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2.7.4.8: guanylate kinase

This is an abbreviated version!
For detailed information about guanylate kinase, go to the full flat file.

Word Map on EC 2.7.4.8

Reaction

ATP
+
GMP
=
ADP
+
GDP

Synonyms

5'-GMP kinase, apo-EcGMPK, ATP: GMP phosphotransferase, ATP:GMP phosphotransferase, BmGK, CASK polypeptide, Cavbeta1b, Cavbeta2a, deoxyguanylate kinase, DLG1/SAP97, ecGMPK, GK, GK3, GKc, GKpm, GMK, GMK3, GMP kinase, GMPK, guanosine monophosphate kinase, guanosine monophosphate kinase (EcGMPK), guanylate kinase, guanylate kinase (GK), guanylate monophosphate kinase, GUK, kinase, guanylate (phosphorylating), MAGUK, MAGUK PSD-95, MAGUKs, membrane associated guanylate kinase, membrane associated guanylate kinase protein, membrane-associated guanylate kinase, membrane-associated guanylate kinases, MoGuk1, MoGuk2, More, organellar GK, post-synaptic density-95 membrane associated guanylate kinase, postsynaptic density protein-95 SH3 GK, PSD-95 GK, PSD-95 MAGUK, PSD-95alpha, PSD-95beta, Staphylococcus aureus guanylate monophosphate kinase, voltage-gated calcium channel beta1b, voltage-gated calcium channel beta2a, YGK

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.4 Phosphotransferases with a phosphate group as acceptor
                2.7.4.8 guanylate kinase

Engineering

Engineering on EC 2.7.4.8 - guanylate kinase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C3S/C5S
-
PSD-95aC3S/C5S mutant
G3A
decrease in Tm-value by 1.4°C as compared to wild-type enzyme. Decrease in catalytic efficiency (kcat/Km) by 14%
R116Q
decrease in Tm-value by 1.8°C as compared to wild-type enzyme. Decrease in catalytic efficiency (kcat/Km) by 18%
R96H
decrease in Tm-value by 4°C as compared to wild-type enzyme. Increase in catalytic efficiency (kcat/Km) by 22%
S121F
decrease in Tm-value by 3.6°C as compared to wild-type enzyme. Decrease in catalytic efficiency (kcat/Km) by 25%
S186Y
decrease in Tm-value by 2.8°C as compared to wild-type enzyme. Decrease in catalytic efficiency (kcat/Km) by 7%
S2L
decrease in Tm-value by 1.9°C as compared to wild-type enzyme. Decrease in catalytic efficiency (kcat/Km) by 11%
S35N/V168F
-
the mutations significantly suppress enzyme catalytic activity
V91M
decrease in Tm-value by 3°C as compared to wild-type enzyme. Decrease in catalytic efficiency (kcat/Km) by 14%
D103N
-
active
E72Q
-
no guanylate or adenylate kinase activity
E72Q/D103D
-
no active
D74A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E101D
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
N103D
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y76F
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
P564S/S631D
-
PSD-95 construct
S35P/D101S
-
reduced activity
S80A
-
sluggish enzyme
Y78F
-
affinity for MgATP2- similar to wild type but affinity for GMP decreases by a factor of 12
additional information