BRENDA home
History
Information on EC 2.7.1.6 - galactokinase
for references in articles please use BRENDA:EC2.7.1.6Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.7.1.6 galactokinaseIUBMB Comments
Part of the Leloir pathway for galactose metabolism. The enzymes from mammals and from the bacterium Escherichia coli have no activity with N-acetyl-alpha-D-galactosamine [4-6].
Specify your search results
Word Map
- 2.7.1.6
- galactose-1-phosphate
- galactosemia
- cataract
-
leloir
- uridyltransferase
- lambda
-
gale
- thymidine
-
uridyl
- bacteriophage
- udp-galactose
- lactis
- 1-phosphate
-
epimerase
- galactitol
- udp-glucose
-
inborn
-
pyrophosphorylase
- kluyveromyces
-
rho-dependent
-
coliphage
-
presenile
-
antitermination
-
gal-1-p
-
galactose-induced
- glucose-1-phosphate
- udp-galactose-4-epimerase
- phosphomevalonate
-
counterselection
-
4'-epimerase
- medicine
- synthesis
- nutrition
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
atgalk, ATP:D-galactose-1-phosphotransferase, BiGalK, CLB.507001.110, CLB.510667.120, GAL1, Gal1p, galactokinase, galactokinase 1, galactose kinase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ATP:D-galactose-1-phosphotransferase
-
-
-
-
GAL1
Gal1p
galactokinase
galactose kinase
GALK
GALK1
GalKAmu
kinase (phosphorylating), galacto-
-
-
-
-
kinase, galacto- (phosphorylating)
-
-
-
-
SCO3136
Gal1p
-
-
-
-
galactose kinase
-
-
-
-
GALK
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + alpha-D-galactose = ADP + alpha-D-galactose 1-phosphate
the most likely kinetic mechanism is an ordered ternary complex in which ATP is the first substrate to bind
-
ATP + alpha-D-galactose = ADP + alpha-D-galactose 1-phosphate
mechanism of D-galactose and nucleotide binding
-
ATP + alpha-D-galactose = ADP + alpha-D-galactose 1-phosphate
mechanism of the reaction is sequential in both directions. Residue Asp183 acts as a catalytic base that deprotonates the C1 hydroxyl group of galactose. The pH-kcat profile of the synthesis of galactose 1-phosphate has a pKa of 6.9 likely due to Asp183. The pH-kcat/KGal profile of the reverse reaction lacks a key pKa required for a direct proton transfer mechanism. Arg36 may lower the pKa of the C1 hydroxyl to facilitate deprotonation
-
ATP + alpha-D-galactose = ADP + alpha-D-galactose 1-phosphate
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
ATP:D-galactose 1-phosphotransferase
Part of the Leloir pathway for galactose metabolism. The enzymes from mammals and from the bacterium Escherichia coli have no activity with N-acetyl-alpha-D-galactosamine [4-6].
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9030-53-9
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
2'-dATP + D-galactose
2'-dADP + alpha-D-galactose 1-phosphate
-
-
-
-
?
2-amino-2-deoxy-D-galactose + ATP
2-amino-2-deoxy-D-galactose 1-phosphate + ADP
-
-
-
-
?
3'-dATP + D-galactose
3'-dADP + alpha-D-galactose 1-phosphate
-
-
-
-
?
ATP + 2-amino-2-deoxy-D-galactose
ADP + 2-amino-2-deoxy-D-galactose 1-phosphate
-
-
-
-
?
ATP + 3-deoxy-3-methyl-D-galactose
ADP + 3-deoxy-3-methyl-D-galactose 1-phosphate
-
-
-
-
?
ATP + 4-deoxy-4-fluorogalactose
ADP + 4-deoxy-4-fluorogalactose 1-phosphate
21% conversion
-
-
?
ATP + 4-deoxy-D-galactose
ADP + 4-deoxy-alpha-D-galactose 1-phosphate
-
substrate only for mutants Y223F, Y223W
-
-
?
ATP + 6-deoxy-6-fluorogalactose
ADP + 6-deoxy-6-fluorogalactose 1-phosphate
28% conversion
-
-
?
ATP + 6-deoxy-D-galactose
ADP + 2-amino-2-deoxy-D-galactose 1-phosphate
-
-
-
-
?
ATP + 6-deoxy-D-galactose
ADP + 6-deoxy-D-galactose 1-phosphate
57% conversion
-
-
?
ATP + D-galacturonic acid
ADP + alpha-D-galacturonic acid 1-phosphate
-
substrate: galacturonic acid, specific activity: 0.09 micromol/min/mg
-
-
?
ATP + L-arabinose
ADP + L-arabinose 1-phosphate
10% conversion after 2 h under optimised conditions
-
-
?
ATP + L-glucose
ADP + alpha-L-glucose 1-phosphate
-
substrate only for mutants Y223F, Y223W
-
-
?
CTP + D-galactose
CDP + alpha-D-galactose 1-phosphate
-
substrate: CTP, specific activity: 0.551 micromol/min/mg
-
-
?
dATP + D-galactose
dADP + alpha-D-galactose 1-phosphate
-
substrate: dATP, specific activity: 138 micromol/min/mg
-
-
?
dCTP + D-galactose
dCDP + alpha-D-galactose 1-phosphate
-
substrate: dCTP, specific activity: 0.931 micromol/min/mg
-
-
?
dGTP + D-galactose
dGDP + alpha-D-galactose 1-phosphate
-
substrate: dGTP, specific activity: 31.9 micromol/min/mg
-
-
?
dTTP + D-galactose
?
-
substrate: dTTP, specific activity: 2.5 micromol/min/mg
-
-
?
dUTP + D-galactose
dUDP + alpha-D-galactose 1-phosphate
-
substrate: dUTP, specific activity: 1.5 micromol/min/mg
-
-
?
GTP + D-galactose
GDP + alpha-D-galactose 1-phosphate
-
substrate: GTP, specific activity: 28.5 micromol/min/mg
-
-
?
ITP + D-galactose
IDP + alpha-D-galactose 1-phosphate
-
substrate: ITP, specific activity: 15.7 micromol/min/mg
-
-
?
UTP + D-galactose
UDP + alpha-D-galactose 1-phosphate
-
substrate: UTP, specific activity: 0.52 micromol/min/mg
-
-
?
ATP + 2-deoxy-D-galactose
ADP + 2-deoxy-alpha-D-galactose 1-phosphate
-
substrate: 2-deoxygalactose, specific activity: 99.7 micromol/min/mg
-
-
?
ATP + 2-deoxy-D-galactose
ADP + 2-deoxy-alpha-D-galactose 1-phosphate
-
-
-
-
?
ATP + 2-deoxy-D-galactose
ADP + 2-deoxy-alpha-D-galactose 1-phosphate
-
-
-
?
ATP + 2-deoxy-D-galactose
ADP + 2-deoxy-alpha-D-galactose 1-phosphate
-
-
-
-
?
ATP + 2-deoxy-D-galactose
ADP + 2-deoxy-alpha-D-galactose 1-phosphate
-
-
-
-
?
ATP + 2-deoxy-D-galactose
ADP + 2-deoxy-D-galactose 1-phosphate
-
-
-
-
?
ATP + 3-deoxy-3-fluorogalactose
ADP + 3-deoxy-3-fluorogalactose 1-phosphate
27% conversion
-
-
?
ATP + 3-deoxy-3-fluorogalactose
ADP + 3-deoxy-3-fluorogalactose 1-phosphate
27% conversion
-
-
?
ATP + 3-deoxy-D-galactose
ADP + 3-deoxy-D-galactose 1-phosphate
19% conversion
-
-
?
ATP + 3-deoxy-D-galactose
ADP + 3-deoxy-D-galactose 1-phosphate
19% conversion
-
-
?
ATP + 3-deoxy-D-galactose
ADP + 3-deoxy-D-galactose 1-phosphate
85% conversion after 2 h under optimised conditions
-
-
?
ATP + 3-deoxy-D-galactose
ADP + 3-deoxy-D-galactose 1-phosphate
85% conversion after 2 h under optimised conditions
-
-
?
ATP + 6-deoxy-D-galactose
ADP + 6-deoxy-alpha-D-galactose 1-phosphate
-
substrate: 6-deoxygalactose, specific activity: 0.0781 micromol/min/mg
-
-
?
ATP + 6-deoxy-D-galactose
ADP + 6-deoxy-alpha-D-galactose 1-phosphate
-
-
-
-
?
ATP + alpha-D-galactose
ADP + alpha-D-galactose 1-phosphate
-
-
-
?
ATP + alpha-D-galactose
ADP + alpha-D-galactose 1-phosphate
-
-
-
?
ATP + alpha-D-galactose
ADP + alpha-D-galactose 1-phosphate
-
-
-
?
ATP + alpha-D-galactose
ADP + alpha-D-galactose 1-phosphate
-
-
-
?
ATP + alpha-D-galactose
ADP + alpha-D-galactose 1-phosphate
the enzyme catalyses the first committed step in the Leloir pathway
-
-
?
ATP + alpha-D-galactose
ADP + alpha-D-galactose 1-phosphate
negative charge at residue 174 is essential for catalysis
-
-
?
ATP + alpha-D-galactose
ADP + alpha-D-galactose 1-phosphate
72% conversion
-
-
?
ATP + alpha-D-galactose
ADP + alpha-D-galactose 1-phosphate
72% conversion
-
-
?
ATP + alpha-D-galactose
ADP + alpha-D-galactose 1-phosphate
involved in Leloir pathway
-
-
?
ATP + alpha-D-galactose
ADP + alpha-D-galactose 1-phosphate
91% conversion after 2 h under optimised conditions
-
-
?
ATP + alpha-D-galactose
ADP + alpha-D-galactose 1-phosphate
involved in Leloir pathway
-
-
?
ATP + alpha-D-galactose
ADP + alpha-D-galactose 1-phosphate
91% conversion after 2 h under optimised conditions
-
-
?
ATP + D-galactosamine
ADP + alpha-D-galactosamine 1-phosphate
-
substrate: D-galactosamine, specific activity: 12.5 micromol/min/mg
-
-
?
ATP + D-galactosamine
ADP + alpha-D-galactosamine 1-phosphate
68% conversion
-
-
?
ATP + D-galactosamine
ADP + alpha-D-galactosamine 1-phosphate
68% conversion
-
-
?
ATP + D-galactosamine
ADP + D-galactosamine 1-phosphate
100% of the activity with alpha-D-galactose
-
-
?
ATP + D-galactosamine
ADP + D-galactosamine 1-phosphate
100% of the activity with alpha-D-galactose
-
-
?
ATP + D-galactosamine
ADP + D-galactosamine 1-phosphate
87% conversion after 2 h under optimised conditions
-
-
?
ATP + D-galactosamine
ADP + D-galactosamine 1-phosphate
87% conversion after 2 h under optimised conditions
-
-
?
ATP + D-galactose
ADP + alpha-D-galactose 1-phosphate
-
very strict substrate specificity for galactose and ATP
-
-
?
ATP + D-galactose
ADP + alpha-D-galactose 1-phosphate
-
substrate: ATP, specific activity: 137 micromol/min/mg
-
-
?
ATP + D-galactose
ADP + alpha-D-galactose 1-phosphate
-
substrate: D-galactose, specific activity: 158 micromol/min/mg
-
-
?
ATP + D-galactose
ADP + alpha-D-galactose 1-phosphate
-
-
-
-
?
ATP + D-galactose
ADP + alpha-D-galactose 1-phosphate
-
-
-
-
?
ATP + D-galactose
ADP + alpha-D-galactose 1-phosphate
-
unidirectional towards galactose phosphorylation
-
-
ir
ATP + D-galactose
ADP + alpha-D-galactose 1-phosphate
-
-
-
-
?
ATP + D-galactose
ADP + alpha-D-galactose 1-phosphate
-
-
-
-
?
ATP + D-galactose
ADP + alpha-D-galactose 1-phosphate
-
-
-
?
ATP + D-galactose
ADP + alpha-D-galactose 1-phosphate
-
-
-
-
?
ATP + D-galacturonic acid
ADP + D-galacturonic acid 1-phosphate
20.2% of the activity with alpha-D-galactose
-
-
?
ATP + D-galacturonic acid
ADP + D-galacturonic acid 1-phosphate
20.2% of the activity with alpha-D-galactose
-
-
?
ATP + D-glucose
ADP + alpha-D-glucose 1-phosphate
52.5% of the activity with alpha-D-galactose
-
-
?
ATP + D-glucose
ADP + alpha-D-glucose 1-phosphate
52.5% of the activity with alpha-D-galactose
-
-
?
ATP + D-talose
ADP + alpha-D-talose 1-phosphate
-
substrate only for mutants Y223F, Y223W
-
-
?
ATP + D-talose
ADP + alpha-D-talose 1-phosphate
41% conversion
-
-
?
ATP + D-talose
ADP + alpha-D-talose 1-phosphate
41% conversion
-
-
?
ATP + galactose
ADP + alpha-D-galactose 1-phosphate
-
the enzyme catalyzes the first step in the conversion of galactose to glucose. Galactokinase deficiency is characterized by galactosemia, galactosuria and cataract formation in early childhood
-
-
?
ATP + galactose
ADP + alpha-D-galactose 1-phosphate
-
galactokinase deficiency is an autosomal recessive disorder, which causes cataract formation in children not maintained on a lactose-free diet
-
-
?
ATP + galactose
ADP + alpha-D-galactose 1-phosphate
-
galaktokinase deficiency is an autosomal recessive disorder characterized by hypergalactosemia and cataract formation
-
-
?
ATP + galactose
ADP + alpha-D-galactose 1-phosphate
-
lack of fully functional galactokinase is one cause of the inherited disease galactosemia, the main clinical manifestation of which is the early onset of cataracts
-
-
?
ATP + galactose
ADP + alpha-D-galactose 1-phosphate
-
first step in the Leloir pathway for galactose metabolism
-
-
?
ATP + N-acetyl-D-galactosamine
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
15.5% of the activity with alpha-D-galactose
-
-
?
ATP + N-acetyl-D-galactosamine
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
15.5% of the activity with alpha-D-galactose
-
-
?
ATP + N-acetyl-D-galactosamine
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
-
?
ATP + N-acetyl-D-galactosamine
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
40% conversion after 2 h under optimised conditions
-
-
?
ATP + N-acetyl-D-galactosamine
ADP + N-acetyl-alpha-D-galactosamine 1-phosphate
40% conversion after 2 h under optimised conditions
-
-
?
additional information
?
-
-
no tolerance for C-4 changes in the substrate
-
-
?
additional information
?
-
-
no substrate: N-acetyl-D-galactosamine, L-arabinose, D-fucose, D-glucose
-
-
?
additional information
?
-
-
amino acid side chains responsible for anchoring the sugar ligand to the protein include Arg36, Glu42, Asp45, ASp183, and Tyr233
-
-
?
additional information
?
-
-
mechanism of the reaction is sequential in both directions. Residue Asp183 acts as a catalytic base that deprotonates the C1 hydroxyl group of galactose. The pH-kcat profile of the synthesis of galactose 1-phosphate has a pKa of 6.9 likely due to Asp183. The pH-kcat/KGal profile of the reverse reaction lacks a key pKa required for a direct proton transfer mechanism. Arg36 may lower the pKa of the C1 hydroxyl to facilitate deprotonation
-
-
?
additional information
?
-
-
galactokinase Gal1p is a regulator of transcription. Gal1p activates Gal4p, the activator of GAL genes. Gal1p activates Gal4p by direct interaction with the Gal4p inhibitor Gal80p. Interaction requires galactose, adenosine triphosphate and the regulatory function of Gal1p. The gal1p-gal80p complex formation results in the inactivation of Gal80p, thereby transmitting the galactose signal to Gal4p
-
-
?
additional information
?
-
-
L-arabinose, D-fucose, L-glucose, and D-talose are no substrates
-
-
?
additional information
?
-
-
L-arabinose, D-fucose, L-glucose, and D-talose are no substrates
-
-
?
additional information
?
-
-
key enzyme for cellulase induction during growth on lactose
-
-
?
additional information
?
-
-
induction of the gal pathway and cellulase genes involves no transcriptional inducer function of the galactokinase in Hypocrea jecorina
-
-
?
additional information
?
-
-
induction of the gal pathway and cellulase genes involves no transcriptional inducer function of the galactokinase in Hypocrea jecorina
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
ATP + alpha-D-galactose
ADP + alpha-D-galactose 1-phosphate
-
-
-
?
ATP + alpha-D-galactose
ADP + alpha-D-galactose 1-phosphate
-
-
-
?
ATP + alpha-D-galactose
ADP + alpha-D-galactose 1-phosphate
-
-
-
?
ATP + alpha-D-galactose
ADP + alpha-D-galactose 1-phosphate
the enzyme catalyses the first committed step in the Leloir pathway
-
-
?
ATP + alpha-D-galactose
ADP + alpha-D-galactose 1-phosphate
involved in Leloir pathway
-
-
?
ATP + alpha-D-galactose
ADP + alpha-D-galactose 1-phosphate
involved in Leloir pathway
-
-
?
ATP + galactose
ADP + alpha-D-galactose 1-phosphate
-
the enzyme catalyzes the first step in the conversion of galactose to glucose. Galactokinase deficiency is characterized by galactosemia, galactosuria and cataract formation in early childhood
-
-
?
ATP + galactose
ADP + alpha-D-galactose 1-phosphate
-
galactokinase deficiency is an autosomal recessive disorder, which causes cataract formation in children not maintained on a lactose-free diet
-
-
?
ATP + galactose
ADP + alpha-D-galactose 1-phosphate
-
galaktokinase deficiency is an autosomal recessive disorder characterized by hypergalactosemia and cataract formation
-
-
?
ATP + galactose
ADP + alpha-D-galactose 1-phosphate
-
lack of fully functional galactokinase is one cause of the inherited disease galactosemia, the main clinical manifestation of which is the early onset of cataracts
-
-
?
ATP + galactose
ADP + alpha-D-galactose 1-phosphate
-
first step in the Leloir pathway for galactose metabolism
-
-
?
additional information
?
-
-
galactokinase Gal1p is a regulator of transcription. Gal1p activates Gal4p, the activator of GAL genes. Gal1p activates Gal4p by direct interaction with the Gal4p inhibitor Gal80p. Interaction requires galactose, adenosine triphosphate and the regulatory function of Gal1p. The gal1p-gal80p complex formation results in the inactivation of Gal80p, thereby transmitting the galactose signal to Gal4p
-
-
?
additional information
?
-
-
key enzyme for cellulase induction during growth on lactose
-
-
?
additional information
?
-
-
induction of the gal pathway and cellulase genes involves no transcriptional inducer function of the galactokinase in Hypocrea jecorina
-
-
?
additional information
?
-
-
induction of the gal pathway and cellulase genes involves no transcriptional inducer function of the galactokinase in Hypocrea jecorina
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Fe2+
Mg2+
Mn2+
Ni2+
Zn2+
additional information
Ca2+
-
absolute requirement for a divalent cation, Ca2+ can be partially replaced by Co2+
Ca2+
-
divalent cations activity in the order of decreasing efficiency: Mn2+, Mg2+, Ca2+, Fe2+
Co2+
-
absolute requirement for a divalent cation, Mg2+ can be partially replaced by Co2+
Co2+
-
divalent cations activate in the order of decreasing efficiency: Mn2+, Mg2+, Ca2+, Fe2+
Co2+
-
divalent cation required, in the order of decreasing efficiency: Mg2+, Co2+, Mn2+, Fe2+
Fe2+
-
divalent cations activity in the order of decreasing efficiency: Mn2+, Mg2+, Ca2+, Fe2+
Fe2+
-
divalent cation required, in the order of decreasing efficiency: Mg2+, Co2+, Mn2+, Fe2+
Mg2+
-
absolute requirement for a divalent cation, maximally active in presence of 5 mM Mg2+
Mg2+
activates. Optimum Mg2+ concentration is around 1 mm, with a very modest decrease in activity as the Mg2+ concentration increases
Mg2+
-
divalent cations activate in the order of decreasing efficiency: Mn2+, Mg2+, Ca2+, Fe2+
Mg2+
-
divalent cation required, in the order of decreasing efficiency: Mg2+, Co2+, Mn2+, Fe2+
Mn2+
-
can partly substitute Mg2+, with the reduction of the activity by about 21%
Mn2+
-
absolute requirement for a divalent cation, Mg2+ can be partially replaced by Co2+
Mn2+
-
divalent cations activate in the order of decreasing efficiency: Mn2+, Mg2+, Ca2+, Fe2+
Mn2+
-
divalent cation required, in the order of decreasing efficiency: Mg2+, Co2+, Mn2+, Fe2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-(1,3-benzoxazol-2-ylamino)-4-(4-chloro-1H-pyrazol-3-yl)-4,6,7,8-tetrahydroquinazolin-5(1H)-one
-
inhibitory to isoform Galk1, no inhibition of isoform Galk2 up to 40 microM. Uncompetitive with respect to galactose, compound directly competes with ATP at the binding site, and galactose may be required to bind first. Compound is able to lower galactose 1-phosphate levels in primary fibroblasts of patients suffering Classic Galactosemia without significant effect on viability of cells
NaCl
50Ć¢ĀĀ500 mM, the enzymatic activity decreases approximately 40%Ć¢ĀĀ60%, respectively; 50Ć¢ĀĀ500 mM, the enzymatic activity decreases approximately 40%Ć¢ĀĀ60%, respectively
ADP
-
competitive with respect to ATP, uncompetitive with respect to galactose
alpha-D-galactose 1-phosphate
-
uncompetitive inhibitor with respect to galactose, mixed inhibitor with respect to ATP
Hg2+
-
0.5 mM HgCl2, complete inhibition, activity is completely restored by 1 mM dithiothreitol
PCMB
-
0.1 mM, complete inhibition, activity is completely restored by 1 mM dithiothreitol
additional information
-
not inhibitory: N-acetyl-D-galactosamine, L-arabinose, D-fucose, D-glucose
-
additional information
discovery of novel inhibitors of human galactokinase by high-throughput structure-based virtual screening
-
additional information
-
discovery of novel inhibitors of human galactokinase by high-throughput structure-based virtual screening
-
additional information
-
Hg-containing compounds at 0.4 mM completely block the enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.3
2-deoxy-D-galactose
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M185L/M180V/D268E/A334S/R366Q/G373S/Y379W
2
2-deoxy-D-galactose
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/D268E/A334S/R366Q/G373S/Y379W
0.15
alpha-D-galactose
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/A334S/D268E/R336Q/G373S
0.23
alpha-D-galactose
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/A334S/G373S
0.27
alpha-D-galactose
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/A334S/D268E/G373S
0.31
alpha-D-galactose
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/D268E/A334S/R366Q/G373S/Y379W
3.278
alpha-D-galactose
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M185L/M180V/D268E/A334S/R366Q/G373S/Y379W
0.0027
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M185L/Y379W, cosubstrate: D-galactosamine
0.0037
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme Y379W, cosubstrate: D-galactosamine
0.004
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M185L/M180V/D268E/A334S/R366Q/G373S/Y379W, cosubstrate: 2-deoxy-D-galactose
0.0044
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M185L/M180V/D268E/A334S/R366Q/G373S/Y379W, cosubstrate: D-galactosamine
0.0066
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/D268E/A334S/R366Q/G373S/Y379W, cosubstrate: D-galactosamine
0.0134
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/D268E/A334S/R366Q/G373S/Y379W, cosubstrate: D-talose
0.016
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme Y379W, cosubstrate: 2-deoxy-D-galactose
0.0173
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M185L, cosubstrate: 2-deoxy-D-galactose
0.0174
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/D268E/A334S/R366Q/G373S/Y379W, cosubstrate: 2-deoxy-D-galactose
0.0432
ATP
pH 7.5, 37ĆĀ°C, wild-type enzyme, cosubstrate: 2-deoxy-D-galactose
0.046
ATP
-
in the presence of 2-deoxy-D-galactose as a substrate, at 30ĆĀ°C, wild type enzyme
0.057
ATP
-
in the presence of D-galactose as a substrate, wild type enzyme
0.162
ATP
pH 7.5, 37ĆĀ°C, wild-type enzyme, cosubstrate: D-galactosamine
0.225
ATP
-
in the presence of D-glucose as a substrate, at 30ĆĀ°C, wild type enzyme
0.36
ATP
pH 8.6, temperature not specified in the publication
0.57
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/A334S/G373S, cosubstrate: alpha-D-galactose
0.82
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/A334S, cosubstrate: alpha-D-galactose
1
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V, cosubstrate: alpha-D-galactose
2.5
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/A334S/D268E/G373S, cosubstrate: alpha-D-galactose
3.8
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/A334S/D268E/R336Q/G373S, cosubstrate: alpha-D-galactose
3.9
ATP
pH 7.5, 37ĆĀ°C, wild type enzyme, cosubstrate: alpha-D-galactose
4.2
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/A334S, cosubstrate: alpha-D-galactose
5
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme Y379W, cosubstrate: alpha-D-galactose
5.4
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M180V, cosubstrate: alpha-D-galactose
7.7
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme R366Q, cosubstrate: alpha-D-galactose
7.9
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme A334S, cosubstrate: alpha-D-galactose
8.1
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/D268E/A334S/R366Q/G373S/Y379W, cosubstrate: alpha-D-galactose
11.4
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M185L/Y379W, cosubstrate: alpha-D-galactose
12.4
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M185L/M180V/D268E/A334S/R366Q/G373S/Y379W, cosubstrate: alpha-D-galactose
13
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme D268E, cosubstrate: alpha-D-galactose
13
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme G373S, cosubstrate: alpha-D-galactose
18
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M60V, cosubstrate: alpha-D-galactose
34.5
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M185L, cosubstrate: alpha-D-galactose
0.62
D-galactosamine
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M185L/M180V/D268E/A334S/R366Q/G373S/Y379W
4.8
D-galactosamine
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/D268E/A334S/R366Q/G373S/Y379W
0.091
D-galactose
pH 8.6, temperature not specified in the publication
0.108
D-galactose
pH 8.6, temperature not specified in the publication
2.2
D-talose
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/D268E/A334S/R366Q/G373S/Y379W
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.7
2-deoxy-D-galactose
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M185L/M180V/D268E/A334S/R366Q/G373S/Y379W
6.8
2-deoxy-D-galactose
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/D268E/A334S/R366Q/G373S/Y379W
1.6
alpha-D-galactose
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/A334S/D268E/R336Q/G373S
1.7
alpha-D-galactose
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/A334S/D268E/G373S
1.7
alpha-D-galactose
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/A334S/G373S
5
alpha-D-galactose
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/D268E/A334S/R366Q/G373S/Y379W
12.9
alpha-D-galactose
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M185L/M180V/D268E/A334S/R366Q/G373S/Y379W
0.2
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/D268E/A334S/R366Q/G373S/Y379W, cosubstrate: D-talose
0.2
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme Y379W, cosubstrate: D-galactosamine
0.3
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M185L/M180V/D268E/A334S/R366Q/G373S/Y379W, cosubstrate: D-galactosamine
0.7
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M185L/M180V/D268E/A334S/R366Q/G373S/Y379W, cosubstrate: 2-deoxy-D-galactose
0.8
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme Y379W, cosubstrate: 2-deoxy-D-galactose
1
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M180V, cosubstrate: alpha-D-galactose
1.5
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V, cosubstrate: alpha-D-galactose
1.6
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/A334S/D268E/R336Q/G373S, cosubstrate: alpha-D-galactose
1.7
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/A334S, cosubstrate: alpha-D-galactose
1.7
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/A334S/D268E/G373S, cosubstrate: alpha-D-galactose
1.7
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/A334S/G373S, cosubstrate: alpha-D-galactose
1.7
ATP
pH 7.5, 37ĆĀ°C, wild type enzyme, cosubstrate: alpha-D-galactose
2.1
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme R366Q, cosubstrate: alpha-D-galactose
2.4
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme G373S, cosubstrate: alpha-D-galactose
2.5
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M185L/Y379W, cosubstrate: alpha-D-galactose
2.6
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/A334S, cosubstrate: alpha-D-galactose
3.2
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme D268E, cosubstrate: alpha-D-galactose
4
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/D268E/A334S/R366Q/G373S/Y379W, cosubstrate: D-galactosamine
4.3
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme A334S, cosubstrate: alpha-D-galactose
4.8
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M60V, cosubstrate: alpha-D-galactose
5
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/D268E/A334S/R366Q/G373S/Y379W, cosubstrate: alpha-D-galactose
6.8
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/D268E/A334S/R366Q/G373S/Y379W, cosubstrate: 2-deoxy-D-galactose
6.8
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme Y379W, cosubstrate: alpha-D-galactose
6.8
ATP
pH 7.5, 37ĆĀ°C, wild-type enzyme, cosubstrate: 2-deoxy-D-galactose
8.1
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M185L, cosubstrate: alpha-D-galactose
9.4
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M185L, cosubstrate: 2-deoxy-D-galactose
12.9
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M185L/M180V/D268E/A334S/R366Q/G373S/Y379W, cosubstrate: alpha-D-galactose
25
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M185L/Y379W, cosubstrate: D-galactosamine
0.3
D-galactosamine
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M185L/M180V/D268E/A334S/R366Q/G373S/Y379W
4
D-galactosamine
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/D268E/A334S/R366Q/G373S/Y379W
0.38
D-galactose
pH 8.6, temperature not specified in the publication
0.2
D-talose
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/D268E/A334S/R366Q/G373S/Y379W
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.3
2-deoxy-D-galactose
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M185L/M180V/D268E/A334S/R366Q/G373S/Y379W
3.1
2-deoxy-D-galactose
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/D268E/A334S/R366Q/G373S/Y379W
3.9
alpha-D-galactose
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M185L/M180V/D268E/A334S/R366Q/G373S/Y379W
6.3
alpha-D-galactose
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/A334S/D268E/G373S
7.3
alpha-D-galactose
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/A334S/G373S
10.9
alpha-D-galactose
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/A334S/D268E/R336Q/G373S
16.1
alpha-D-galactose
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/D268E/A334S/R366Q/G373S/Y379W
17.6
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/D268E/A334S/R366Q/G373S/Y379W, cosubstrate: D-talose
19.4
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M185L/M180V/D268E/A334S/R366Q/G373S/Y379W, cosubstrate: 2-deoxy-D-galactose
23
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M185L, cosubstrate: 2-deoxy-D-galactose
50
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme Y379W, cosubstrate: 2-deoxy-D-galactose
50
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme Y379W, cosubstrate: D-galactosamine
67
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M185L/M180V/D268E/A334S/R366Q/G373S/Y379W, cosubstrate: D-galactosamine
185
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M180V, cosubstrate: alpha-D-galactose
190
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme G373S, cosubstrate: alpha-D-galactose
190
ATP
pH 7.5, 37ĆĀ°C, wild-type enzyme, cosubstrate: 2-deoxy-D-galactose
220
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M185L/Y379W, cosubstrate: alpha-D-galactose
236
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M185L, cosubstrate: alpha-D-galactose
240
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme D268E, cosubstrate: alpha-D-galactose
270
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M60V, cosubstrate: alpha-D-galactose
270
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme R366Q, cosubstrate: alpha-D-galactose
390
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/A334S/D268E/R336Q/G373S, cosubstrate: alpha-D-galactose
390
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/D268E/A334S/R366Q/G373S/Y379W, cosubstrate: 2-deoxy-D-galactose
430
ATP
pH 7.5, 37ĆĀ°C, wild type enzyme, cosubstrate: alpha-D-galactose
550
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme A334S, cosubstrate: alpha-D-galactose
550
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/D268E/A334S/R366Q/G373S/Y379W, cosubstrate: alpha-D-galactose
600
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/D268E/A334S/R366Q/G373S/Y379W, cosubstrate: D-galactosamine
620
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/A334S, cosubstrate: alpha-D-galactose
680
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/A334S/D268E/G373S, cosubstrate: alpha-D-galactose
950
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M185L/Y379W, cosubstrate: D-galactosamine
1000
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M185L/M180V/D268E/A334S/R366Q/G373S/Y379W
1360
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme Y379W, cosubstrate: alpha-D-galactose
1430
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V, cosubstrate: alpha-D-galactose
2000
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/A334S, cosubstrate: alpha-D-galactose
3000
ATP
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/A334S/G373S, cosubstrate: alpha-D-galactose
0.4
D-galactosamine
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M185L/M180V/D268E/A334S/R366Q/G373S/Y379W
0.9
D-galactosamine
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/D268E/A334S/R366Q/G373S/Y379W
3.5
D-galactose
pH 8.6, temperature not specified in the publication
0.2
D-talose
pH 7.5, 37ĆĀ°C, mutant enzyme M60V/M180V/D268E/A334S/R366Q/G373S/Y379W
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.41
ATP
isoform GalK2, pH 8.6, temperature not specified in the publication
28
alpha-D-galactose 1-phosphate
-
pH 8, 37ĆĀ°C, uncompetitive inhibition constant with respect to galactose
39
alpha-D-galactose 1-phosphate
-
pH 8, 37ĆĀ°C, uncompetitive inhibition constant with respect to ATP
90
alpha-D-galactose 1-phosphate
-
pH 8, 37ĆĀ°C, competitive inhibition constant with respect to ATP
3.5
D-galactose 1-phosphate
-
pH 7.3, 25ĆĀ°C, competitive inhibition with galactose as the variable substrate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0047
2-(1,3-benzoxazol-2-ylamino)-4-(4-chloro-1H-pyrazol-3-yl)-4,6,7,8-tetrahydroquinazolin-5(1H)-one
Homo sapiens
-
isoform Galk1, pH not specified in the publication, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0781
-
substrate: ATP + 6-deoxy-D-galactose, pH 8, 37ĆĀ°C
0.09
-
substrate: ATP + D-galacturonic acid, pH 8, 37ĆĀ°C
12.5
-
substrate: ATP + D-galactosamine, pH 8, 37ĆĀ°C
99.7
-
substrate: ATP + 2-deoxy-D-galactose, pH 8, 37ĆĀ°C
additional information
additional information
1.04 units/mg for strain IMDOST40 and 0.41 units/mg for strain IMDOST07 in 100 mM triethanolamine buffer (pH 7.8), containing 5 mM MgCl2, 2 mM phosphoenolpyruvate, 2 mM ATP, and 10 mM galactose
additional information
-
1.04 units/mg for strain IMDOST40 and 0.41 units/mg for strain IMDOST07 in 100 mM triethanolamine buffer (pH 7.8), containing 5 mM MgCl2, 2 mM phosphoenolpyruvate, 2 mM ATP, and 10 mM galactose
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5 - 9.5
7.8
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 10
pH 4.0: about 90% of maximal activity, pH 10.0: about 90% of maximal activity
5.5 - 8
-
pH 5.5: about 60% of maximal activity, pH 8.0: about 70% of maximal activity, potassium phosphate buffer
6.7 - 8.7
-
pH 6.7: about 45% of maximal activity, pH 8.7: about 35% of maximal activity
7 - 10
pH 7.0: about 65% of maximal activity, pH 10.0: about 90% of maximal activity
7 - 9
7 - 9
-
pH-optimum at pH 8 with a sharp drop in activity above pH 9.0 and a more gradual drop below pH 7.0
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 60
15ĆĀ°C: about 55% of maximal activity, 60ĆĀ°C: about 70% of maximal activity
20 - 60
-
20ĆĀ°C: about 30% of maximal activity, 60ĆĀ°C: about 40% of maximal activity
37 - 60
37ĆĀ°C: about 65% of maximal activity, 60ĆĀ°C: about 55% of maximal activity
5 - 50
5ĆĀ°C: about 60% of maximal activity, 55ĆĀ°C: about 50% of maximal activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.7
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Japanese patients with GALK deficiency, Caucasian patients with GALK deficiency and Japanese wild-type controls
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
expression of both isoforms GalK1 and GalK2
brenda
expression of both isoforms GalK1 and GalK2
brenda
-
activity is high at birth and decrases so that by the age of approximately 4 years it reaches the adult value
brenda
-
of 2-week-old piglets. Activities in livers of fetal or suckling mammals and decreases at weaning so that the activity in adults is between 10 and 20% of the maximum attained during development
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug target
malfunction
metabolism
drug target
a pharmacological inhibitor of galactokinase is hypothesized to be therapeutic strategy for treating galactosemia by reducing production of alpha-D-galactose 1-phosphate
malfunction
-
an AtGALK T-DNA insertion mutant (atgalk) that (a) is AtGALK transcript deficient, (b) displays no GALK activity in vegetative tissues; and (c) accumulates Gal up to 6.8 mg/g FW in vegetative tissues, in contrast to wild-type plants. By constitutively overexpressing functional AtGALK cDNA, atgalk is functionally rescued
malfunction
galactosemia type 2 is an autosomal recessive disorder characterized by the deficiency of galactokinase enzyme due to missense mutations in GALK1 gene, which is associated with various manifestations such as hypergalactosemia and formation of cataracts. Systematically searched for the mutations that have been reported in the GALK1 protein that cause galactosemia type 2. Genetic variations form the basis of the evolution; however, not all genetic mutations are disease-causing
metabolism
-
bimodal expression of yeast GAL genes is controlled by a long noncoding RNA and a bifunctional galactokinase
metabolism
the enzyme catalyses the first committed step in the Leloir pathway
Show AA Sequence and Transmembrane Helices (14711 entries)
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM