2.7.1.6: galactokinase
This is an abbreviated version!
For detailed information about galactokinase, go to the full flat file.
Word Map on EC 2.7.1.6
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2.7.1.6
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galactose-1-phosphate
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galactosemia
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cataract
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leloir
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uridyltransferase
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lambda
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gale
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uridyl
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thymidine
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bacteriophage
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udp-galactose
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1-phosphate
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epimerase
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lactis
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galactitol
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inborn
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udp-glucose
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kluyveromyces
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pyrophosphorylase
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gal-1-p
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presenile
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rho-dependent
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coliphage
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antitermination
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phosphomevalonate
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galactose-induced
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4'-epimerase
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glucose-1-phosphate
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counterselection
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udp-galactose-4-epimerase
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medicine
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synthesis
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nutrition
- 2.7.1.6
- galactose-1-phosphate
- galactosemia
- cataract
-
leloir
- uridyltransferase
- lambda
-
gale
-
uridyl
- thymidine
- bacteriophage
- udp-galactose
- 1-phosphate
-
epimerase
- lactis
- galactitol
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inborn
- udp-glucose
- kluyveromyces
-
pyrophosphorylase
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gal-1-p
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presenile
-
rho-dependent
-
coliphage
-
antitermination
- phosphomevalonate
-
galactose-induced
-
4'-epimerase
- glucose-1-phosphate
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counterselection
- udp-galactose-4-epimerase
- medicine
- synthesis
- nutrition
Reaction
Synonyms
atgalk, ATP:D-galactose-1-phosphotransferase, BiGalK, CLB.507001.110, CLB.510667.120, GAL1, Gal1p, galactokinase, galactokinase 1, galactose kinase, GALK, GALK1, GalKAmu, GalKSpe4, kinase (phosphorylating), galacto-, kinase, galacto- (phosphorylating), SCO3136
ECTree
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APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
medicine
nutrition
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expression of enzyme in Streptococcus thermophilus, recombinant strain grows on galactose with a generation time of 55 min, which is almost double the generation time on lactose. During growth on milk and under conditions simulating those used to produce mozzarella cheese, recombinant strain grows and produces acid more rapidly than wild-type strain
synthesis
medicine
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analysis of residues involved in type II galactosemia within three-dimensional architecture of enzyme
medicine
identification of five mutations of GALK1 gene in five unrelated Korean patients with GALK deficiency and investigaion of their biochemical characteristics using mammalian cell expression studies. Four missense mutations (p.G137R, p.R256W, p.R277Q, and p.V281M) and one small insertion (c.850_851insG) are identified. Among four patients with severely reduced GALK activity, two are found to be homozygotes for p.R256W and the other two are compound heterozygotes for different molecular defects (p.G137R/p.R277Q and p.V281M/c.850_851insG). One patient with moderately decreased GALK activity is heterozygous for p.R256W. Expression analysis in Cos7 cells confirms that each of the mutations results in reduction of GALK activity and causes GALK deficiency
medicine
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in primary fibroblasts of patients suffering Classic Galactosemia, inhibitor 2-(1,3-benzoxazol-2-ylamino)-4-(4-chloro-1H-pyrazol-3-yl)-4,6,7,8-tetrahydroquinazolin-5(1H)-one is able to lower galactose 1-phosphate levels without significant effect on viability of cells
medicine
the enzyme has biotechnological potential in enzyme replacement therapy for type II galactosaemia
synthesis
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enzyme mutant Y371H/M173L, substrate range is much wider than wild-type, generation of unnatural sugar 1-phosphates
synthesis
LgGalK and galactose oxidase variant M1 are combined in a one-pot, two-step system to synthesize 6-oxogalactose-1-phosphate and 6-oxo-2-fluorogalactose-1-phosphate, which are subsequently used to produce a panel of 30 substituted 6-aminogalactose-1-phosphate derivatives by chemical reductive amination in a one-pot, three-step chemoenzymatic process
synthesis
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LgGalK and galactose oxidase variant M1 are combined in a one-pot, two-step system to synthesize 6-oxogalactose-1-phosphate and 6-oxo-2-fluorogalactose-1-phosphate, which are subsequently used to produce a panel of 30 substituted 6-aminogalactose-1-phosphate derivatives by chemical reductive amination in a one-pot, three-step chemoenzymatic process
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