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2.7.4.26: isopentenyl phosphate kinase

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

Word Map on EC 2.7.4.26

Reaction

ATP
+
isopentenyl phosphate
=
ADP
 +
isopentenyl diphosphate

Synonyms

HvIpk, HVO_2762, IPK, Ipk2, isopentenyl phosphate kinase, MJ0044, MM_1763, Ta0103

ECTree

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

Engineering

Engineering on EC 2.7.4.26 - isopentenyl phosphate kinase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F83A/I86A/I156A
the mutant shows a 27% rate of conversion of (2E,6E)-farnesyl phosphate to (2E,6E)-farnesyl diphosphate. The reaction is not catalyzed by the wild-type enzyme
H60Q
His60 plays a key role in binding and catalysis, the mutant enzyme shows increased values for Km and decreased vaules for kcat and kcat/Km
F83A/I86A/I156A
-
the mutant shows a 27% rate of conversion of (2E,6E)-farnesyl phosphate to (2E,6E)-farnesyl diphosphate. The reaction is not catalyzed by the wild-type enzyme
-
H60Q
-
His60 plays a key role in binding and catalysis, the mutant enzyme shows increased values for Km and decreased vaules for kcat and kcat/Km
-
A53V
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, the mutant shows increased activity compared to the wild-type enzyme
G44A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
G45A
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
G49A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
I140V
site-directed mutagenesis, the mutant shows highly increased activity compared to the wild-type enzyme
K204A
K204G
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
V130A
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
V73I
site-directed mutagenesis, the mutant shows highly increased activity compared to the wild-type enzyme
V73I/K204G
site-directed mutagenesis, the mutant shows highly increased activity compared to the wild-type enzyme
V73I/Y141V
site-directed mutagenesis, the mutant shows highly increased activity compared to the wild-type enzyme
V73I/Y141V/K204G
site-directed mutagenesis, the mutant shows highly increased activity compared to the wild-type enzyme
V73T
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
Y141L
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
Y141V
site-directed mutagenesis, the mutant shows highly increased activity compared to the wild-type enzyme
Y141V/K204G
site-directed mutagenesis, the mutant shows highly increased activity compared to the wild-type enzyme
additional information