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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
- udp-glcnac
- n-acetylglucosamine-1-phosphate
-
4-epimerase
-
leloir
-
glucosamine-1-phosphate
- medicine
-
galactose-restricted
-
uridylylated
- drug development
- diagnostics
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
galactose 1-phosphate uridylyltransferase, galactose-1-phosphate uridyl transferase, galactose-1-phosphate uridyltransferase, galactose-1-phosphate uridylyltransferase, galactose-1-phosphate:uridyltransferase, GALT, GALT enzyme, GalT1, GalT2, hexose 1-phosphate uridyltransferase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
galactose 1-phosphate uridylyltransferase
galactose-1-phosphate uridyl transferase
galactose-1-phosphate uridyltransferase
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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-
-
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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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-
-
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uridine diphosphoglucose:alpha-D-galactose-1-phosphate uridilyltransferase
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uridyl transferase
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-
-
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uridyltransferase
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-
-
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uridylyltransferase, hexose 1-phosphate
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-
-
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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
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
-
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
UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
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
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
double-displacement mechanism
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
mutant H166G, random equilibrium, intrinsically ordered substrate binding mechanism, ping pong kinetics
-
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
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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
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
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
active site nucleophil H166
UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
formation of a stable nucleotidylated histidine intermediate
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UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
formation of a stable nucleotidylated histidine intermediate
UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
amino acid residues of both subunits contribute to the active site
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
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: C160SNPHP165
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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
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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
UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
mechanism model
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
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
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
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleotidyl group transfer
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-
-
-
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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
-
-
-
-
?
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
-
-
-
-
?
alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate
-
-
-
-
r
alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate
-
-
-
r
CDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + CDP-galactose
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no activity
-
-
?
CDP-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + CDP-galactose
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low activity
-
-
?
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
-
no activity
-
-
?
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
-
-
-
?
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 + 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
the enzyme is involved in galactose metabolism via the Leloir pathway
-
-
?
UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
binding of the glucose moiety of the substrate, but not the UDP moiety, gives rise to a large structural change around 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
the enzyme is involved in galactose metabolism via the Leloir pathway
-
-
?
UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
binding of the glucose moiety of the substrate, but not the UDP moiety, gives rise to a large structural change around the active site
-
-
?
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
-
-
-
?
UDP-alpha-D-glucose + N-acetyl-alpha-D-glucosamine 1-phosphate
alpha-D-glucose 1-phosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
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
-
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
-
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
-
(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
-
kinetic study
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r
UDP-glucose + 2-methylimidazole
uridine 5'-phospho-2-methylimidazole + alpha-D-glucose 1-phosphate
-
mutant H166G, i.e. UDP-hexose synthase
-
r
UDP-glucose + 4-methylimidazole
uridine 5'-phospho-4-methylimidazole + alpha-D-glucose 1-phosphate
-
kinetic study
-
r
UDP-glucose + 4-methylimidazole
uridine 5'-phospho-4-methylimidazole + alpha-D-glucose 1-phosphate
-
mutant H166G, i.e. UDP-hexose synthase
-
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
-
important step in galactose metabolism
-
-
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
-
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
-
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
-
-
-
r
UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
the enzyme is involved in galactose metabolism via the Leloir pathway
-
-
?
UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
the enzyme is involved in galactose metabolism via the Leloir pathway
-
-
?
UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate
alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
-
-
-
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
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
Fe2+
-
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
Fe2+
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
Fe2+
mutant C160A: 0.5 mol per mol of subunit, mutant S161A: 0.4 mol per mol of subunit
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+
-
coordinated in a tetrahedral geometry by Cys52, Cys55, His115, and His164
Zn2+
coordinated in a tetrahedral geometry by Cys52, Cys55, His115, and His164
Zn2+
mutant C160A: 1.3 mol per mol of subunit, mutant S161A: 1.2 mol per mol of subunit like the wild-type
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
2-fluoro-galactose-1-phosphate
competitively inhibit recombinant enzyme
-
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
Clinical features of galactokinase deficiency: a review of the literature.
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
Abnormal N-glycan fucosylation, galactosylation, and sialylation of IgG in adults with classical galactosemia, influence of dietary galactose intake.
Galactosemias
An extensive computational approach to analyze and characterize the functional mutations in the galactose-1-phosphate uridyl transferase (GALT) protein responsible for classical galactosemia.
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
Assessment of galactose-1-phosphate uridyltransferase activity in cells and tissues.
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
Misfolding of galactose 1-phosphate uridylyltransferase can result in type I galactosemia.
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
Reversal of aberrant PI3K/Akt signaling by Salubrinal in a GalT-deficient mouse model.
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]
Genetic Diseases, Inborn
Assessment of galactose-1-phosphate uridyltransferase activity in cells and tissues.
Genetic Diseases, Inborn
Misfolding of galactose 1-phosphate uridylyltransferase can result in type I galactosemia.
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.
Pseudotumor Cerebri
Clinical features of galactokinase deficiency: a review of the literature.
Pyuria
Hemolysis due to Alpha-Hemolytic Enterococcus Urinary Infection: A Rare Cause of Early and Severe Unconjugated Hyperbilirubinemia in a Neonate.
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
Molecular analysis of GALT gene in Argentinian population: Correlation with enzyme activity and characterization of a novel Duarte-like allele.
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
0.77
alpha-D-galactose 1-phosphate
recombinant mutant E182A, pH 8.5, 27°C
0.14
alpha-D-glucose 1-phosphate
recombinant mutant C160A, pH 8.5, 27°C
0.16
alpha-D-glucose 1-phosphate
recombinant wild-type, pH 8.5, 27°C
0.19
alpha-D-glucose 1-phosphate
recombinant mutant E182A, 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
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
kinetics at 4°C, wild-type and mutants
-
additional information
additional information
-
wild-type and mutants in the 2-step reaction
-
additional information
additional information
-
wild-type and mutants in the 2-step reaction
-
additional information
additional information
-
wild-type and mutants in the 2-step reaction
-
additional information
additional information
-
wild-type and mutants in the 2-step reaction
-
additional information
additional information
-
kinetics forward and reverse reaction, overview
-
additional information
additional information
-
steady-state kinetics of G, 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
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
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
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
55
UDP-galactose
recombinant mutant C160A, 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
0.9
2-fluoro-galactose-1-phosphate
pH and temperature not specified in the publication
-
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
14.9
16.3
180
79.5
9.9
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
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
-
-
brenda
-
UniProt
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
drug target
evolution
malfunction
metabolism
physiological function
additional information
-
homology modeling of the three-dimensional protein structure, overview
drug target
-
galactose-1-phosphate uridyltransferase (GALT) provides immune protection in the murine model, and confers partial cross protection against heterologous APP sevorars. The enzyme is an effective cross-protective antigen, which can be used as a potential vaccine candidate against multiple Actinobacillus leuropneumoniae serotypes. An in vivo-induced antigen of Actinobacillus pleuropneumoniae serovar 5b strain L20, provides immunoprotection against serovar 1 strain MS71
drug target
-
galactose-1-phosphate uridyltransferase (GALT) provides immune protection in the murine model, and confers partial cross protection against heterologous APP sevorars. The enzyme is an effective cross-protective antigen, which can be used as a potential vaccine candidate against multiple Actinobacillus leuropneumoniae serotypes. An in vivo-induced antigen of Actinobacillus pleuropneumoniae serovar 5b strain L20, provides immunoprotection against serovar 1 strain MS71
-
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
malfunction
a galactose-1 phosphate uridylyltransferase (GALT)-deficient mouse model reveals reduced fertility and growth restriction. Mutant mice experience cerebellar hypoplasia, which may result from the down-regulation of the PI3K/Akt signaling pathway
malfunction
classic galactosemia (CG) is a potentially lethal inborn error of metabolism, if untreated, that results from profound deficiency of galactose-1-phosphate. An uidylyltransferasegalactose-1-phosphate uridylyltransferase-null rat model of CG documentes phenotypes and defines the relationships among three key galactose metabolites in different tissues and across post-natal development
malfunction
classic galactosemia is a potentially lethal disease caused by the dysfunction of galactose 1-phosphate uridylyltransferase
malfunction
galactosemia type I is caused by a deficiency of the galactose-1-phosphate uridylyltransferase enzyme (GALT). Galactosemic patients show accumulation of Gal, Gal-1-P, galactitol, and galactonate and decrease levels of UDP-hexoses, all are responsible of the observed phenotype. Galactosemia type I patients harbor variations along the whole sequence of the GALT gene, most variations are of the missense type and are commonly present in compound heterozygous state
malfunction
genetic defects of human galactose-1-phosphate uridyltransferase (hGALT) and the partial loss of enzyme function result in an altered galactose metabolism with serious long-term developmental impairment of organs in classic galactosemia patients. GALT deficiency (classic galactosemia) leads to an accumulation of galactose-1-phosphate, is associated with a potentially lethal acute hepatotoxic syndrome, unless affected newborns are kept under a galactose-restricted diet. Endogenously synthesized galactose however, can exert chronic cell toxic effects and worsen the prospects of patient son longer terms. Most patients suffer from a cognitive impairment, from speech defects, motor function disturbances, and a hypergonadotropic hypogonadism in female patients. The metabolic induction of galactosemia-like phenotypes in healthy epithelial/neuronal cells can support studies on the molecular pathomechanisms in classic galactosemia, in particular under conditions of low galactose stress and residual GALT activity
malfunction
genetic defects of human galactose-1-phosphate uridyltransferase are responsible for classical galactosemia, a are genetic metabolic disorder that is passed down in an autosomal recessive manner. Classical galactosemia mainly occurs due to reduced activity of the enzyme GALT owing to a single nucleotide change in the galactose-1-phosphate uridylyltransferase gene (GALT; 9p13.3). Low activity of the GALT enzyme results in increased accumulation of galactose-1-phosphate in a variety of tissues resulting in severe clinical representation, including liver dysfunction, cataract formation, vomiting, hepatomegaly, hypotonia, septicemia, weight loss, diarrhea, jaundice, lethargy, bleeding tendencies, and ovarian failure, which vary from patient to patient. Intellectual retardation, and developmental and cognitive defects are also observed in patients with galactosemia
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 critical step in the Leloir pathway, overview
metabolism
-
the enzyme catalyzes a critical step in the Leloir pathway, overview
metabolism
the enzyme catalyzes a pivotal step in the Leloir pathway of galactose metabolism, overview
metabolism
the enzyme is involved in galactose metabolism via the Leloir pathway
metabolism
-
the enzyme catalyzes a pivotal step in the Leloir pathway of galactose metabolism, overview
-
metabolism
-
the enzyme is involved in galactose metabolism via the Leloir pathway
-
physiological function
-
UDPGal is an important substrate for agar synthesis in red alga
physiological function
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
physiological function
-
GalT is a preferentially expressed antigen during APP infection
physiological function
-
GalT is a preferentially expressed antigen during APP infection
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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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
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
-
catalytically inactive subunits of mutants R333W and Q188R form normal homo- and heterodimers
additional information
-
a second band of MW 22 kDa is found in SDS-PAGE, which shows no enzyme activity
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
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
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
sitting-drop vapor diffusion method, two different crystal structures of Pyrobaculum aerophilum galactose 1-phosphate uridylyltransferase (GalT) are determined: the substrate-free enzyme at 2.33 A and the UDP-bound H140F mutant enzyme at 1.78 A
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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
D28Y
variant associated with type I galactosemia. 13.5% of wild-type activity
E203K
-
native heterozygous mutant, reduced activity by about 50% in erythrocytes
E291K
-
site-directed mutagenesis for construction of the naturally occuring mutation, 62.8% of wild-type activity, accumulation of alpha-D-galactose 1-phosphate, UDP-galactose and UDP-glucose
E340X/L218L/N314D
-
native mutant, no or nearly no enzyme activity, L218L is a silent mutation, galactosemia phenotype
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
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
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
K285N
the most common mutations, include p.S135L, p.N314D, p.Q188R, and p.K285N from different ethnicities. Computational pipeline is used to explore the crystal structure and effects due to the most prevalent mutations in the GALT protein. The mutation p.K285N is located in the alpha helix region (alpha4) of the protein is less pathogenic
K285N
the p.K285N allele shows a high frequency in Caucasians and is associated to null blood GALT activity and a severe clinical phenotype
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
-
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
the most common mutations, include p.S135L, p.N314D, p.Q188R, and p.K285N from different ethnicities. Computational pipeline is used to explore the crystal structure and effects due to the most prevalent mutations in the GALT protein. p.N314D mutation, located in the loop region is less pathogenic
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
-
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
Q188R
-
20-30% activity of wild-type activity as heterodimer with wild-type subunit, no activity as homodimer
Q188R
-
most common native mutation causing galactosemia in the white population
Q188R
-
site-directed mutagenesis for expression of the mutant in Escherichia coli, nearly no activity in vitro
Q188R
-
native mutant, no enzyme activity in vivo, galactosemia phenotype
Q188R
higher tendency of hGALT(p.Q188R) to aggregate due to its reduced ability to be uridylylated
Q188R
significant deviation and fluctuation in the p.Q188R mutation with a loss in compactness reduced the amount of intramolecular hydrogen bonds. p.Q188R mutation (located in the beta-sheet eight region) is extremely pathogenic and has destabilizing effects compared to the native and the other mutations
Q188R
the p.Q188R allele shows a high frequency in Caucasians and is associated to null blood GALT activity and a severe clinical phenotype
R333G
variant associated with type I galactosemia, residue is strictly conserved across species. 0.6% of wild.type activtiy
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
R333W
-
20-30% activity of wild-type activity as heterodimer with wild-type subunit, no activity as homodimer
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
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
the mutant demonstrates reduced compactness and increased intramolecular hydrogen bonds. p.S135L mutation (located at the loop region) is extremely pathogenic and has destabilizing effects compared to the native and the other mutations
S135L
the substitution p.S135L is common in Africans and is associated to a mild phenotype albeit having less than 1% residual enzymatic GALT activity
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
-
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
-
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
-
Munich2 mutant with base exchange at 2252 G to T, 20-25% activity compared to wild-type, no clinical symptoms
additional information
-
native Schönstadt mutant with base exchange at 897 G to C, 15-20% activity compared to wild-type, some clinical symptoms
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
-
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
5 - 10
no loss of the activity when incubated between pH 5.0 and pH 10.0 for 10 minutes at 50°C
762352
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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
about 500fold
His-tagged recombinant wild-type and mutants F171Y and F171L to near homogeneity
-
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 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 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
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gene GALT, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree, expression in Escherichia coli strain BL21(DE3) plysS
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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
-
overexpression of wild-type and mutants in strain BL21(DE3)pLysS
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