2.7.7.27: glucose-1-phosphate adenylyltransferase
This is an abbreviated version!
For detailed information about glucose-1-phosphate adenylyltransferase, go to the full flat file.
Word Map on EC 2.7.7.27
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2.7.7.27
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starch
-
endosperm
-
potato
-
grain
-
maize
-
glycogen
-
tuber
-
wheat
-
3-phosphoglycerate
-
tuberosum
-
sink
-
amylose
-
plastid
-
solanum
-
invertase
-
granule-bound
-
heterotetrameric
-
kernel
-
plastidial
-
ppases
-
amylopectin
-
orthophosphate
-
sh2
-
phosphoglucomutase
-
debranching
-
amyloplasts
-
grain-filling
-
waxy
-
starchless
-
source-sink
-
biotechnology
-
anthesis
-
agriculture
-
endosperm-specific
-
spikelets
-
synthesis
-
isoamylase
-
pyrophosphorolysis
-
fructose-1,6-bisphosphate
-
photosynthate
-
photoassimilate
-
pullulanase
-
starch-branching
- 2.7.7.27
- starch
- endosperm
- potato
- grain
- maize
- glycogen
- tuber
- wheat
- 3-phosphoglycerate
- tuberosum
-
sink
- amylose
- plastid
- solanum
- invertase
-
granule-bound
-
heterotetrameric
- kernel
- plastidial
- ppases
- amylopectin
- orthophosphate
- sh2
- phosphoglucomutase
-
debranching
- amyloplasts
-
grain-filling
-
waxy
-
starchless
-
source-sink
- biotechnology
-
anthesis
- agriculture
-
endosperm-specific
-
spikelets
- synthesis
- isoamylase
-
pyrophosphorolysis
- fructose-1,6-bisphosphate
-
photosynthate
-
photoassimilate
- pullulanase
-
starch-branching
Reaction
Synonyms
adenosine 5'-diphosphate (ADP)-glucose pyrophosphorylase, adenosine 5'-diphosphate glucose pyrophosphorylase, adenosine diphosphate glucose pyrophosphorylase, adenosine diphosphoglucose pyrophosphorylase, adenosine-5'-diphosphoglucose pyrophosphorylase, adenylyltransferase, glucose 1-phosphate, ADG2, ADP glucose pyrophosphorylase, ADP-Glc PPase, ADP-Glc pyrophosphorylase, ADP-glucose pyrophosphorylase, ADP-glucose synthase, ADP-glucose synthetase, ADPG pyrophosphorylase, ADPGlc PPase, ADPglucose pyrophosphorylase, AGP, AGP-S, AGP1, AGP2, AGPase, AGPL2, AGPS, AGPS1, AGPS2b, APS1, Brittle-2, BT2, GlgC, GlgD, OtaL, OtaS, SH2, Shrunken-2
ECTree
2.7.7.27 glucose-1-phosphate adenylyltransferaseAdvanced search results
results (
results (KM Value
KM Value on EC 2.7.7.27 - glucose-1-phosphate adenylyltransferase
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KM VALUE [mM] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
0.45
ADP-glucose
pH 7.8, 37°C, heterotetramer comprised of large subunit isoform L1 and small subunit S
0.72
ADP-glucose
pH 7.8, 37°C, heterotetramer comprised of large subunit isoform L3 and small subunit S
0.017
alpha-D-glucose 1-phosphate
-
chimeric enzyme, pH 7.4, 37°C, presence of 3-phosphoglycerate
0.017
alpha-D-glucose 1-phosphate
chimeric enzyme, pH 7.4, 37°C, presence of 3-phosphoglycerate
0.018
alpha-D-glucose 1-phosphate
-
pH 7.6, 37°C, wild-type enzyme, comparison of Km of wild-type and mutant enzymes
0.019
alpha-D-glucose 1-phosphate
pH 7.9, APS1/APL1 in presence of 0.1 mM 3-phosphoglycerate
0.021
alpha-D-glucose 1-phosphate
pH 8, 37°C, in absence of fructose 6-phosphate
0.023
alpha-D-glucose 1-phosphate
-
wild-type, S0.5 value, Hill coefficient 1.4, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.031
alpha-D-glucose 1-phosphate
-
pH 7.3, 37°C, in presence of 1 mM 3-phosphoglycerate
0.038
alpha-D-glucose 1-phosphate
large subunit mutant Q96G/D161G/A443R, presence of 3-phosphoglycerate, 37°C, pH 7.4
0.039
alpha-D-glucose 1-phosphate
wild-type, presence of 3-phosphoglycerate, 37°C, pH 7.4
0.04
alpha-D-glucose 1-phosphate
-
wild-type, presence of 2 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.04
alpha-D-glucose 1-phosphate
wild-type, pH 7.4, 37°C, presence of 3-phosphoglycerate
0.05
alpha-D-glucose 1-phosphate
-
reduced wild-type, pH 7.4, 37°C, presence of 3-phosphoglycerate
0.052
alpha-D-glucose 1-phosphate
pH 7.9, APS1/APL3 in presence of 2 mM 3-phosphoglycerate
0.056
alpha-D-glucose 1-phosphate
pH 8, 37°C, in presence of fructose 6-phosphate
0.06
alpha-D-glucose 1-phosphate
pH 7.9, APS1/APL4 in presence of 1 mM 3-phosphoglycerate
0.06
alpha-D-glucose 1-phosphate
large subunit mutant D161G, presence of 3-phosphoglycerate, 37°C, pH 7.4
0.07
alpha-D-glucose 1-phosphate
hyperbolic behavior, Hill coefficient 1.3, presence of mannose 6-phosphate, pH 8.0, 37°C
0.07
alpha-D-glucose 1-phosphate
M9TIK1; M9TG57
S0.5 value, Hill coefficient 1.2, GlgC/GlgD complex, pH 8.0, 37°C
0.074
alpha-D-glucose 1-phosphate
large subunit mutant G101N, pH 7.5, 37°C
0.076
alpha-D-glucose 1-phosphate
pH 7.9, homotetramer APS1 in presence of 20 mM 3-phosphoglycerate
0.081
alpha-D-glucose 1-phosphate
large subunit mutant E38K/G101N, pH 7.5, 37°C
0.085
alpha-D-glucose 1-phosphate
pH 7.9, APS1/APL2 in presence of 4 mM 3-phosphoglycerate
0.086
alpha-D-glucose 1-phosphate
-
pH 7.4, 37°C, fruit enzyme, in presence of 3-phosphoglycerate
0.09
alpha-D-glucose 1-phosphate
hyperbolic behavior, Hill coefficient 1.1, presence of glucose 6-phosphate, pH 8.0, 37°C
0.1
alpha-D-glucose 1-phosphate
-
oxidized wild-type, pH 7.4, 37°C, presence of 3-phosphoglycerate
0.105
alpha-D-glucose 1-phosphate
-
pH 7.3, 37°C, in absence of 3-phosphoglycerate
0.11
alpha-D-glucose 1-phosphate
-
pH 8.0, in presence of 2.5 mM 3-phosphoglycerate
0.12
alpha-D-glucose 1-phosphate
-
mutant Q106A, S0.5 value, Hill coefficient 1.3, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.12
alpha-D-glucose 1-phosphate
-
mutant R107A, S0.5 value, Hill coefficient 1.0, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.13
alpha-D-glucose 1-phosphate
-
pH 8.4, 37°C, influence of activators on Km
0.13
alpha-D-glucose 1-phosphate
large subunit E370G/small subunit wild-type, pH 7.4, 37°C
0.143
alpha-D-glucose 1-phosphate
-
mutant R115A, S0.5 value, Hill coefficient 1.7, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.158
alpha-D-glucose 1-phosphate
heterodimer of small/large subunit, presence of ATPgammaS, pH 7.4, 25°C
0.16
alpha-D-glucose 1-phosphate
hyperbolic behavior, Hill coefficient 0.7, presence of fructose 6-phosphate, pH 8.0, 37°C
0.17
alpha-D-glucose 1-phosphate
-
pH 8.0, in presence of 5 mM 3-phosphoglycerate
0.17
alpha-D-glucose 1-phosphate
mutation K41R/T51K, large subunit, plus D143N, small subunit
0.17
alpha-D-glucose 1-phosphate
hyperbolic behavior, Hill coefficient 0.8, presence of phosphoenolpyruvate, pH 8.0, 37°C
0.17
alpha-D-glucose 1-phosphate
large subunit mutant E38K, pH 7.5, 37°C
0.17
alpha-D-glucose 1-phosphate
-
mutant P103A, S0.5 value, Hill coefficient 1.4, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.194
alpha-D-glucose 1-phosphate
heterodimer of small/large subunit, pH 7.4, 25°C
0.2
alpha-D-glucose 1-phosphate
-
pH 7.0, 37°C, strain AC70R1, kinetic study
0.21
alpha-D-glucose 1-phosphate
-
pH 8.4, 37°C, influence of activators on Km
0.21
alpha-D-glucose 1-phosphate
-
mutation P52L, large subunit, plus mutation P112L, small subunit, 37°C, pH 7.0
0.22
alpha-D-glucose 1-phosphate
-
pH 7.4, 37°C, leaf enzyme, in presence of 3-phosphoglycerate
0.22
alpha-D-glucose 1-phosphate
-
mutant P103A, S0.5 value, Hill coefficient 1.1, pH 8.0, 37°C
0.23
alpha-D-glucose 1-phosphate
-
S0.5 value, Hill coefficient 1.0, presence of 25 mM pyruvate and 0.01 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.25
alpha-D-glucose 1-phosphate
pH 7.5, 37°C, mutant TG-15, kinetic study
0.25
alpha-D-glucose 1-phosphate
-
mutant Q106A, S0.5 value, Hill coefficient 1.6, pH 8.0, 37°C
0.26
alpha-D-glucose 1-phosphate
-
mutant R107A, S0.5 value, Hill coefficient 0.9, pH 8.0, 37°C
0.27
alpha-D-glucose 1-phosphate
-
mutant Y114A, S0.5 value, Hill coefficient 0.2, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.28
alpha-D-glucose 1-phosphate
-
mutant R115A, S0.5 value, Hill coefficient 1.7, pH 8.0, 37°C
0.29
alpha-D-glucose 1-phosphate
pH 7.8, 37°C, heterotetramer comprised of large subunit isoform L1 and small subunit S
0.34
alpha-D-glucose 1-phosphate
-
mutant W113A, S0.5 value, Hill coefficient 1.3, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.36
alpha-D-glucose 1-phosphate
-
mutation P52L, large subunit, plus mutation L46F, small subunit, 37°C, pH 7.0
0.37
alpha-D-glucose 1-phosphate
-
wild-type, S0.5 value, Hill coefficient 1.5, pH 8.0, 37°C
0.38
alpha-D-glucose 1-phosphate
mutation K41R, large subunit, plus D143N, small subunit
0.39
alpha-D-glucose 1-phosphate
-
pH 8.0, 37°C, chimeric enzyme EA contains the N-terminus of Escherichia coli enzyme and the C-terminus of Agrobacterium tumefaciens enzyme
0.39
alpha-D-glucose 1-phosphate
-
pH 8.0, 37°C, chimeric enzyme EA contains the N-terminus of Escherichia coli enzyme and the C-terminus of Agrobacterium tumefaciens enzyme
0.39
alpha-D-glucose 1-phosphate
-
mutation P52L, large subunit, plus mutation P308L, small subunit, 37°C, pH 7.0
0.4
alpha-D-glucose 1-phosphate
hyperbolic behavior, Hill coefficient 0.6, presence of ribose 5-phosphate, pH 8.0, 37°C
0.41
alpha-D-glucose 1-phosphate
-
mutation P52L, large subunit, plus mutation R350K, small subunit, 37°C, pH 7.0
0.41
alpha-D-glucose 1-phosphate
-
mutant W113A, presence of 2 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.42
alpha-D-glucose 1-phosphate
-
mutation P52L, large subunit, 37°C, pH 7.0
0.43
alpha-D-glucose 1-phosphate
-
mutant Y114A, S0.5 value, Hill coefficient 0.3, pH 8.0, 37°C
0.46
alpha-D-glucose 1-phosphate
pH 7.8, 37°C, heterotetramer comprised of large subunit isoform L3 and small subunit S
0.46
alpha-D-glucose 1-phosphate
-
mutant W113A, S0.5 value, Hill coefficient 1.7, pH 8.0, 37°C
0.47
alpha-D-glucose 1-phosphate
-
mutant Q74A, presence of 2 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.57
alpha-D-glucose 1-phosphate
-
S0.5 value, Hill coefficient 1.0, presence of 25 mM pyruvate, pH 8.0, 37°C
0.72
alpha-D-glucose 1-phosphate
-
S0.5 value, large subunit mutant A171V with wild-type small subunit, 37°C, pH 7.0
0.77
alpha-D-glucose 1-phosphate
-
S0.5 value, Hill coefficient 1.0, presence of 0.01 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.92
alpha-D-glucose 1-phosphate
-
pH 8.0, 37°C, chimeric enzyme AE contains the N-terminus of Agrobacterium tumefaciens enzyme and the C-terminus of Escherichia coli enzyme
0.92
alpha-D-glucose 1-phosphate
-
pH 8.0, 37°C, chimeric enzyme AE contains the N-terminus of Agrobacterium tumefaciens enzyme and the C-terminus of Escherichia coli enzyme
0.95
alpha-D-glucose 1-phosphate
-
S0.5 value, Hill coefficient 1.1, pH 8.0, 37°C
1.01
alpha-D-glucose 1-phosphate
mutation T51K, large subunit, plus D143N, small subunit
1.32
alpha-D-glucose 1-phosphate
-
S0.5 value, wild-type small subunit alone, 37°C, pH 7.0
1.43
alpha-D-glucose 1-phosphate
-
S0.5 value, large subunit mutant T139I with wild-type small subunit, 37°C, pH 7.0
1.8
alpha-D-glucose 1-phosphate
hyperbolic behavior, Hill coefficient 0.9, pH 8.0, 37°C
1.81
alpha-D-glucose 1-phosphate
wild-type, pH 7.4, 37°C, presence of phosphate
2.04
alpha-D-glucose 1-phosphate
M9TIK1; M9TG57
S0.5 value, Hill coefficient 1.7, subunit GlgC in presence of fructose 1,6-bisphosphate, pH 8.0, 37°C
2.1
alpha-D-glucose 1-phosphate
pH 7.8, 37°C, large subunit isoform L3
3.44
alpha-D-glucose 1-phosphate
M9TIK1; M9TG57
S0.5 value, Hill coefficient 0.9, subunit GlgC, pH 8.0, 37°C
4.01
alpha-D-glucose 1-phosphate
-
oxidized wild-type, pH 7.4, 37°C, presence of phosphate
5.18
alpha-D-glucose 1-phosphate
-
reduced wild-type, pH 7.4, 37°C, presence of phosphate
6.79
alpha-D-glucose 1-phosphate
-
chimeric enzyme, pH 7.4, 37°C, presence of phosphate
6.79
alpha-D-glucose 1-phosphate
chimeric enzyme, pH 7.4, 37°C, presence of phosphate
6.8
alpha-D-glucose 1-phosphate
large subunit mutant D161G, 37°C, pH 7.4
8.74
alpha-D-glucose 1-phosphate
large subunit mutant Q96G/D161G/A443R, 37°C, pH 7.4
0.018
ATP
-
pH 7.4, 37°C, mutant Mos(1-198), in absence of 3-phosphoglycerate
0.039
ATP
-
pH 7.4, 37°C, mutant Mos(1-198, 430-475), in absence of 3-phosphoglycerate
0.039
ATP
-
pH 7.4, 37°C, mutant Mos(1-198, 430-475), in absence of 3-phosphoglycerate
0.04
ATP
-
pH 7.4, 37°C, mutant Mos(1-198, 377-429), in absence of 3-phosphoglycerate
0.04
ATP
-
pH 7.4, 37°C, mutant Mos(1-198, 377-429), in absence of 3-phosphoglycerate
0.04
ATP
-
pH 7.4, 37°C, mutant Mos(1-376), in absence of 3-phosphoglycerate
0.044
ATP
-
pH 7.4, 37°C, mutant Mos(1-277), in absence of 3-phosphoglycerate
0.044
ATP
large subunit mutant D161G, presence of 3-phosphoglycerate, 37°C, pH 7.4
0.051
ATP
-
pH 7.4, 37°C, mutant Mos(1-198), in presence of 3-phosphoglycerate
0.053
ATP
-
chimeric enzyme, pH 7.4, 37°C, presence of 3-0.040 phosphoglycerate
0.053
ATP
chimeric enzyme, pH 7.4, 37°C, presence of 3-phosphoglycerate
0.056
ATP
-
pH 7.4, 37°C, mutant Mos(1-198, 377-475), in absence of 3-phosphoglycerate
0.056
ATP
-
pH 7.4, 37°C, mutant Mos(1-198, 377-475), in absence of 3-phosphoglycerate
0.057
ATP
large subunit mutant Q96G/D161G/A443R, presence of 3-phosphoglycerate, 37°C, pH 7.4
0.067
ATP
pH 7.9, APS1/APL1 in presence of 0.1 mM 3-phosphoglycerate
0.074
ATP
-
pH 7.4, 37°C, wild-type enzyme, in presence of 3-phosphoglycerate
0.075
ATP
-
pH 7.4, 37°C, wild-type enzyme, in absence of 3-phosphoglycerate
0.094
ATP
pH 7.9, APS1/APL3 in presence of 2 mM 3-phosphoglycerate
0.118
ATP
pH 7.9, APS1/APL4 in presence of 1 mM 3-phosphoglycerate
0.12
ATP
-
pH 7.4, 37°C, fruit enzyme, in presence of 3-phosphoglycerate
0.13
ATP
-
oxidized wild-type, pH 7.4, 37°C, presence of 3-phosphoglycerate
0.15
ATP
hyperbolic behavior, Hill coefficient 1.3, presence of mannose 6-phosphate, pH 8.0, 37°C
0.155
ATP
-
pH 8.0, 37°C, chimeric enzyme EA contains the N-terminus of Escherichia coli enzyme and the C-terminus of Agrobacterium tumefaciens enzyme
0.155
ATP
-
pH 8.0, 37°C, chimeric enzyme EA contains the N-terminus of Escherichia coli enzyme and the C-terminus of Agrobacterium tumefaciens enzyme
0.162
ATP
-
pH 8.0, 37°C, chimeric enzyme AE contains the N-terminus of Agrobacterium tumefaciens enzyme and the C-terminus of Escherichia coli enzyme
0.162
ATP
-
pH 8.0, 37°C, chimeric enzyme AE contains the N-terminus of Agrobacterium tumefaciens enzyme and the C-terminus of Escherichia coli enzyme
0.17
ATP
-
wild-type, S0.5 value, Hill coefficient 2.0, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.22
ATP
pH 8, 37°C, enzyme modified for 30 min with 5 mM 2,3-butanedione
0.22
ATP
-
mutation P52L, large subunit, plus mutation P112L, small subunit, 37°C, pH 7.0
0.24
ATP
-
mutation P52L, large subunit, plus mutation L46F, small subunit, 37°C, pH 7.0
0.24
ATP
-
mutation P52L, large subunit, plus mutation P308L, small subunit, 37°C, pH 7.0
0.24
ATP
hyperbolic behavior, Hill coefficient 1.6, presence of glucose 6-phosphate, pH 8.0, 37°C
0.26
ATP
-
pH 7.6, 37°C, wild-type enzyme, comparison of Km of wild-type and mutant enzymes
0.29
ATP
-
mutation P52L, large subunit, plus mutation R350K, small subunit, 37°C, pH 7.0
0.32
ATP
-
wild-type, presence of 2 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.34
ATP
pH 7.8, 37°C, heterotetramer comprised of large subunit isoform L1 and small subunit S
0.35
ATP
mutation K41R/T51K, large subunit, plus D143N, small subunit
0.37
ATP
M9TIK1; M9TG57
S0.5 value, Hill coefficient 1.5, subunit GlgC in presence of fructose 1,6-bisphosphate, pH 8.0, 37°C
0.4
ATP
hyperbolic behavior, Hill coefficient 1.4, presence of phosphoenolpyruvate, pH 8.0, 37°C
0.42
ATP
pH 7.9, homotetramer APS1 in presence of 20 mM 3-phosphoglycerate
0.49
ATP
-
S0.5 value, large subunit mutant T139I with wild-type small subunit, 37°C, pH 7.0
0.5
ATP
pH 7.8, 37°C, heterotetramer comprised of large subunit isoform L3 and small subunit S
0.5
ATP
hyperbolic behavior, Hill coefficient 1.1, presence of fructose 6-phosphate, pH 8.0, 37°C
0.5
ATP
hyperbolic behavior, Hill coefficient 1.3, presence of ribose 5-phosphate, pH 8.0, 37°C
0.51
ATP
-
S0.5 value, large subunit mutant A171V with wild-type small subunit, 37°C, pH 7.0
0.57
ATP
pH 7.9, APS1/APL2 in presence of 4 mM 3-phosphoglycerate
0.81
ATP
-
mutant P103A, S0.5 value, Hill coefficient 1.5, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.99
ATP
-
S0.5 value, Hill coefficient 3.6, presence of 25 mM pyruvate and 0.01 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
1.3
ATP
-
mutant R115A, S0.5 value, Hill coefficient 1.7, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
1.63
ATP
-
mutant R107A, S0.5 value, Hill coefficient 2.3, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
1.67
ATP
-
S0.5 value, Hill coefficient 2.5, presence of 25 mM pyruvate, pH 8.0, 37°C
2
ATP
-
pH 8.0, 37°C, strain JP102, kinetic study
2.2
ATP
-
pH 7.0, 37°C, wild-type enzyme in the absence of fructose 1,6-bisphosphate, comparison of Km of wild-type and mutant enzymes in the presence and absence of fructose 1,6-bisphosphate
2.3
ATP
-
mutant Y114A, S0.5 value, Hill coefficient 1.9, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
2.4
ATP
-
pH 8.4, 37°C, influence of activators on Km
2.4
ATP
-
pH 8.0, 37°C, strain LT-2, kinetic study
2.5
ATP
-
mutant W113A, presence of 2 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
3.1
ATP
-
mutant W113A, S0.5 value, Hill coefficient 1.1, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
4.4
ATP
-
mutant Q106A, S0.5 value, Hill coefficient 1.2, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
5
ATP
-
S0.5 value, Hill coefficient 2.1, presence of 0.01 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
9.8
ATP
-
mutant Q74A, presence of 2 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.08
diphosphate
pH 7.8, 37°C, heterotetramer comprised of large subunit isoform L1 and small subunit S
0.12
diphosphate
pH 7.8, 37°C, heterotetramer comprised of large subunit isoform L3 and small subunit S
additional information
additional information
-
kinetic study
-
additional information
additional information
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kinetic study
-
additional information
additional information
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kinetic study
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
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additional information
additional information
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effect of activators on substrate kinetic parameters of bacterial enzymes
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additional information
additional information
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effect of activators on substrate kinetic parameters of bacterial enzymes
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additional information
additional information
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effect of activators on substrate kinetic parameters of bacterial enzymes
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additional information
additional information
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effect of activators on substrate kinetic parameters of bacterial enzymes
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additional information
additional information
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effect of activators on substrate kinetic parameters of bacterial enzymes
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additional information
additional information
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effect of activators on substrate kinetic parameters of bacterial enzymes
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additional information
additional information
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effect of activators on substrate kinetic parameters of bacterial enzymes
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additional information
additional information
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effect of activators on substrate kinetic parameters of bacterial enzymes
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additional information
additional information
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effect of activators on substrate kinetic parameters of bacterial enzymes
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additional information
additional information
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effect of activators on substrate kinetic parameters of bacterial enzymes
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additional information
additional information
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effect of activators on substrate kinetic parameters of bacterial enzymes
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additional information
additional information
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effect of activators on substrate kinetic parameters of bacterial enzymes
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additional information
additional information
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effect of activators on substrate kinetic parameters of bacterial enzymes
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additional information
additional information
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effect of activators on substrate kinetic parameters of bacterial enzymes
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additional information
additional information
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effect of activators on substrate kinetic parameters of bacterial enzymes
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additional information
additional information
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effect of activators on substrate kinetic parameters of bacterial enzymes
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additional information
additional information
Sorghum sp.
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effect of activators on substrate kinetic parameters of bacterial enzymes
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additional information
additional information
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effect of activators on substrate kinetic parameters of bacterial enzymes
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additional information
additional information
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effect of activators on substrate kinetic parameters of bacterial enzymes
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additional information
additional information
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effect of activators on substrate kinetic parameters of bacterial enzymes
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additional information
additional information
Escherichia aurescens
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effect of activators on substrate kinetic parameters of bacterial enzymes
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additional information
additional information
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effect of activators on substrate kinetic parameters of bacterial enzymes
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additional information
additional information
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effect of activators on substrate kinetic parameters of bacterial enzymes
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additional information
additional information
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effect of activators on substrate kinetic parameters of bacterial enzymes
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additional information
additional information
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effect of activators on substrate kinetic parameters of bacterial enzymes
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additional information
additional information
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effect of activators on substrate kinetic parameters of bacterial enzymes
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additional information
additional information
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effect of activators on substrate kinetic parameters of bacterial enzymes
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additional information
additional information
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comparison of Km of proteolyzed and non-proteolyzed enzyme at pH 7.4 and pH 6.8
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additional information
additional information
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comparison of Km of alpha-D-glucose 1-phosphate at different ATP concentrations, at two levels of 3-phosphoglycerate and in aqueous or by polyethylenglycol crowded medium, comparison of Km of ATP at different alpha-D-glucose 1-phosphate concentrations, at two levels of 3-phosphoglycerate and in aqueous or by polyethylenglycol crowded medium
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additional information
additional information
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the allosteric properties of Enterobacter hafniae are distinctly different from other bacteria of the genus Enterobacter
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additional information
additional information
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the allosteric properties of Enterobacter hafniae are distinctly different from other bacteria of the genus Enterobacter
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additional information
additional information
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KM-values for mosaic AGPases derived from protein motifs normally expressed in the Zea mays endosperm and the Solanum tuberosum tuber
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additional information
additional information
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KM-values for mosaic AGPases derived from protein motifs normally expressed in the Zea mays endosperm and the Solanum tuberosum tuber
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additional information
additional information
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kinetics of wild-type and mutant large subunits, overview
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additional information
additional information
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kinetics wild-type and mutant enzymes, photoaffinity labeling of the AGPase heterotetramers, overview
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additional information
additional information
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ordered kinetic mechanism, regulation of AGPase by effectors, detailed overview
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additional information
additional information
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recombinant wild-type and mutant AGPase kinetic and allosteric properties for the forward and reverse reaction directions, overview
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additional information
additional information
wild-type and ADPGlc PPase H379R and ADPGlc PPase H379K mutant kinetics, overview
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additional information
additional information
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wild-type and ADPGlc PPase H379R and ADPGlc PPase H379K mutant kinetics, overview
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additional information
additional information
wild-type and mutant kinetics, forward and reverse reaction directions
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additional information
additional information
wild-type and mutant kinetics, forward and reverse reaction directions
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additional information
additional information
wild-type and mutant kinetics, forward and reverse reaction directions
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additional information
additional information
wild-type and mutant kinetics, forward and reverse reaction directions
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additional information
additional information
wild-type and mutant kinetics, forward and reverse reaction directions
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