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
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epimerase
- lactis
- galactitol
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inborn
- udp-glucose
- kluyveromyces
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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
-
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
2.7.1.6 galactokinaseAdvanced search results
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results (Engineering
Engineering on EC 2.7.1.6 - galactokinase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
M173L
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moderate activity on D-glucose, wider substrate specificity than wild-type
M173L/Y371H
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acts on additional substrates such as 4-azido-4-deoxy-D-galactose, 6-ido-6-deoxy-D-galactose, 6-chloro-6-deoxy-D-galactose, 6-bromo-6-deoxy-D-galactose, 4-deoxy-D-galactose, 6-thio-6-deoxy-D-galactose, 6-thio-6-deoxy-D-glucose, 6-azido-6-deoxy-D-glucose
Y223F
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activity similar to wild-type, converts additional substrates L-glucose, D-talose, 4-deoxy-D-galactose, less active on D-galactosamine than wild-type
Y223W
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significant reduction in activity, converts additional substrates L-glucose, D-talose, 4-deoxy-D-galactose, with less efficiency than mutant Y223F, less active on D-galactosamine than wild-type
A198V
A384P
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mutant enzyme is not present in the soluble fraction after sonication and can not be purified
C32M
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mutant enzyme is not present in the soluble fraction after sonication and can not be purified
E244S
significantly increased (5fold) Michaelis constant for ATP, indicating that this variation impacts on the interaction of the protein with ATP. Significantly increased Michaelis constants for galactose. Turnover number is significantly increased
E245S
catalyzes less efficiently the phosphorylation of galactose than the wild-type enzyme. Significantly increased Michaelis constants for galactose. Turnover number is significantly increased
G346S
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mutant enzyme shows substantial reduction in turnover number. Lower specificity constant for galactose than wild-type enzyme
G347S
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mutant enzyme shows substantial reduction in turnover number, increase in Km-value for galactose. Lower specificity constant for galactose than wild-type enzyme
G349S
G36R
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mutant enzyme is not present in the soluble fraction after sonication and can not be purified
H44Y
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increrase in Km-value for galactose compared to wild-type. Lower specificity constant for galactose than wild-type enzyme
L139P
a loss of stability and function is predicted by molecular docking and simulation modeling
L231S
catalyzes less efficiently the phosphorylation of galactose than the wild-type enzyme. Reduced turnover and decreased catalytic efficiency with the substrates 2-deoxy-D-galactose and ATP
M185L
statistically significantly increased catalytic turnover, with corresponding increases in the Michaelis constants for both substrates ATP and alpha-D-galactose. The specificity constants for galactose and ATP are not significantly changed. This variant is significantly less thermally stable than the wild-type protein and is less resistant to denaturation by urea
M60V/M180V
modest, but significant, increase in the melting temperature compared to the wild type, but no change in the turnover number
M60V/M180V/A334S
none of the steady state kinetic parameters is significantly altered. The variant has significantly increased thermal stability
M60V/M180V/A334S/D268E/G373S
increase in thermal stability, but no significant change in the kinetic parameters
M60V/M180V/A334S/G373S
increase in thermal stability, but no significant change in the kinetic parameters
M60V/M180V/D268E/A334S/R366Q/G373S
mutant enzyme with increased thermal stability and increased turnover towards some substrates. The conformation of the protein is altered at key sites. The number of salt bridges and hydrogen bonds is increased. More stable towards denaturation by urea
P28T
Q242S
the turnover number and the catalytic efficiency with ATP (cosubstrate 2-deoxy-D-galactose) are increased. Inactive with D-galactosamine. Turnover number is significantly increased
R228M
interaction with both ATP and galactose is affected. The variant is significantly less stable than the wild-type protein
R256W
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drastic reduction of activity when expressed in COS cells, missense mutation causes GALK deficiency
T288M
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mutant enzyme is not present in the soluble fraction after sonication and can not be purified
T344M
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drastic reduction of activity when expressed in COS cells, missense mutation causes GALK deficiency
D186A
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residue D186 interacts with galactose, possible catalytic residue, no activity of mutant enzyme
D186E
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residue D186 interacts with galactose, possible catalytic residue, no activity of mutant enzyme
D186N
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residue D186 interacts with galactose, possible catalytic residue, no activity of mutant enzyme
D62A
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abolishes all detectable galactokinase activity but retains the ability to use D-glucose as a substrate
D62F
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abolishes all detectable galactokinase activity but retains the ability to use D-glucose as a substrate
D62H
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abolishes all detectable galactokinase activity but retains the ability to use D-glucose as a substrate
D62L
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abolishes all detectable galactokinase activity but retains the ability to use D-glucose as a substrate
D62A
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abolishes all detectable galactokinase activity but retains the ability to use D-glucose as a substrate
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additional information
A198V
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GALK variant associated with an A198V mutation in three infants with mild GALK deficiency. Km-values from healthy and mutant individuals are similar. The variant A198V probably originates in Japanese and Korean ancestors and is one of the genetic factors that cause cataract in elderly individuals
A198V
a loss of stability and function is predicted by molecular docking and simulation modeling
G349S
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lower specificity constant for galactose than wild-type enzyme. Lower specificity constant for galactose than wild-type enzyme
G349S
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drastic reduction of activity when expressed in COS cells, missense mutation causes GALK deficiency
P28T
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mutant enzyme is not present in the soluble fraction after sonication and can not be purified
P28T
a loss of stability and function is predicted by molecular docking and simulation modeling
additional information
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all exchanges for D37 are detrimental to the enzyme
additional information
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the two deletions, of 410delG and 509-510delGT , occur at the nucleotide repeats GGGGGG and GTGTGT, respectively and result in in-frame nonsense codons at amino acids 163 and 201. These mutations arise by slipped strand mispairing
additional information
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enzyme deletion mutant, strain shows reduced growth on D-galactose but is only slightly affected in growth on lactose. In mutant strain, induction of D-galactose-1-phosphate uridylyltransferase by D-galactose, but not by L-arabinose, is impaired
