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ATP + 5-ethyl-L-glutamate
?
ATP + 5-methyl-L-glutamate
?
ATP + cis-cycloglutamate
ADP + cis-cycloglutamyl phosphate
ATP + glutaric acid
?
29% activity compared to L-glutamate
-
-
?
ATP + L-glutamate
ADP + L-glutamate 5-phosphate
GTP + L-glutamate
GDP + L-glutamate 5-phosphate
additional information
?
-
ATP + 5-ethyl-L-glutamate
?
-
5% of the activity with L-glutamate
-
-
?
ATP + 5-ethyl-L-glutamate
?
-
5% of the activity with L-glutamate
-
-
?
ATP + 5-methyl-L-glutamate
?
-
6% of the activity with L-glutamate
-
-
?
ATP + 5-methyl-L-glutamate
?
-
6% of the activity with L-glutamate
-
-
?
ATP + cis-cycloglutamate
ADP + cis-cycloglutamyl phosphate
-
no reaction with trans-cycloglutamate
-
?
ATP + cis-cycloglutamate
ADP + cis-cycloglutamyl phosphate
-
no reaction with trans-cycloglutamate
-
?
ATP + L-glutamate
ADP + L-glutamate 5-phosphate
-
-
-
?
ATP + L-glutamate
ADP + L-glutamate 5-phosphate
-
-
-
?
ATP + L-glutamate
ADP + L-glutamate 5-phosphate
-
-
-
-
?
ATP + L-glutamate
ADP + L-glutamate 5-phosphate
-
-
-
-
?
ATP + L-glutamate
ADP + L-glutamate 5-phosphate
-
-
-
?
ATP + L-glutamate
ADP + L-glutamate 5-phosphate
-
the enzyme catalyzes the first step in the pathway from glutamate to proline
-
-
?
ATP + L-glutamate
ADP + L-glutamate 5-phosphate
-
enzyme is involved in biosynthesis of proline
-
-
?
ATP + L-glutamate
ADP + L-glutamate 5-phosphate
-
enzyme catalyzes the first step of proline biosynthesis
-
-
?
ATP + L-glutamate
ADP + L-glutamate 5-phosphate
AAK domain is responsible for catalysis
-
-
?
ATP + L-glutamate
ADP + L-glutamate 5-phosphate
-
-
-
-
?
ATP + L-glutamate
ADP + L-glutamate 5-phosphate
-
the enzyme catalyzes the first step in the pathway from glutamate to proline
-
-
?
ATP + L-glutamate
ADP + L-glutamate 5-phosphate
-
-
-
?
ATP + L-glutamate
ADP + L-glutamate 5-phosphate
100% activity
-
-
?
ATP + L-glutamate
ADP + L-glutamate 5-phosphate
-
-
-
-
?
ATP + L-glutamate
ADP + L-glutamate 5-phosphate
-
-
-
?
ATP + L-glutamate
ADP + L-glutamate 5-phosphate
-
-
-
?
ATP + L-glutamate
ADP + L-glutamate 5-phosphate
-
-
-
-
?
ATP + L-glutamate
ADP + L-glutamate 5-phosphate
-
-
-
-
?
ATP + L-glutamate
ADP + L-glutamate 5-phosphate
-
-
-
-
?
ATP + L-glutamate
ADP + L-glutamate 5-phosphate
-
-
-
?
ATP + L-glutamate
ADP + L-glutamate 5-phosphate
-
-
-
-
?
ATP + L-glutamate
ADP + L-glutamate 5-phosphate
-
-
-
?
ATP + L-glutamate
ADP + L-glutamate 5-phosphate
-
-
-
-
?
ATP + L-glutamate
ADP + L-glutamate 5-phosphate
-
-
-
-
?
ATP + L-glutamate
ADP + L-glutamate 5-phosphate
-
-
-
-
?
ATP + L-glutamate
ADP + L-glutamate 5-phosphate
-
-
-
-
?
ATP + L-glutamate
ADP + L-glutamate 5-phosphate
-
enzyme GK 1 is the first enzyme of the proline biosynthetic pathway
-
-
?
ATP + L-glutamate
ADP + L-glutamate 5-phosphate
-
enzyme form GK1 is involved in biosynthesis of L-Pro, enzyme form GK 2 is involved in biosynthesis of glutamine and the function of enzyme form GK 3 has not been found
-
-
?
ATP + L-glutamine
?
-
10% of the activity with L-glutamate
-
-
?
ATP + L-glutamine
?
-
10% of the activity with L-glutamate
-
-
?
GTP + L-glutamate
GDP + L-glutamate 5-phosphate
-
10% of the activity with ATP
-
-
?
GTP + L-glutamate
GDP + L-glutamate 5-phosphate
-
10% of the activity with ATP
-
-
?
additional information
?
-
GTP, CTP or UTP do not replace ATP as phosphate donor. The enzyme has no activity with aminovaleric acid and 2-amino-4-phosphonobutyric acid
-
-
-
additional information
?
-
-
GTP, CTP or UTP do not replace ATP as phosphate donor. The enzyme has no activity with aminovaleric acid and 2-amino-4-phosphonobutyric acid
-
-
-
additional information
?
-
-
relation of glutamate kinase activity to cadmium and zinc concentration in the above-ground biomass, regulatory role in plant heavy metal stress adaptation
-
-
?
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3,4-dehydro-L-proline
9% residual activity at 1 mM
5-oxo-L-Pro
-
12 mM, 10% inhibition
5-oxoproline
AAK domain has a crater on the beta sheet C-edge that hosts the active centre and binds 5-oxoproline
alpha-methyl-L-proline
82% residual activity at 1 mM
-
As2+
-
applied into soil strongly decreases activity by 87.7%
DL-3,4-Didehydroproline
-
9 mM, 50% inhibition
Hg2+
-
0.1 mM, complete inhibition
iodoacetamide
-
0.125 mM, 60% inhibition. Preincubation with 0.25 mM dithiothreitol for 5 min partially protects
L-4-thioproline
66% residual activity at 1 mM
-
L-azetidine-2-carboxylic acid
L-methionine-DL-sulphoximine
-
competitive with L-glutamate
L-Orn
-
12 mM, 10% inhibition
L-prolinamide
96% residual activity at 1 mM
L-Thioproline
-
12 mM, 10% inhibition
L-trans-pyrrolidine-2,4-dicarboxylic acid
84% residual activity at 1 mM
-
N-acetyl-L-proline
93% residual activity at 1 mM
-
NEM
-
0.125 mM, complete inhibition. Preincubation with 0.25 mM dithiothreitol for 5 min partially protects
PCMB
-
0.125 mM, complete inhibition. Preincubation with 0.25 mM dithiothreitol for 5 min partially protects
trans-4-hydroxy-L-proline
ADP
-
-
Cd2+
-
0.1 mM, complete inhibition
Cd2+
-
applied into soil strongly decreases activity
Cd2+
-
increased content in soil decreases enzyme activity
cis-4-hydroxy-L-proline
87% residual activity at 1 mM
cis-4-hydroxy-L-proline
-
-
L-azetidine-2-carboxylic acid
25% residual activity at 1 mM
L-azetidine-2-carboxylic acid
-
3 mM, 50% inhibition
L-Pro
-
enzyme from strain PAO1: 5 mM, 50% inhibition, complete inhibition at 30 mM, noncompetitive. Strain PAO 879, a proline-auxotroph mutant lacks a proline-inhibitable gamma-glutamyl kinase
L-Pro
-
IC50: 0.08 mM, at room temperature. At low temperatures the inhibition switches over into allosteric activation and the biosynthesis of proline is started
L-Pro
-
feedback-inhibition
L-proline
completely inhibits the activity of wild-type gamma-glutamyl kinase/gamma-glutamyl phosphate reductase at concentrations greater than 0.1mM, and inhibits it by 30% at 0.01mM
L-proline
-
results indicate that the sensitivity of Chlamydomonas glutamte kinase to feedback inhibition by L-proline is much lower than that of similar microbial glutamte kinase
L-proline
AAK domain is responsible for inhibition
L-proline
4% residual activity at 1 mM
L-proline
feedback inhibitor
L-proline
GK activity is subject to feedback inhibition by proline
L-proline
feedback inhibition
L-proline
-
free proline decreases activity, allosteric regulation
Mg2+
-
trans-4-hydroxy-L-proline
89% residual activity at 1 mM
trans-4-hydroxy-L-proline
-
-
Zn2+
-
applied into soil strongly decreases activity
Zn2+
-
increased content in soil decreases enzyme activity
additional information
L-pipecolinic acid, D-pipecolinic acid, N-methyl-L-proline, cis-3-hydroxy-L-proline, trans-1-acetyl-4-hydroxy-L-proline, D-proline as well as L-citrulline and D,L-ornithine at 1 mM concentration do not inhibit the enzymatic conversion of L-glutamate
-
additional information
-
L-pipecolinic acid, D-pipecolinic acid, N-methyl-L-proline, cis-3-hydroxy-L-proline, trans-1-acetyl-4-hydroxy-L-proline, D-proline as well as L-citrulline and D,L-ornithine at 1 mM concentration do not inhibit the enzymatic conversion of L-glutamate
-
additional information
no significant differences in growth between mutant yeast cells on SD agar medium with heat shock (50°C, 3 to 5 h), ethanol (16 to20%), and sorbitol (2.0 to 2.5 M) stresses, although the proline-accumulating cells are more resistant to these stresses than cells expressing wild-type GK
-
additional information
-
no significant differences in growth between mutant yeast cells on SD agar medium with heat shock (50°C, 3 to 5 h), ethanol (16 to20%), and sorbitol (2.0 to 2.5 M) stresses, although the proline-accumulating cells are more resistant to these stresses than cells expressing wild-type GK
-
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0.49
3,4-dehydro-L-proline
Leishmania donovani
at pH 7.4 and 25°C
1.8
L-4-thioproline
Leishmania donovani
at pH 7.4 and 25°C
-
0.73
L-azetidine-2-carboxylic acid
Leishmania donovani
at pH 7.4 and 25°C
0.08
L-Pro
Triticum aestivum
-
IC50: 0.08 mM, at room temperature. At low temperatures the inhibition switches over into allosteric activation and the biosynthesis of proline is started
0.011
L-proline
Escherichia coli
mutant T169A
0.016
L-proline
Escherichia coli
mutant K217A
0.02
L-proline
Escherichia coli
mutant K217R
0.021
L-proline
Escherichia coli
mutant T169S
0.05
L-proline
Escherichia coli
-
mutant Q100A, pH not specified in the publication, 37°C
0.05
L-proline
Escherichia coli
-
mutant Q80A, pH not specified in the publication, 37°C
0.14
L-proline
Escherichia coli
-
mutant E135A, pH not specified in the publication, 37°C
0.15
L-proline
Escherichia coli
wild-type
0.15
L-proline
Escherichia coli
-
wild-type, pH not specified in the publication, 37°C
0.165
L-proline
Escherichia coli
mutant M214A
0.17
L-proline
Escherichia coli
mutant D170A
0.176
L-proline
Escherichia coli
mutant D150N
0.18
L-proline
Escherichia coli
-
mutant R25S/E30K,I193A, pH not specified in the publication, 37°C
0.22
L-proline
Escherichia coli
mutant D170N
0.26
L-proline
Escherichia coli
mutant K10A
0.39
L-proline
Leishmania donovani
at pH 7.4 and 25°C
0.5
L-proline
Saccharomyces cerevisiae
wild-type
0.5
L-proline
Escherichia coli
-
mutant S50A, pH not specified in the publication, 37°C
0.51
L-proline
Escherichia coli
mutant G51A
1.2
L-proline
Escherichia coli
-
mutant I53A, pH not specified in the publication, 37°C
1.3
L-proline
Escherichia coli
-
mutant K145A, pH not specified in the publication, 37°C
2.16
L-proline
Escherichia coli
mutant N149A
5.7
L-proline
Escherichia coli
-
mutant E143A, pH not specified in the publication, 37°C
5.9
L-proline
Escherichia coli
mutant D148N
6.1
L-proline
Escherichia coli
-
mutant D107A, pH not specified in the publication, 37°C
9.4
L-proline
Escherichia coli
-
mutant R118A, pH not specified in the publication, 37°C
11.5
L-proline
Escherichia coli
-
mutant N134D, pH not specified in the publication, 37°C
21
L-proline
Escherichia coli
mutant D148A
21.4
L-proline
Escherichia coli
-
mutant D137A, pH not specified in the publication, 37°C
26
L-proline
Escherichia coli
-
mutant I69E, pH not specified in the publication, 37°C
32
L-proline
Saccharomyces cerevisiae
mutant D154N
50
L-proline
Saccharomyces cerevisiae
mutant I150T
54
L-proline
Saccharomyces cerevisiae
mutant N142D/I166V
90
L-proline
Chlamydomonas reinhardtii
-
pH 7.0, 37°C
96
L-proline
Escherichia coli
-
mutant E143A/K145A, pH not specified in the publication, 37°C
840
L-proline
Saccharomyces cerevisiae
mutant E149K
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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
D170A
activity is less than 1% of that of wild-type G5K
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
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
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
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
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
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
N177D
mutant of the proBA fusion gene, improves the osmotolerance of host cells of Escherichia coli JM83, leads to overproduction of proline by host cells, is about 100fold less sensitive to proline-mediated feedback inhibition than the control
N177D
-
mutant of the proBA fusion gene, improves the osmotolerance of host cells of Escherichia coli JM83, leads to overproduction of proline by host cells, is about 100fold less sensitive to proline-mediated feedback inhibition than the control
-
A226S
the mutant has 1.2fold increased activity and higher thermostability compared to the wild type enzyme
A226S
-
the mutant has 1.2fold increased activity and higher thermostability compared to the wild type enzyme
-
D154N
the mutation results in a prominant increase in cell viability after freezing at -20°C compared to the viability of the cells harboring the wild-type PRO1 gene. The altered gamma-glutamyl kinase results in stabilization of the complex with gamma-glutamyl phosphate reductase or has an indirect effect on gamma-glutamyl phosphate reductase activity which leads to an increase in L-proline production in Saccharomyces cerevisiae
D154N
is 64fold less sensitive to feedback inhibition than wild-type GK, leading to proline accumulation
D154N
site-directed mutagenesis, the mutant enzyme is less sensitive to proline feedback inhibition compared to the wild-type enzyme and shows an increased thermostability
I150T
very insensitive to feedback inhibition, shows prominent increase in the proline content, is more tolerant to freezing stress than cells expressing the D154N mutant
I150T
site-directed mutagenesis, the mutant enzyme is less sensitive to proline feedback inhibition compared to the wild-type enzyme and shows an increased thermostability
I150T
the mutant is greatly insensitive to feedback inhibition, leading to L-proline overproduction. The relative activity of the variant is 59% in the presence of 100 mM L-proline. The specific activity of the variant is slightly reduced compared with the wild type enzyme
I149F
-
drastic reduction in specific activity. 222.2fold increase in Ki-value for L-Pro compared to wild-type enzyme
I149F
-
222.2fold increase in Ki-value for L-Pro compared to wild-type enzyme
additional information
-
2-amino-acid insertion (Val and Asn) in front of Glu143: insertion mutant exhibits a dramatic reduction in catalytic ability (the velocity at infinite concentration of substrates is 5% relative to wild-type), IC50 (L-proline) is enhanced compared to wild-type
additional information
-
truncated yeast gamma-glutamyl kinase proteins are engineered from which the C-terminal region is deleted. A complementation test in Escherichia coli and yeast and enzymatic analysis of recombinant proteins reveal that a 67-residue linker sequence between a 255-residue kinase domain and a 106-residue archaeosine transglycosylase (PUA) domain is essential for gamma-glutamyl kinase activity. 67 or more residues of the C-terminal region, not the PUA domain itself, are required for the full enzymatic activity
additional information
construction of a gene PRO1 disruption mutant, phenotype, detailed overview. Overexpression of wild-type enzyme partially suppresses the phenotype of the DELTApro1 strain, which is deficient in ribophagy
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Hayzer, D.J.; Moses, V.
The enzymes of proline biosynthesis in Escherichia coli. Their molecular weights and the problem of enzyme aggregation
Biochem. J.
173
219-228
1978
Escherichia coli
brenda
Garcia-Rios, M; Fujita, T.; Larosa, P.C.; Locy, R.D.; Clitero, J.M.; Bressan, R.A.; Csonka, L.N.
Cloning of a polycistronic cDNA from tomato encoding gamma-glutamyl kinase and gamma-glutamyl phosphate reductase
Proc. Natl. Acad. Sci. USA
94
8249-8254
1997
Solanum lycopersicum
brenda
Yaklichkin, S.Y.; Zimina, M.S.; Neumyvakin, L.V.
Proline biosynthesis gene proB of thermophilic Bacterium Thermus ruber: cloning, sequencing, and properties of encoded gamma-glutamylphosphate kinase
Mol. Biol.
33
628-635
1999
Meiothermus ruber
-
brenda
Meijer, P.J.; Lilius, G.; Holmberg, N.; Bulow, L
An artificial bifunctional enzyme, gamma-glutamyl kinase/gamma-glutamyl phosphate reductase, improves NaCl tolerance when expressed in Escherichia Coli
Biotechnol. Lett.
18
1133-1138
1996
Escherichia coli
-
brenda
Massarelli, I.; Forlani, G.; Ricca, E.; De Felice, M.
Enhanced and feedback-resistant gamma-glutamyl kinase activity of an Escherichia coli transformant carrying a mutated proB gene of Streptococcus thermophilus
FEMS Microbiol. Lett.
182
143-147
2000
Streptococcus thermophilus
brenda
Smith, C.J.; Deutch, A.H.; Rushlow, K.E.
Purification and characteristics of a gamma-glutamyl kinase involved in Escherichia coli proline biosynthesis
J. Bacteriol.
157
545-551
1984
Escherichia coli
brenda
Seddon, A.P.; Zhao, K.Y.; Meister, A.
Activation of glutamate by gamma-glutamate kinase: formation of gamma-cis-cycloglutamyl phosphate, an analog of gamma-glutamyl phosphate
J. Biol. Chem.
264
11326-11335
1989
Escherichia coli, Escherichia coli CM 25
brenda
Krishna, R.V.; Leisinger, T.
Biosynthesis of proline in Pseudomonas aeruginosa. Partial purification and characterization of gamma-glutamyl kinase
Biochem. J.
181
215-222
1979
Pseudomonas aeruginosa, Pseudomonas aeruginosa PAO 1
brenda
Vasakova, L.; Stefl, M.
Glutamate kinases from winter-wheat leaves and some properties of the proline-inhibitable glutamate kinase
Collect. Czech. Chem. Commun.
47
349-359
1982
Triticum aestivum
-
brenda
Stefl, M.; Vasakova, L.
Allosteric regulation of proline-inhibitable glutamate kinase from winter-wheat leaves by L-proline, adenosine diphosphate and low temperature
Collect. Czech. Chem. Commun.
47
360-369
1982
Triticum aestivum
-
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Stefl, M.; Vasakova, L.
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