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Literature summary for 2.7.7.27 extracted from

  • Boehlein, S.K.; Sewell, A.K.; Cross, J.; Stewart, J.D.; Hannah, L.C.
    Purification and characterization of adenosine diphosphate glucose pyrophosphorylase from maize/potato mosaics (2005), Plant Physiol., 138, 1552-1562.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.7.27

Activating Compound

Activating Compound Comment Organism Structure
3-phosphoglycerate 10 mM, 16fold stimulation, enzyme from maize endosperm Zea mays
D-fructose 25 mM, 1.3fold stimulation, enzyme from maize endosperm Zea mays
D-fructose 6-phosphate 25 mM, 15fold stimulation, enzyme from maize endosperm Zea mays
D-glucose 6-phosphate 25 mM, 12fold stimulation, enzyme from maize endosperm Zea mays

Cloned(Commentary)

Cloned (Comment) Organism
mosaic AGPases derived from protein motifs normally expressed in the Zea mays endosperm and the Solanum tuberosum tuber, expression in Escherichia coli Zea mays
mosaic AGPases derived from protein motifs normally expressed in the Zea mays endosperm and the Solanum tuberosum tuber, expression in Escherichia coli Solanum tuberosum

Protein Variants

Protein Variants Comment Organism
additional information mosaic AGPases derived from protein motifs normally expressed in the Zea mays endosperm and the Solanum tuberosum tuber. Km for ATP and alpha-D-glucose 1-phosphate do not differ significantly for the mosaic enzymes in the presence of 3-phosphoglycerate. 2fold increase in Km for ATP when the potato small subunit is combined with the maize large subunit (Pss/Mls). Interestingly, the turnover number is increased for all mosaics Zea mays
additional information mosaic AGPases derived from protein motifs normally expressed in the Zea mays endosperm and the Solanum tuberosum tuber. Km for ATP and alpha-D-glucose 1-phosphate do not differ significantly for the mosaic enzymes in the presence of 3-phosphoglycerate. 2fold increase in Km for ATP when the potato small subunit is combined with the maize large subunit (Pss/Mls). Interestingly, the turnover number is increased for all mosaics Solanum tuberosum

Inhibitors

Inhibitors Comment Organism Structure
phosphate
-
 Zea mays

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information KM-values for mosaic AGPases derived from protein motifs normally expressed in the Zea mays endosperm and the Solanum tuberosum tuber Zea mays
additional information
-
 additional information KM-values for mosaic AGPases derived from protein motifs normally expressed in the Zea mays endosperm and the Solanum tuberosum tuber Solanum tuberosum
0.06
-
 alpha-D-glucose 1-phosphate pH 7.4, 37°C, enzyme from Zea mays endosperm Zea mays
0.12
-
 ATP pH 7.4, 37°C, enzyme from Zea mays endosperm Zea mays

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + alpha-D-glucose 1-phosphate Zea mays rate-limiting step in starch biosynthesis diphosphate + ADP-glucose
-
 ?
ATP + alpha-D-glucose 1-phosphate Solanum tuberosum rate-limiting step in starch biosynthesis diphosphate + ADP-glucose
-
 ?

Organism

Organism UniProt Comment Textmining
Solanum tuberosum
-
-
-
Zea mays
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant mosaic AGPases derived from protein motifs normally expressed in the Zea mays endosperm and the Solanum tuberosum tuber Zea mays
recombinant mosaic AGPases derived from protein motifs normally expressed in the Zea mays endosperm and the Solanum tuberosum tuber Solanum tuberosum

Source Tissue

Source Tissue Comment Organism Textmining
endosperm
-
 Zea mays
-
tuber
-
 Solanum tuberosum
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
41.1
-
 recombinant enzyme from maize endosperm Zea mays

Storage Stability

Storage Stability Organism
-80°C, majority of activity is retained for several months, mosaic AGPases derived from protein motifs normally expressed in the Zea mays endosperm and the Solanum tuberosum tuber Solanum tuberosum
-80°C, majority of activity is retained for several months, recombinant enzyme from maize and mosaic AGPases derived from protein motifs normally expressed in the Zea mays endosperm and the Solanum tuberosum tuber Zea mays

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + alpha-D-glucose 1-phosphate
-
 Zea mays diphosphate + ADP-glucose
-
 ?
ATP + alpha-D-glucose 1-phosphate
-
 Solanum tuberosum diphosphate + ADP-glucose
-
 ?
ATP + alpha-D-glucose 1-phosphate rate-limiting step in starch biosynthesis Zea mays diphosphate + ADP-glucose
-
 ?
ATP + alpha-D-glucose 1-phosphate rate-limiting step in starch biosynthesis Solanum tuberosum diphosphate + ADP-glucose
-
 ?

Synonyms

Synonyms Comment Organism
adenosine diphosphate glucose pyrophosphorylase
-
 Zea mays
adenosine diphosphate glucose pyrophosphorylase
-
 Solanum tuberosum
AGPase
-
 Zea mays
AGPase
-
 Solanum tuberosum

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information turnover numbers for mosaic AGPases derived from protein motifs normally expressed in the Zea mays endosperm and the Solanum tuberosum tuber Zea mays
additional information
-
 additional information turnover numbers for mosaic AGPases derived from protein motifs normally expressed in the Zea mays endosperm and the Solanum tuberosum tuber Solanum tuberosum
85
-
 alpha-D-glucose 1-phosphate pH 7.4, 37°C, enzyme from Zea mays endosperm Zea mays
98
-
 ATP pH 7.4, 37°C, enzyme from Zea mays endosperm Zea mays

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.96
-
 phosphate pH 7.4, 37°C, enzyme from maize endosperm Zea mays