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Literature summary extracted from

  • Boehlein, S.K.; Shaw, J.R.; Stewart, J.D.; Hannah, L.C.
    Characterization of an autonomously activated plant adenosine diphosphate glucose pyrophosphorylase (2008), Plant Physiol., 149, 318-326.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.7.27 3-phosphoglycerate activation of mutant Mos(1-198) is reduced compared to the wild-type enzyme, overview Zea mays
2.7.7.27 ADP-D-glucose activation of mutant Mos(1-198) is reduced compared to the wild-type enzyme, overview Solanum tuberosum
2.7.7.27 additional information mutant Mos(1-198) naturally occurs in a semiactivated state in the absence of an activator Zea mays
2.7.7.27 additional information mutant Mos(1-198) naturally occurs in a semiactivated state in the absence of an activator Solanum tuberosum

Protein Variants

EC Number Protein Variants Comment Organism
2.7.7.27 F332S site-directed mutagenesis in the potato part of the chimeric mutant Zea mays
2.7.7.27 F332S site-directed mutagenesis in the potato part of the chimeric mutant Solanum tuberosum
2.7.7.27 H341Y site-directed mutagenesis in the potato part of the chimeric mutant Zea mays
2.7.7.27 H341Y site-directed mutagenesis in the potato part of the chimeric mutant Solanum tuberosum
2.7.7.27 I323V site-directed mutagenesis in the potato part of the chimeric mutant Zea mays
2.7.7.27 I323V site-directed mutagenesis in the potato part of the chimeric mutant Solanum tuberosum
2.7.7.27 additional information expression of the maize/potato small subunit mosaic mutant MP, Mos(1-198), containing the first 198 amino acids of the small subunit of the maize endosperm enzyme and the last 277 amino acids from the potato tuber enzyme, Mos(1-198) and its derivatives are expressed exclusively with the wild-type maize large subunit, SH2. In the absence of activator, performs like a wild-type AGPase that is partially activated with 3-phosphoglycerate, enzymatic activity in the absence of 3-phosphoglycerate is substantially 2-5fold higher than that of wild-type enzyme, while in presence of 3-phosphoglycerate, Mos(1-198) AGPase activity is actually less than that of wild-type enzyme, phenotype, mutant Mos(1-198) naturally occurs in a semiactivated state in the absence of an activator, overview. Mutational exchange of carboxylterminal region containing 15 polymorphic amino acids from 377 to 475 to create Mos(1-198, 430-475) and Mos(1-198, 377-429) leading to reduced enzyme activity independent of 3-phosphoglycerate. Constructed mutant Mos(1-277) exhibits 3-phosphoglycerate-independent activity that is less than mutant Mos(1-198) and wild-type activity. Mutant Mos(1-321) has no detectible activity in the absence of 3-phosphoglycerate. In the presence of 3-phosphoglycerate however, Mos(1-321) activity in the reverse direction is identical to that of Mos(1-277), overview Zea mays
2.7.7.27 additional information expression of the maize/potato small subunit mosaic mutant MP, Mos(1-198), containing the first 198 amino acids of the small subunit of the maize endosperm enzyme and the last 277 amino acids from the potato tuber enzyme, Mos(1-198) and its derivatives are expressed exclusively with the wt maize large subunit, SH2. In the absence of activator, performs like a wild-type AGPase that is partially activated with ADP-D-glucose, enzymatic activity in the absence of 3-phosphoglycerate is substantially 2-5fold higher than that of wild-type enzyme, while in presence of 3-phosphoglycerate, Mos(1-198) AGPase activity is actually less than that of wild-type enzyme, phenotype, mutant Mos(1-198) naturally occurs in a semiactivated state in the absence of an activator, overview. Mutational exchange of carboxylterminal region containing 15 polymorphic amino acids from 377 to 475 to create Mos(1-198, 430-475) and Mos(1-198, 377-429) leading to reduced enzyme activity independent of 3-phosphoglycerate. Constructed mutant Mos(1-277) exhibits 3-phosphoglycerate-independent activity that is less than mutant Mos(1-198) and wild-type activity. Mutant Mos(1-321) has no detectible activity in the absence of 3-phosphoglycerate. In the presence of 3-phosphoglycerate however, Mos(1-321) activity in the reverse direction is identical to that of Mos(1-277), overview Solanum tuberosum
2.7.7.27 N369H site-directed mutagenesis in the potato part of the chimeric mutant Zea mays
2.7.7.27 N369H site-directed mutagenesis in the potato part of the chimeric mutant Solanum tuberosum
2.7.7.27 V347M site-directed mutagenesis in the potato part of the chimeric mutant Zea mays
2.7.7.27 V347M site-directed mutagenesis in the potato part of the chimeric mutant Solanum tuberosum

General Stability

EC Number General Stability Organism
2.7.7.27 bovine serum albumin stabilizes the purified enzyme at 0.5 mg/ml Zea mays
2.7.7.27 bovine serum albumin stabilizes the purified enzyme at 0.5 mg/ml Solanum tuberosum

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.7.27 phosphate 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 Solanum tuberosum
2.7.7.27 phosphate 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 Zea mays

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.7.27 0.018
-
 ATP pH 7.4, 37°C, mutant Mos(1-198), in absence of 3-phosphoglycerate Zea mays
2.7.7.27 0.018
-
 ATP pH 7.4, 37°C, mutant Mos(1-198), in absence of 3-phosphoglycerate Solanum tuberosum
2.7.7.27 0.039
-
 ATP pH 7.4, 37°C, mutant Mos(1-198, 430-475), in absence of 3-phosphoglycerate Zea mays
2.7.7.27 0.039
-
 ATP pH 7.4, 37°C, mutant Mos(1-198, 430-475), in absence of 3-phosphoglycerate Solanum tuberosum
2.7.7.27 0.04
-
 ATP pH 7.4, 37°C, mutant Mos(1-198, 377-429), in absence of 3-phosphoglycerate Zea mays
2.7.7.27 0.04
-
 ATP pH 7.4, 37°C, mutant Mos(1-198, 377-429), in absence of 3-phosphoglycerate Solanum tuberosum
2.7.7.27 0.04
-
 ATP pH 7.4, 37°C, mutant Mos(1-376), in absence of 3-phosphoglycerate Zea mays
2.7.7.27 0.04
-
 ATP pH 7.4, 37°C, mutant Mos(1-376), in absence of 3-phosphoglycerate Solanum tuberosum
2.7.7.27 0.044
-
 ATP pH 7.4, 37°C, mutant Mos(1-277), in absence of 3-phosphoglycerate Zea mays
2.7.7.27 0.044
-
 ATP pH 7.4, 37°C, mutant Mos(1-277), in absence of 3-phosphoglycerate Solanum tuberosum
2.7.7.27 0.051
-
 ATP pH 7.4, 37°C, mutant Mos(1-198), in presence of 3-phosphoglycerate Zea mays
2.7.7.27 0.051
-
 ATP pH 7.4, 37°C, mutant Mos(1-198), in presence of 3-phosphoglycerate Solanum tuberosum
2.7.7.27 0.056
-
 ATP pH 7.4, 37°C, mutant Mos(1-198, 377-475), in absence of 3-phosphoglycerate Zea mays
2.7.7.27 0.056
-
 ATP pH 7.4, 37°C, mutant Mos(1-198, 377-475), in absence of 3-phosphoglycerate Solanum tuberosum
2.7.7.27 0.074
-
 ATP pH 7.4, 37°C, wild-type enzyme, in presence of 3-phosphoglycerate Zea mays
2.7.7.27 0.074
-
 ATP pH 7.4, 37°C, wild-type enzyme, in presence of 3-phosphoglycerate Solanum tuberosum
2.7.7.27 0.075
-
 ATP pH 7.4, 37°C, wild-type enzyme, in absence of 3-phosphoglycerate Zea mays
2.7.7.27 0.075
-
 ATP pH 7.4, 37°C, wild-type enzyme, in absence of 3-phosphoglycerate Solanum tuberosum

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.7.27 Mg2+
-
 Zea mays
2.7.7.27 Mg2+
-
 Solanum tuberosum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.27 ATP + alpha-D-glucose 1-phosphate Zea mays
-
 ADP-D-glucose + diphosphate
-
 r
2.7.7.27 ATP + alpha-D-glucose 1-phosphate Solanum tuberosum
-
 ADP-D-glucose + diphosphate
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.27 Solanum tuberosum
-
-
-
2.7.7.27 Zea mays
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.27 recombinant wild-type and mutant AGPases using protamine sulfate and ammonium sulfate fractionation, followed by ion exchange and hydroxyapatite chromatography Zea mays
2.7.7.27 recombinant wild-type and mutant AGPases using protamine sulfate and ammonium sulfate fractionation, followed by ion exchange and hydroxyapatite chromatography Solanum tuberosum

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.7.27 leaf
-
 Zea mays
-
2.7.7.27 leaf
-
 Solanum tuberosum
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7.7.27 0.72
-
 purified mutant Mos(1-198, 377-475) in absence of 3-phosphoglycerate Zea mays
2.7.7.27 0.72
-
 purified mutant Mos(1-198, 377-475) in absence of 3-phosphoglycerate Solanum tuberosum
2.7.7.27 1.47
-
 purified mutant Mos(1-376) in absence of 3-phosphoglycerate Zea mays
2.7.7.27 1.47
-
 purified mutant Mos(1-376) in absence of 3-phosphoglycerate Solanum tuberosum
2.7.7.27 1.68
-
 purified mutant Mos(1-198, 430-475) in absence of 3-phosphoglycerate Zea mays
2.7.7.27 1.68
-
 purified mutant Mos(1-198, 430-475) in absence of 3-phosphoglycerate Solanum tuberosum
2.7.7.27 1.78
-
 purified mutant Mos(1-198, 377-429) in absence of 3-phosphoglycerate Zea mays
2.7.7.27 1.78
-
 purified mutant Mos(1-198, 377-429) in absence of 3-phosphoglycerate Solanum tuberosum
2.7.7.27 1.8
-
 purified mutant Mos(1-277) in absence of 3-phosphoglycerate Zea mays
2.7.7.27 1.8
-
 purified mutant Mos(1-277) in absence of 3-phosphoglycerate Solanum tuberosum
2.7.7.27 2.45
-
 purified wild-type enzyme, in absence of 3-phosphoglycerate Zea mays
2.7.7.27 2.45
-
 purified wild-type enzyme, in absence of 3-phosphoglycerate Solanum tuberosum
2.7.7.27 4.87
-
 purified mutant Mos(1-198) in absence of 3-phosphoglycerate Zea mays
2.7.7.27 4.87
-
 purified mutant Mos(1-198) in absence of 3-phosphoglycerate Solanum tuberosum
2.7.7.27 6.14
-
 purified mutant Mos(1-198, 430-475) in presence of 3-phosphoglycerate Zea mays
2.7.7.27 6.14
-
 purified mutant Mos(1-198, 430-475) in presence of 3-phosphoglycerate Solanum tuberosum
2.7.7.27 6.81
-
 purified mutant Mos(1-198, 377-429) in presence of 3-phosphoglycerate Zea mays
2.7.7.27 6.81
-
 purified mutant Mos(1-198, 377-429) in presence of 3-phosphoglycerate Solanum tuberosum
2.7.7.27 7.29
-
 purified mutant Mos(1-277) in presence of 3-phosphoglycerate Zea mays
2.7.7.27 7.29
-
 purified mutant Mos(1-277) in presence of 3-phosphoglycerate Solanum tuberosum
2.7.7.27 8.59
-
 purified mutant Mos(1-198, 377-475) in presence of 3-phosphoglycerate Zea mays
2.7.7.27 8.59
-
 purified mutant Mos(1-198, 377-475) in presence of 3-phosphoglycerate Solanum tuberosum
2.7.7.27 9.38
-
 purified mutant Mos(1-376) in presence of 3-phosphoglycerate Zea mays
2.7.7.27 9.38
-
 purified mutant Mos(1-376) in presence of 3-phosphoglycerate Solanum tuberosum
2.7.7.27 10.87
-
 purified mutant Mos(1-198) in presence of 3-phosphoglycerate Zea mays
2.7.7.27 10.87
-
 purified mutant Mos(1-198) in presence of 3-phosphoglycerate Solanum tuberosum
2.7.7.27 21.81
-
 purified wild-type enzyme in presence of 3-phosphoglycerate Zea mays
2.7.7.27 21.81
-
 purified wild-type enzyme in presence of 3-phosphoglycerate Solanum tuberosum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.27 ATP + alpha-D-glucose 1-phosphate
-
 Zea mays ADP-D-glucose + diphosphate
-
 r
2.7.7.27 ATP + alpha-D-glucose 1-phosphate
-
 Solanum tuberosum ADP-D-glucose + diphosphate
-
 r
2.7.7.27 ATP + alpha-D-glucose 1-phosphate substrate binding structure and kinetics, regulation of wild-type and mutant enzymes, mapping the polymorphic sites important in altered allosteric properties, overview Zea mays ADP-D-glucose + diphosphate
-
 r
2.7.7.27 ATP + alpha-D-glucose 1-phosphate substrate binding structure and kinetics, regulation of wild-type and mutant enzymes, mapping the polymorphic sites important in altered allosteric properties, overview Solanum tuberosum ADP-D-glucose + diphosphate
-
 r

Synonyms

EC Number Synonyms Comment Organism
2.7.7.27 adenosine diphosphate glucose pyrophosphorylase
-
 Zea mays
2.7.7.27 adenosine diphosphate glucose pyrophosphorylase
-
 Solanum tuberosum
2.7.7.27 ADP-glucose pyrophosphorylase
-
 Zea mays
2.7.7.27 ADP-glucose pyrophosphorylase
-
 Solanum tuberosum
2.7.7.27 AGPase
-
 Zea mays
2.7.7.27 AGPase
-
 Solanum tuberosum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.7.27 37
-
 assay at Zea mays
2.7.7.27 37
-
 assay at Solanum tuberosum

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.7.7.27 42
-
 wild-type AGPAse in the absence of 3-phosphoglycerate has a half-life of 1 min, whereas mutant Mos(1-198) has a half-life of 5.5 min, when 3-phosphoglycerate is added to the wid-type enzyme, the half-life increases to 5.5 min and the half-life of the mutant is incrwased to 9.4 min Zea mays
2.7.7.27 42
-
 wild-type AGPAse in the absence of 3-phosphoglycerate has a half-life of 1 min, whereas mutant Mos(1-198) has a half-life of 5.5 min, when 3-phosphoglycerate is added to the wid-type enzyme, the half-life increases to 5.5 min and the half-life of the mutant is incrwased to 9.4 min Solanum tuberosum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.7.27 7.4
-
 assay at Zea mays
2.7.7.27 7.4
-
 assay at Solanum tuberosum

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.7.7.27 1
-
 phosphate the phosphate inhibition pattern of Mos(1-198) is complex and biphasic. Inhibition at relatively high phopshate concentrations is less than predicted at low phosphate concentrations, the calculated Ki for phosphate is about 1 mM before 50% inhibition and 36 mM after 50% inhibition. Inhibition kinetics of mutants in presence and absence of 3-phosphoglycerate Solanum tuberosum
2.7.7.27 1
-
 phosphate the phosphate inhibition pattern of Mos(1-198) is complex and biphasic. Inhibition at relatively high phosphate concentrations is less than predicted at low phosphate concentrations, the calculated Ki for phosphate is about1 mM before 50% inhibition and 36 mM after 50% inhibition. Inhibition kinetics of mutants in presence and absence of 3-phosphoglycerate Zea mays
2.7.7.27 1.4
-
 phosphate wild-type enzyme, in presence of 3-phosphoglycerate Zea mays
2.7.7.27 1.4
-
 phosphate wild-type enzyme, in presence of 3-phosphoglycerate Solanum tuberosum
2.7.7.27 8.7
-
 phosphate mutant Mos(1-198), in presence of 3-phosphoglycerate Zea mays
2.7.7.27 8.7
-
 phosphate mutant Mos(1-198), in presence of 3-phosphoglycerate Solanum tuberosum