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2.7.2.11: glutamate 5-kinase

This is an abbreviated version!
For detailed information about glutamate 5-kinase, go to the full flat file.

Word Map on EC 2.7.2.11

Reaction

ATP
+
L-glutamate
=
ADP
 +
L-glutamate 5-phosphate

Synonyms

ATP-L-glutamate 5-phosphotransferase, ATP:gamma-L-glutamate phosphotransferase, G5K, gamma-GK, gamma-glutamate kinase, gamma-glutamyl kinase, gamma-glutamylphosphate kinase, GK, GKA, glutamate kinase, glutamate-5-kinase, GPK, kinase (phosphorylating), glutamate, kinase, glutamate (phosphorylating), PRO1, proB, scGK

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.2 Phosphotransferases with a carboxy group as acceptor
                2.7.2.11 glutamate 5-kinase

Engineering

Engineering on EC 2.7.2.11 - glutamate 5-kinase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N177D
D107A
-
mutant shows 40fold increased IC50 (L-proline)
D137A
-
mutation hampers proline binding and glutamate binding, IC50 (L-proline) 142fold increased compared to wild-type
D148A
is active, 150fold increased proline requirement
D148N
is active, 40fold increased proline requirement
D150A
is not active
D150N
is active
D170A
activity is less than 1% of that of wild-type G5K
D170N
is active
E135A
-
mutation of Glu135 and Lys145 only produce relatively small changes in proline activity, IC50 (L-proline) comparable to wild-type
E143A
-
mutant shows an 38fold augmented IC0.5 (L-proline) while kinetic parameters of glutamate and ATP are scarcely changed, IC50 (L-proline) 38fold increased compared to wild-type
E143A/K145A
-
mutant shows an enhanced affinity for L-glutamate and increased IC50 (L-proline) compared to wild-type
G51A
is active
I53A
-
decreased kinetic parameters, IC50 (L-proline) increased 5fold compared to wild-type
I69E
-
mutation produces a very strong (170fold) decrease on proline activity with no other consequence on the kinetic parameters of the enzyme
K10A
activity is less than 1% of that of wild-type G5K
K145A
-
mutant shows an enhanced affinity for L-glutamate and increased IC50 (L-proline) compared to wild-type
K217A
activity is less than 1% of that of wild-type G5K, decreased proline requirement
K217R
is active, decreased proline requirement
M214A
is active
N134D
-
mutation hampers proline binding and glutamate binding, IC50 (L-proline) 76fold increased compared to wild-type
N149A
activity is less than 1% of that of wild-type G5K, 14fold increased proline requirement
Q100A
-
mutant shows drastically reduced catalytic rate and reduced affinity for glutamate, IC50 (L-proline) 3fold decreased compared to wild-type
Q80A
-
mutant shows drastically reduced catalytic rate and reduced affinity for glutamate, IC50 (L-proline) 3fold decreased compared to wild-type
R118A
-
mutant shows increased affinity for glutamate and reduced L-proline affinity (63fold increased IC50)
R25S/E30K/I193A
-
mutant behaves as a dimer in gel filtration experiments, kinetically indistinguishable from wild-type, IC50 (L-proline) comparable to wild-type
S50A
-
mutant exhibits a greatly reduced catalytic rate but has a small effect on apparent affinities for glutamate or ATP, IC50 (L-proline) 3fold increased compared to wild-type
T169A
is active, decreased proline requirement
T169S
is active, decreased proline requirement
A226S
D154N
D156A
site-directed mutagenesis, inactive mutant
E149K
very insensitive to feedback inhibition, shows prominent increase in the proline content, freeze tolerance like the D154N mutant
I150T
N142D/I166V
very insensitive to feedback inhibition, shows prominent increase in the proline content, is more tolerant to freezing stress than cells expressing the D154N mutant
Q79H
the mutation results in extreme desensitization to feedback inhibition by L-proline, leading to L-proline overproduction. The relative activity of the variant is 96% in the presence of 100 mM L-proline and 87% in the presence of 400 mM L-proline. The specific activity of the variant is slightly reduced compared with the wild type enzyme
S146P
shows prominent increase in the proline content
A62T
-
drastic reduction in specific activity. 911fold increase in Ki-value for L-Pro compared to wild-type enzyme
A62V
-
drastic reduction in specific activity. 188fold increase in Ki-value for L-Pro compared to wild-type enzyme
D147G
-
reduction in catalytic activity. 2000fold increase in Ki-value for L-Pro compared to wild-type enzyme
D162G
-
drastic reduction in specific activity. 611.1fold increase in Ki-value for L-Pro compared to wild-type enzyme
D162N
-
drastic reduction in specific activity. 644fold increase in Ki-value for L-Pro compared to wild-type enzyme
E153A
-
reduction in catalytic activity. 555.5fold increase in Ki-value for L-Pro compared to wild-type enzyme
E153G
-
reduction in catalytic activity. 555.5fold increase in Ki-value for L-Pro compared to wild-type enzyme
E153K
-
reduction in catalytic activity. 3444.4fold increase in Ki-value for L-Pro compared to wild-type enzyme
I149F
I79T
-
reduction in catalytic activity. 21.1fold increase in Ki-value for L-Pro compared to wild-type enzyme
L154S
-
reduction in catalytic activity. 1000fold increase in Ki-value for L-Pro compared to wild-type enzyme
M94T
-
reduction in catalytic activity. 255.6fold increase in Ki-value for L-Pro compared to wild-type enzyme
S159P
-
reduction in catalytic activity. 211.1fold increase in Ki-value for L-Pro compared to wild-type enzyme
D192G
-
the mutation causes an enhanced feedback-resistant gamma-glutamyl kinase activity and conferrs an analogue-resistant phenotype to an Escherichia coli transformant containing the mutated gene
additional information