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
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endosperm
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potato
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grain
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maize
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glycogen
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tuber
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wheat
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3-phosphoglycerate
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tuberosum
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sink
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amylose
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plastid
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solanum
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invertase
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granule-bound
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heterotetrameric
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kernel
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plastidial
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ppases
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amylopectin
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orthophosphate
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sh2
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phosphoglucomutase
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debranching
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amyloplasts
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grain-filling
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waxy
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starchless
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source-sink
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biotechnology
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anthesis
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agriculture
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endosperm-specific
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spikelets
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synthesis
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isoamylase
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pyrophosphorolysis
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fructose-1,6-bisphosphate
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photosynthate
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photoassimilate
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pullulanase
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starch-branching
- 2.7.7.27
- starch
- endosperm
- potato
- grain
- maize
- glycogen
- tuber
- wheat
- 3-phosphoglycerate
- tuberosum
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sink
- amylose
- plastid
- solanum
- invertase
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granule-bound
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heterotetrameric
- kernel
- plastidial
- ppases
- amylopectin
- orthophosphate
- sh2
- phosphoglucomutase
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debranching
- amyloplasts
-
grain-filling
-
waxy
-
starchless
-
source-sink
- biotechnology
-
anthesis
- agriculture
-
endosperm-specific
-
spikelets
- synthesis
- isoamylase
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pyrophosphorolysis
- fructose-1,6-bisphosphate
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photosynthate
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photoassimilate
- pullulanase
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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 (Inhibitors
Inhibitors on EC 2.7.7.27 - glucose-1-phosphate adenylyltransferase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
3-phosphoglycerate
inhibits at higher concentrations; inhibits at higher concentrations; inhibits at higher concentrations; inhibits at higher concentrations; inhibits at higher concentrations; inhibits at higher concentrations
8-azaADP-glucose
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photoinactivation, competitive inhibition, ADP-glucose and ATP protects
8-azaATP
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photoinactivation, competitive inhibition, 0.5 mol/mol enzyme subunit for complete inactivation, ADP-glucose and ATP protects
ADP-glucose
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in the presence of 3-phosphoglycerate, ADP-glucose is a competitve inhibitor with respect to ATP
D-fructose 6-phosphate
only endosperm enzyme is inhibited, activation of leaf enzyme
DTT
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3-phosphoglycerate protects completely when added before the inhibition, but does not affect the enzyme activity after inhibition by DTT takes place
sulfate
is a competitive inhibitor for the allosteric activator fructose 6-phosphate, binds to the interface between the N- and C-terminal domains, binding structure, modelling
ADP
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most effective, fructose 6-phosphate or fructose 1,6-bisphosphate partially reverses
ADP
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inhibition under activated and unactivated conditions
ADP
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less effective than AMP; phosphoenolpyruvate, fructose bisphosphate, pyridoxal phosphate, NADPH, 3-phosphoglycerate, fructose 6-phosphate or pyruvate does not reverse
ADP
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allosteric inhibitor; glycolytic metabolites do not affect inhibition; less effective than AMP; not
ADP-alpha-D-glucose
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in wild-type, competitive with ATP, noncompetitive with glucose 1-phosphate. In chimeric mutant, competitive with ATP, mixed type inhibition with glucose 1-phosphate
ADP-alpha-D-glucose
in wild-type, competitive with ATP, noncompetitive with glucose 1-phosphate. In chimeric mutant, competitive with ATP, mixed type inhibition with glucose 1-phosphate
AMP
AMP activation at pH 7, AMP acting as a competitive ligand for an allosteric site at pH 8 where both activators and inhibitors bind and mediate their effect
AMP
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the most potent inhibitor, inhibition under activated and unactivated conditions
AMP
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allosteric inhibitor; kinetics; not; pyruvate modulates the sensitivity of enzyme to AMP inhibition
AMP
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the most potent inhibitor, inhibition under activated and unactivated conditions
AMP
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allosteric inhibitor; kinetics; not
AMP
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allosteric inhibitor; kinetics; not; wild-type and mutant enzymes
AMP
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allosteric inhibitor; glycolytic metabolites do not affect inhibition; kinetics; not; wild-type and mutant enzymes
diphosphate
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in wild-type, mixed type inhibition with ATP, competitive with glucose 1-phosphate. In chimeric mutant, mixed type inhibition with ATP, competitive with glucose 1-phosphate
diphosphate
in wild-type, mixed type inhibition with ATP, competitive with glucose 1-phosphate. In chimeric mutant, mixed type inhibition with ATP, competitive with glucose 1-phosphate
dithiothreitol
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in presence of 3-phophoglycerate, decrease of acitivity
dithiothreitol
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inhibition is prevented by pre- or by coincubation with 3-phophoglycerate, but incubation of already inhibited enzyme with 3-phophoglycerate may not reverse the inhibition
dithiothreitol
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in presence of 3-phophoglycerate, decrease of acitivity for enzyme from tuber
inorganic phosphate
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inhibitor in the absence of 3-phosphoglycerate and high substrate levels
phosphate
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effect of temperature on the activity of enzyme in the presence of phosphate
phosphate
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the inhibitory action of phosphate interferes with the activating role exerted by 3-phosphoglycerate, a 2fold higher positive cooperation is induced by allosteric inhibitor in crowded medium in comparison to the aqueous condition
phosphate
kinetic study and comparison of activation of recombinant enzymes, the inhibition is more drastic for recombinant enzyme APS1/APL1; kinetic study and comparison of activation of recombinant enzymes, the inhibition is more drastic for recombinant enzyme APS1/APL1; kinetic study and comparison of activation of recombinant enzymes, the inhibition is more drastic for recombinant enzyme APS1/APL1; kinetic study and comparison of activation of recombinant enzymes, the inhibition is more drastic for recombinant enzyme APS1/APL1; kinetic study and comparison of activation of recombinant enzymes, the inhibition is more drastic for recombinant enzyme APS1/APL1
phosphate
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wild-type, 50% inhibition at 0.044 mM, mutant A33K, 50% inhibition at 0.043 mM, mutant G96N, 50% inhibition at 0.054 mM, mutant A33K/G96N, 50% inhibition at 0.268 mM, all in presence of 3-phosphoglycerate in at concentration of halfmaximal activation
phosphate
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allosteric inhibitor; kinetics; plants, algae, cyanobacteriae
phosphate
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allosteric inhibitor; kinetics; most effective, fructose 6-phosphate reverses
phosphate
the presence of 2.5 mM D-fructose 6-phosphate completely prevents phosphate inhibition, in the presence of 1 mM phosphate, inhibition by phosphoenolpyruvate drops to 50%
phosphate
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allosteric inhibitor; kinetics; plants, algae, cyanobacteriae
phosphate
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inhibition under activated and unactivated conditions
phosphate
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allosteric inhibitor; kinetics
phosphate
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allosteric inhibitor; kinetics; plants, algae, cyanobacteriae
phosphate
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at 0.5 mM 3-phosphoglycerate, 50% inhibition of wild-type at 0.54 mM, of mutation P52L, large subunit, at 0.52 mM, of mutation P52L, large subunit, plus mutation L46F, small subunit at 0.61 mM, of mutation P52L, large subunit, plus mutation P112L, small subunit at 0.43 mM, of mutation P52L, large subunit, plus mutation P308L, small subunit at 2.5 mM, of mutation P52L, large subunit, plus mutation R350K, small subunit at 1.9 mM
phosphate
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mutant Mos(1-198) is significantly inhibited in the absence of 3-phosphoglycerate even at low phosphate concentrations. Inhibition levels of wild-type and deletion mutants by phosphate, overview
phosphate
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3-phosphoglycerate reverses, increasing concentration of Mg2+ does not overcome the inhibition; kinetics
phosphate
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allosteric inhibitor; kinetics; plants, algae, cyanobacteriae
phosphate
phosphate inhibits leaf and endosperm enzymes, 3-phosphoglycerate and D-fructose 6-phosphate reverse endosperm inhibition
phosphate
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plastidial isoform of endosperm not sensitive at physiological concentrations of phosphate
phosphate
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allosteric inhibitor; kinetics; plants, algae, cyanobacteriae
phosphate
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phosphate binds tightly to the endosperm AGPase, but does not inhibit catalytic activity, it acts by displacing bound activators and returning the enzyme to its activity in their absence. Phosphate, in the absence of 3-PGA, also stabilizes maize endosperm AGPase
phosphate
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mutant Mos(1-198) is significantly inhibited in the absence of 3-phosphoglycerate even at low Pi concentrations. Inhibition levels of wild-type and deletion mutants by phosphate, overview
phosphoenolpyruvate
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most effective in vitro, D-fructose 6-phosphate protects
phosphoenolpyruvate
in the presence of 1 mM phosphate, inhibition by the 1 mM phosphoenolpyruvate drops to 50%, inhibition is reduced to 20% in the presence of 0.15 mM fructose 6-phosphate
phosphoenolpyruvate
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most effective in vitro, D-fructose 6-phosphate protects
phosphoenolpyruvate
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most effective in vitro, D-fructose 6-phosphate protects
phosphoenolpyruvate
M9TIK1; M9TG57
inhibitory to GlgC/GlgD complex, inhibitory to subunit GlgC only in presence of fructose 1,6-bisphosphate
Rabbit antiserum raised against spinach enzyme
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not antiserum against E. coli enzyme
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Rabbit antiserum raised against spinach enzyme
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not antiserum against E. coli enzyme
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Rabbit antiserum raised against spinach enzyme
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not antiserum against E. coli enzyme
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additional information
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activator/inhibitor interaction in vivo and in vitro
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additional information
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no inhibition by trehalose, trehalose diphosphate, fructose 6-phosphate, ribose 5-phosphate or 3-phosphoglyceraldehyde
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