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2.7.1.147: ADP-specific glucose/glucosamine kinase

This is an abbreviated version!
For detailed information about ADP-specific glucose/glucosamine kinase, go to the full flat file.

Word Map on EC 2.7.1.147

Reaction

ADP
+
D-glucosamine
=
AMP
 +
D-glucosamine 6-phosphate

Synonyms

ADP-dependent glucokinase, ADP-dependent hexokinase, ADP-dependent kinase, ADP-GK, ADP-HK, ADP-Pfk, ADP-specific glucokinase, ADP:D-glucose 6-phosphotransferase, ADPGK, ancGK/PFK, AncMsPFK/GK, bifunctional ADP-dependent phosphofructokinase/glucokinase, GlcN kinase, glucosamine kinase, MevePFK/GK, MjPFK/GK, MmazPFK/GK, MmPFK/GK, More, NagC4, pfGK, pfkC, PhPFK, TK1110, tlGK

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.1 Phosphotransferases with an alcohol group as acceptor
                2.7.1.147 ADP-specific glucose/glucosamine kinase

Engineering

Engineering on EC 2.7.1.147 - ADP-specific glucose/glucosamine kinase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D481A
greatly reduced activity
D481E
greatly reduced activity
D481N
greatly reduced activity
D84A
greatly reduced activity
H264A
greatly reduced activity, no substrate inhibition with glucose concentrations of up to 55 mM
H382A
no catalytic activity
H382V/H387V
no catalytic activity
H387A
no catalytic activity
R228A
greatly reduced activity
C174S
site-directed mutagenesis, activity and oligomarization state are similar to the wild-type enzyme
C94S
site-directed mutagenesis, activity is similar to the wild-type enzyme, the mutant enzyme forms no dimers, but monomers
C94S/C174S
site-directed mutagenesis, activity is similar to the wild-type enzyme, the mutant enzyme forms no dimers, but monomers
D451A
site-directed mutagenesis, nearly inactive mutant
D451N
site-directed mutagenesis, nearly inactive mutant
D451S
site-directed mutagenesis, nearly inactive mutant
E279D
mutation does not affect the KM value for MgADP-, but causes a large increase on KM value for glucose and an 87fold weaker binding of glucose onto the non-hydrolysable enzyme-AMP-AlF3 complex. Mutant is still inhibited by free Mg2+
E279L
mutation does not affect the KM value for MgADP-, but causes a large increase on KM value for glucose and an 87fold weaker binding of glucose onto the non-hydrolysable enzyme-AMP-AlF3 complex. Mutant is still inhibited by free Mg2+
E279Q
mutation does not affect the KM value for MgADP-, but causes a large increase on KM value for glucose and an 87fold weaker binding of glucose onto the non-hydrolysable enzyme-AMP-AlF3 complex. Mutant is still inhibited by free Mg2+
E308Q
mutation increases the KM value for MgADP-, mutant is activated by free Mg2+
E279D
-
mutation does not affect the KM value for MgADP-, but causes a large increase on KM value for glucose and an 87fold weaker binding of glucose onto the non-hydrolysable enzyme-AMP-AlF3 complex. Mutant is still inhibited by free Mg2+
-
E279L
-
mutation does not affect the KM value for MgADP-, but causes a large increase on KM value for glucose and an 87fold weaker binding of glucose onto the non-hydrolysable enzyme-AMP-AlF3 complex. Mutant is still inhibited by free Mg2+
-
E279Q
-
mutation does not affect the KM value for MgADP-, but causes a large increase on KM value for glucose and an 87fold weaker binding of glucose onto the non-hydrolysable enzyme-AMP-AlF3 complex. Mutant is still inhibited by free Mg2+
-
E308Q
-
mutation increases the KM value for MgADP-, mutant is activated by free Mg2+
-
E72A
-
site-directed mutagenesis, the mutant shows reduced glucokinase and phosphofructokinase activities compared to wild-type enzyme