
brenda
-
642828, 642830, 642832, 642833, 642835, 642838, 642840, 642842, 642851, 642855, 642861, 642863, 673857, 703249, 722074, 722427
-
-
brenda
missense mutant N314D, Duarte allele; native galactosemic Q188R mutant; native galactosemic R333W mutant; native mutant F171S
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
derived from anterior pituitary gland gonadotropin-producing cells in different stages of the estrous cycle: proestrus, estrus, metestrus, and diestrus
brenda
additional information
-
expression level of the enzyme changes during the estrous cycle in the anterior pituitary gland
brenda
-
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
-
homology modeling of the three-dimensional protein structure, overview
malfunction
-
Duarte galactosemia results from partial impairment of galactose-1-phosphate uridylyltransferase
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 pivotal step in the Leloir pathway of galactose metabolism, overview
metabolism
-
the enzyme catalyzes a critical step in the Leloir pathway, overview
metabolism
-
the enzyme catalyzes a critical step in the Leloir pathway, overview
metabolism
-
galactose-1-phosphate uridylyltransferase is a key enzyme in the Leloir pathway, the main route for galactose metabolism in red algae
metabolism
-
the enzyme catalyzes a pivotal step in the Leloir pathway of galactose metabolism, overview
-
physiological function
-
UDPGal is an important substrate for agar synthesis in red alga
physiological function
A2AMS3
GalT-deficient mice exhibit a subfertility phenotype in adult females and growth restriction in both sexes. The growth potential and the protein levels of the Akt(Thr308), Akt(Ser473), pan-Akt, Pdk1, and Hsp90 proteins are significantly reduced by 62.5%, 60.3%, 66%, 66%, and 50%, respectively in GalT-deficient primary fibroblast cells. Reduced expression of phosphorylated Akt proteins in the mutant cells leads to diminished phosphorylation of Gsk-3b (-74%). Protein expression of BiP and pPten are 276% and 176% higher, respectively in cells with GalT-deficiency. The mRNA abundance of Akt1, Pdpk1, Hsp90aa1 and Pi3kca genes are significantly reduced at least 2.03-, 1.37-, 2.45-, and 1.78fold, respectively in mutant fibroblasts. Both serum-fasted normal and GalT-deficient cells respond to Igf-1-induced activation of Akt phosphorylation at +15 min, but the mutant cells have lower phosphorylation levels. The steady-state protein abundance of Igf-1 receptor is also significantly reduced in mutant cells
Show AA Sequence and Transmembrane Helices (11980 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Escherichia coli (strain K12)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
41000
80000
additional information
-
the recombinant chimeric fusion protein exists as monomer, dimer and tetramer, all are active
41000
-
2 * 41000, urea/mercaptoethanol treated and S-carboxymethylated enzyme, sedimentation equilibrium centrifugation in 5 M guanidine hydrochloride
41000
-
2 * 41000, urea/mercaptoethanol treated and S-carboxymethylated enzyme, sedimentation equilibrium centrifugation in 5 M guanidine hydrochloride
80000
-
recombinant bifunctional chimeric fusion protein, monomer, gel filtration
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
additional information
dimer
-
2 * 41000, urea/mercaptoethanol treated and S-carboxymethylated enzyme, sedimentation equilibrium centrifugation in 5 M guanidine hydrochloride
additional information
-
the recombinant chimeric fusion protein exists as monomer, dimer and tetramer, all are active
additional information
-
homology modeling of the three-dimensional protein structure, overview
additional information
-
a second band of MW 22 kDa is found in SDS-PAGE, which shows no enzyme activity
additional information
-
catalytically inactive subunits of mutants R333W and Q188R form normal homo- and heterodimers
additional information
-
modeling of the human enzyme structure onto the crystal structure of the Escherichia coli enzyme
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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
-
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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C160A
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
H166G
Q168N
Q168R
S161A
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
F171S
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
K285N
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
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
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
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
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
H166G
-
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
H166G
-
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; site-directed mutagenesis
Q168N
-
site-directed mutagenesis, 50fold reduced activity compared to wild-type, 40fold decreased kcat
Q168R
-
site-directed mutagenesis, 270000fold reduced activity compared to wild-type, i.e. nearly no remaining activity, mutant active sites can be uridylated by 65%, with very slow deuridylylation, compared to 100% for the wild-type, reduced metal content
Q168R
-
in humans galactosemia causing mutation, used as a model in bacterial system, 30000fold loss of activity, 28% reduced metal ion content; site-directed mutagenesis, 270000fold reduced activity compared to wild-type, i.e. nearly no remaining activity, mutant active sites can be uridylated by 65%, with very slow deuridylylation, compared to 100% for the wild-type, reduced metal content
S161A
site-directed mutagenesis, 7000fold reduced activity compared to wild-type
F171S
-
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
F171S
-
variant associated with type I galactosemia, residue is strictly conserved across species. No residual activity
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
N314D
-
native missense mutant Duarte D, homozygous, characteristic isoform, partial impairment of enzyme activity in human erythrocytes, fibroblasts, and transformed lymphoblasts, reduced Vmax, increased thermal lability
N314D
-
site-directed mutagenesis for construction of the naturally occuring mutation, unaltered activity, accumulation of alpha-D-galactose 1-phosphate, UDP-galactose and UDP-glucose
N314D/G1105C/G1391A
-
native Duarte-2 D2 variant, 40-50% activity compared to the wild-type
N314D/G1105C/G1391A
-
native Duarte-2 D2 variant with additional exchange of bases at 1323 G to A, 20-25% activity compared to wild-type, no clinical symptoms
Q188R
-
most common native mutation causing galactosemia in the white population; native mutant, no enzyme activity in vivo, galactosemia phenotype; site-directed mutagenesis for expression of the mutant in Escherichia coli, nearly no activity in vitro
Q188R
-
20-30% activity of wild-type activity as heterodimer with wild-type subunit, no activity as homodimer; native mutant, no enzyme activity in vivo, galactosemia phenotype
Q188R
-
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
-
variant associated with type I galactosemia, residue is strictly conserved across species. 0.6% of wild.type activtiy
R333W
-
20-30% activity of wild-type activity as heterodimer with wild-type subunit, no activity as homodimer; native mutant, catalytically inactive, galactosemic phenotype
R333W
-
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
S135L
-
native mutant, can be found in about 50% of galactosemia patients of African-American descent, 10fold reduced enzyme activity compared to wild-type, no steric or electrochemical changes sufficiently close to the active site to result in partial impairment of the reaction
S135L
-
site-directed mutagenesis for construction of the naturally occuring mutation, 2.7% of wild-type activity, accumulation of alpha-D-galactose 1-phosphate, UDP-galactose and UDP-glucose
additional information
-
construction and expression of bifunctional fusion protein composed of galactose-2-phosphate uridylyltransferase and UDP-galactose 4-epimerase with an intervening linker of 3 Ala residues, 20% increased Vmax compared to a mixture of the single enzymes
additional information
introduction of Asn and Arg at residue 188, normally Gln, in a three-dimensional model of the Escherichia coli enzyme-UMP-crystal
additional information
-
Munich2 mutant with base exchange at 2252 G to T, 20-25% activity compared to wild-type, no clinical symptoms; native Schönstadt mutant with base exchange at 897 G to C, 15-20% activity compared to wild-type, some clinical symptoms
additional information
-
coexpression of wild-type and/or mutant subunits in yeast, study of dimer formation pattern and subunit assortment, mutations: S135L, F171S, F171W, H186G, Q188R, N314D, R333W, overview
additional information
-
characterization of a large deletion spanning 8489 bp in the GALT gene accounting for the majority of disease alleles in Cypriot patients with classic galactosemia
additional information
construction of transgenic mice expressing a luciferase transgene under control of a 1.9 kb fragment of the UDP-glucose-hexose-1-phosphate uridylyltransferase promotor region , activity is found in most tissues with higher than expected reporter levels in neonatal brain
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
additional information
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
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freeze-thawing inactivates purified enzyme
freezing of dilute enzyme solution inactivates, concentration procedures lead to considerable loss of activity
-
purified enzyme has tendency to undergo transition to a lower specific activity form
-
sulfhydryl reagents restore activity of partially denatured enzyme and protect against inactivation
-
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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
-
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
-
4°C, in 0.01 M potassium phosphate buffer, pH 7.5, inactivation within 2 weeks, 2-mercaptoethanol, DTT and 20% glycerol slightly stabilize
-
metal ions or/and substrates do not protect from oxidation or proteolysis during prolonged storage
-
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
4190fold; placental enzyme to homogeneity, coelutes with a 67 kDa glycoprotein
-
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 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 from overexpressing strain BL21(DE3); recombinant wild-type and mutants Q168R and Q168N
-
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 wild-type and mutants from strain BL21(DE3)pLysS to near homogeneity
-
to homogeneity
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
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 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 wild-type and mutants as His-tagged proteins in Escherichia coli Bl21(DE3)
-
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 of wild-type and mutant S135L as His-tagged proteins, 2fold lower expression than the wild-type, in a null-background yeast
-
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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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
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
medicine
-
identification of six likely pathogenic variations including three missense (Ala101Asp, Tyr165His, and Pro257Thr), one small deletion/insertion [c.826_827delinsAA (Ala276Asn)], one frameshift (Asn96Serfs*5), and one splicing (c.378-1G > C) in patients with classic galactosemia. The most frequent variation is the Duarte variant (c.940A > G, 35.3%), followed by c.507G > C (p.Gln169His, 9.6%), among 34 Korean patients
medicine
-
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
medicine
-
characterization of a large deletion spanning 8489 bp in the GALT gene accounting for the majority of disease alleles in Cypriot patients with classic galactosemia. The deletion eliminates all GALT exons as well as the non-translated sequences of the adjacent interleukin 11 receptor IL11RA gene. It is flanked by a 6 bp block of homologous sequence on either side. Patients homozygous for the deletion show a lack of IL11RA transcripts
medicine
-
not all pathogenic GALT mutations are inherited and GALT may have a higher new mutation rate than previously believed. The variant Q188P 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
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fukasawa, T.; Segawa, T.; Nogi, Y.
Uridine diphosphate glucose-4-epimerase and galactose-1-phosphate uridylyltransferase from Saccharomyces cerevisiae
Methods Enzymol.
89
584-592
1982
Saccharomyces cerevisiae 106-3D, Saccharomyces cerevisiae
brenda
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
brenda
Feusi, M.E.S.; Burton, J.D.; Williamson, J.D.; Pharr, D.M.
Galactosyl-sucrose metabolism and UDP-galactose pyrophosphorylase from Cucumis melo L. fruit
Physiol. Plant.
106
9-16
1999
Cucumis melo, Glycine max
-
brenda
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
brenda
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
brenda
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
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Escherichia coli
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Bifidobacterium bifidum
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Bos taurus, Homo sapiens
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Purification, properties, and isozyme pattern of galactose-1-phosphate uridyl transferase from calf liver
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Bos taurus
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Helmer, G.R.; Williams, V.P.
Purification of galactose-1-phosphate uridylyltransferase from human placenta
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210
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1981
Homo sapiens
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Williams, V.P.; Helmer, G.R.; Fried, C.
Human galactose-1-phosphate uridylyltransferase: purification and comparison of the red blood cell and placental enzymes
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216
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Homo sapiens
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Williams, V.P.
Purification and some properties of galactose 1-phosphate uridylyltransferase from human red cells
Arch. Biochem. Biophys.
191
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1978
Homo sapiens
brenda
Kelly, S.; Sweeney, P.; Schedlbauer, L.
Galactose-l-phosphate uridyl transferase activity in red cells of various animal species
Experientia
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550-553
1981
Bos taurus, Capra hircus, Cavia porcellus, Cavia porcellus Hartley, Chlorocebus aethiops, Equus caballus, Homo sapiens, Oryctolagus cuniculus, Ovis aries, Rattus norvegicus
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Chowdhury, R.R.
Purification & some properties of galactose-1-phosphate uridylyl transferase from E. coli
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1979
Escherichia coli
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Ellis, G.; Goldberg, D.M.
Galactose-1-phosphate uridylytransferase. UDPglucose:alpha-D-galactose-1-phosphate uridylyltransferase, EC 2.7.7.12
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1983
Bos taurus, Homo sapiens
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Banroques, J.; Gregori, C.; Schapira, F.
Purification and characterization of human erythrocyte uridylyl transferase
Biochim. Biophys. Acta
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1981
Homo sapiens
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Frey, P.A.; Wong, L.J.; Sheu, K.F.; Yang, S.L.
Galactose-1-phosphate uridylyltransferase: detection, isolation, and characterization of the uridylyl enzyme
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1982
Escherichia coli, Homo sapiens, Saccharomyces cerevisiae
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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
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1996
Escherichia coli
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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
brenda
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
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1996
Homo sapiens
brenda
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
brenda
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
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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.
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28-38
1998
Homo sapiens
brenda
Lai, K.; Willis, A.C.; Elsas, L.J.
The biochemical role of glutamine 188 in human galactose-1-phosphate uridyltransferase
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274
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1999
Escherichia coli (P09148), Homo sapiens
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Leslie, N.D.; Bai, S.
Functional analysis of the mouse galactose-1-phosphate uridyl transferase (GALT)promoter
Mol. Genet. Metab.
72
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2001
Mus musculus (Q03249)
brenda
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)
brenda
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)
brenda
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
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1994
Homo sapiens
brenda
Gross, W.; Schnarrenberger, C.
Purification and characterization of a galactose-1-phosphate: UDP-glucose uridyltransferase from the red alga Galdieria sulphuraria
Eur. J. Biochem.
234
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1995
Galdieria sulphuraria
brenda
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
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1995
Escherichia coli
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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
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1999
Homo sapiens
brenda
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
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1996
Escherichia coli, Homo sapiens
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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
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1996
Homo sapiens
brenda
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
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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)
brenda
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
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275
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2000
Homo sapiens
brenda
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)
brenda
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
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2001
Homo sapiens
brenda
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
brenda
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
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2002
Escherichia coli, Homo sapiens
brenda
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
brenda
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)
brenda
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
brenda
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)
brenda
Satomura, T.; Hiraki, A.; Kawai, T.; Kawakami, R.; Ohshima, T.; Sakuraba, H.
Expression, purification, crystallization and preliminary X-ray diffraction analysis of a galactose 1-phosphate uridylyltransferase from the hyperthermophilic archaeon Pyrobaculum aerophilum
Acta Crystallogr. Sect. F
68
330-332
2012
Pyrobaculum aerophilum (Q8ZXN7), Pyrobaculum aerophilum DSM 7523 (Q8ZXN7)
brenda
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
brenda
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
brenda
Li, M.; Sui, Z.; Kang, K.; Zhang, X.; Zhu, M.; Yan, B.
Cloning and analysis of the galactose-1-phosphate uridylyltransferase (galt) gene of Gracilariopsis lemaneiformis (Rhodophyta) and correlation between gene expression and agar synthesis
J. Appl. Phycol.
22
157-164
2010
Gracilariopsis lemaneiformis
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brenda
Siow, R.; Teo, S.; Ho, W.; Shukor, M.; Phang, S.; Ho, C.
Molecular cloning and biochemical characterization of galactose-1-phosphate uridylyltransferase from Gracilaria changii (Rhodophyta)
J. Phycol.
48
155-162
2012
Gracilaria changii
brenda
De Bruyn, F.; Beauprez, J.; Maertens, J.; Soetaert, W.; De Mey, M.
Unraveling the Leloir pathway of Bifidobacterium bifidum: significance of the uridylyltransferases
Appl. Environ. Microbiol.
79
7028-7035
2013
Bifidobacterium bifidum, Bifidobacterium bifidum (M4M7K7), Bifidobacterium bifidum (M4MCS2), Bifidobacterium bifidum PRL2010 (M4M7K7), Bifidobacterium bifidum PRL2010 (M4MCS2)
brenda
Balakrishnan, B.; Chen, W.; Tang, M.; Huang, X.; Cakici, D.D.; Siddiqi, A.; Berry, G.; Lai, K.
Galactose-1 phosphate uridylyltransferase (GalT) gene: A novel positive regulator of the PI3K/Akt signaling pathway in mouse fibroblasts
Biochem. Biophys. Res. Commun.
470
205-212
2016
Mus musculus (A2AMS3)
brenda
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)
brenda
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, Homo sapiens (P07902)
brenda
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)
brenda
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, Homo sapiens (P07902)
brenda
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, Homo sapiens (P07902)
brenda
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